EC 1.1.1.144     Relevance: 100%
Accepted name: perillyl-alcohol dehydrogenase
Reaction: perillyl alcohol + NAD+ = perillyl aldehyde + NADH + H+
Other name(s): perillyl alcohol dehydrogenase
Systematic name: perillyl-alcohol:NAD+ oxidoreductase
Comments: Oxidizes a number of primary alcohols with the alcohol group allylic to an endocyclic double bond and a 6-membered ring, either aromatic or hydroaromatic.
References:
1.  Ballal, N.R., Bhattacharyya, P.K. and Rangachari, P.N. Perillyl alcohol dehydrogenase from a soil pseudomonad. Biochem. Biophys. Res. Commun. 23 (1966) 473–478. [PMID: 4289759]
[EC 1.1.1.144 created 1972]
 
 
EC 1.17.99.8     Relevance: 85.2%
Accepted name: limonene dehydrogenase
Reaction: (1) (S)-limonene + H2O + acceptor = (–)-perillyl alcohol + reduced acceptor
(2) (R)-limonene + H2O + acceptor = (+)-perillyl alcohol + reduced acceptor
Glossary: limonene = 1-methyl-4-(prop-1-en-2-yl)cyclohex-1-ene
perillyl alcohol = [4-(prop-1-en-2-yl)cyclohex-1-en-1-yl]methanol
(–)-perillyl alcohol = (S)-perillyl alcohol = [(4S)-4-(prop-1-en-2-yl)cyclohex-1-en-1-yl]methanol
(+)-perillyl alcohol = (R)-perillyl alcohol = [(4R)-4-(prop-1-en-2-yl)cyclohex-1-en-1-yl]methanol
(–)-limonene = (S)-limonene = (4S)-1-methyl-4-(prop-1-en-2-yl)cyclohexene
(+)-limonene = (R)-limonene = (4R)-1-methyl-4-(prop-1-en-2-yl)cyclohexene
Other name(s): ctmAB (gene names)
Systematic name: limonene:acceptor oxidoreductase (7-hydroxylating)
Comments: Contains FAD. The enzyme, characterized from the bacterium Castellaniella defragrans 65Phen, hydroxylates the R- and S-enantiomers at a similar rate. The in vivo electron acceptor may be a heterodimeric electron transfer flavoprotein (ETF).
References:
1.  Petasch, J., Disch, E.M., Markert, S., Becher, D., Schweder, T., Huttel, B., Reinhardt, R. and Harder, J. The oxygen-independent metabolism of cyclic monoterpenes in Castellaniella defragrans 65Phen. BMC Microbiol. 14:164 (2014). [PMID: 24952578]
2.  Puentes-Cala, E., Liebeke, M., Markert, S. and Harder, J. Limonene dehydrogenase hydroxylates the allylic methyl group of cyclic monoterpenes in the anaerobic terpene degradation by Castellaniella defragrans. J. Biol. Chem. 293 (2018) 9520–9529. [PMID: 29716998]
[EC 1.17.99.8 created 2020]
 
 
EC 1.14.13.49      
Transferred entry: (S)-limonene 7-monooxygenase. Now classified as EC 1.14.14.52, (S)-limonene 7-monooxygenase
[EC 1.14.13.49 created 1992, modified 2003, deleted 2017]
 
 
EC 1.14.13.47      
Transferred entry: (S)-limonene 3-monooxygenase. Now EC 1.14.14.99, (S)-limonene 3-monooxygenase
[EC 1.14.13.47 created 1992, modified 2003, deleted 2018]
 
 
EC 1.14.13.48      
Transferred entry: (S)-limonene 6-monooxygenase. Now classified as EC 1.14.14.51, (S)-limonene 6-monooxygenase
[EC 1.14.13.48 created 1992, modified 2003, deleted 2017]
 
 
EC 1.14.14.52     Relevance: 71.5%
Accepted name: (S)-limonene 7-monooxygenase
Reaction: (S)-limonene + [reduced NADPH—hemoprotein reductase] + O2 = (–)-perillyl alcohol + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: limonene = a monoterpenoid
(S)-limonene = (–)-limonene
Other name(s): (–)-limonene 7-monooxygenase; (–)-limonene hydroxylase; (–)-limonene monooxygenase; (–)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating)
Systematic name: (S)-limonene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (7-hydroxylating)
Comments: A cytochrome P-450 (heme thiolate) enzyme. The enzyme, characterized from the plant Perilla frutescens, participates in the biosynthesis of perillyl aldehyde, the major constituent of the essential oil that accumulates in the glandular trichomes of this plant. Some forms of the enzyme also catalyse the oxidation of (–)-perillyl alcohol to (–)-perillyl aldehyde.
References:
1.  Karp, F., Mihaliak, C.A., Harris, J.L. and Croteau, R. Monoterpene biosynthesis: specificity of the hydroxylations of (-)-limonene by enzyme preparations from peppermint (Mentha piperita), spearmint (Mentha spicata), and perilla (Perilla frutescens) leaves. Arch. Biochem. Biophys. 276 (1990) 219–226. [PMID: 2297225]
2.  Mau, C.J., Karp, F., Ito, M., Honda, G. and Croteau, R.B. A candidate cDNA clone for (–)-limonene-7-hydroxylase from Perilla frutescens. Phytochemistry 71 (2010) 373–379. [PMID: 20079506]
3.  Fujiwara, Y. and Ito, M. Molecular cloning and characterization of a Perilla frutescens cytochrome P450 enzyme that catalyzes the later steps of perillaldehyde biosynthesis. Phytochemistry 134 (2017) 26–37. [PMID: 27890582]
[EC 1.14.14.52 created 1992 as EC 1.14.13.49, modified 2003, transferred 2017 to EC 1.14.14.52]
 
 
EC 5.3.3.11     Relevance: 48.3%
Accepted name: isopiperitenone Δ-isomerase
Reaction: isopiperitenone = piperitenone
Systematic name: isopiperitenone Δ84-isomerase
Comments: Involved in the biosynthesis of menthol and related monoterpenes in peppermint (Mentha piperita) leaves.
References:
1.  Kjonaas, R.B., Venkatachalam, K.V. and Croteau, R. Metabolism of monoterpenes: oxidation of isopiperitenol to isopiperitenone, and subsequent isomerization to piperitenone by soluble enzyme preparations from peppermint (Mentha piperita) leaves. Arch. Biochem. Biophys. 238 (1985) 49–60. [PMID: 3885858]
[EC 5.3.3.11 created 1989]
 
 
EC 1.1.1.194     Relevance: 45.6%
Accepted name: coniferyl-alcohol dehydrogenase
Reaction: coniferyl alcohol + NADP+ = coniferyl aldehyde + NADPH + H+
Other name(s): CAD (ambiguous)
Systematic name: coniferyl-alcohol:NADP+ oxidoreductase
Comments: Specific for coniferyl alcohol; does not act on cinnamyl alcohol, 4-coumaryl alcohol or sinapyl alcohol.
References:
1.  Mansell, R.L., Babbel, G.R. and Zenk, M.H. Multiple forms and specificity of coniferyl alcohol dehydrogenase from cambial regions of higher plants. Phytochemistry 15 (1976) 1849–1853.
2.  Wyrambik, D. and Grisebach, H. Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures. Eur. J. Biochem. 59 (1975) 9–15. [PMID: 1250]
[EC 1.1.1.194 created 1984]
 
 
EC 1.1.1.243     Relevance: 45.5%
Accepted name: carveol dehydrogenase
Reaction: (–)-trans-carveol + NADP+ = (–)-carvone + NADPH + H+
Other name(s): (–)-trans-carveol dehydrogenase
Systematic name: (–)-trans-carveol:NADP+ oxidoreductase
References:
1.  Gershenzon, J., Maffei, M. and Croteau, R. Biochemical and histochemical-localization of monoterpene biosynthesis in the glandular trichomes of spearmint (Mentha spicata). Plant Physiol. 89 (1989) 1351–1357. [PMID: 16666709]
[EC 1.1.1.243 created 1992]
 
 
EC 1.1.1.195     Relevance: 45.2%
Accepted name: cinnamyl-alcohol dehydrogenase
Reaction: cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
Other name(s): cinnamyl alcohol dehydrogenase; CAD (ambiguous)
Systematic name: cinnamyl-alcohol:NADP+ oxidoreductase
Comments: Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and cinnamyl alcohol (cf. EC 1.1.1.194 coniferyl-alcohol dehydrogenase).
References:
1.  Sarni, F., Grand, C. and Baudet, A.M. Purification and properties of cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase from poplar stems (Populus X euramericana). Eur. J. Biochem. 139 (1984) 259–265. [PMID: 6365550]
2.  Wyrambik, D. and Grisebach, H. Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures. Eur. J. Biochem. 59 (1975) 9–15. [PMID: 1250]
3.  Wyrambik, D. and Grisebach, H. Enzymic synthesis of lignin precursors. Further studies on cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures. Eur. J. Biochem. 97 (1979) 503–509. [PMID: 572771]
[EC 1.1.1.195 created 1984]
 
 
EC 1.14.14.51     Relevance: 43.8%
Accepted name: (S)-limonene 6-monooxygenase
Reaction: (S)-limonene + [reduced NADPH—hemoprotein reductase] + O2 = (–)-trans-carveol + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: limonene = a monoterpenoid
(S)-limonene = (–)-limonene
Other name(s): (–)-limonene 6-hydroxylase; (–)-limonene 6-monooxygenase; (–)-limonene,NADPH:oxygen oxidoreductase (6-hydroxylating)
Systematic name: (S)-limonene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6-hydroxylating)
Comments: A cytochrome P-450 (heme thiolate) enzyme. The enzyme participates in the biosynthesis of (–)-carvone, which is responsible for the aroma of spearmint.
References:
1.  Karp, F., Mihaliak, C.A., Harris, J.L. and Croteau, R. Monoterpene biosynthesis: specificity of the hydroxylations of (-)-limonene by enzyme preparations from peppermint (Mentha piperita), spearmint (Mentha spicata), and perilla (Perilla frutescens) leaves. Arch. Biochem. Biophys. 276 (1990) 219–226. [PMID: 2297225]
[EC 1.14.14.51 created 1992 as EC 1.14.13.48, modified 2003, transferred 2017 to EC 1.14.14.51]
 
 
EC 4.2.3.16     Relevance: 43.6%
Accepted name: (4S)-limonene synthase
Reaction: geranyl diphosphate = (S)-limonene + diphosphate
Glossary: limonene = a monoterpenoid
(S)-limonene = (-)-limonene
Other name(s): (-)-(4S)-limonene synthase; 4S-(-)-limonene synthase; geranyldiphosphate diphosphate lyase (limonene forming); geranyldiphosphate diphosphate lyase [cyclizing, (4S)-limonene-forming]; geranyl-diphosphate diphosphate-lyase [cyclizing; (-)-(4S)-limonene-forming]
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing; (S)-limonene-forming]
Comments: A recombinant enzyme (also known as a monoterpene synthase or cyclase) from the grand fir (Abies grandis) requires Mn2+ and K+ for activity. Mg2+ is essentially ineffective as the divalent metal ion cofactor.
References:
1.  Bohlmann, J., Steele, C.L. and Croteau, R. Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, characterization, and functional expression of myrcene synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase. J. Biol. Chem. 272 (1997) 21784–21792. [PMID: 9268308]
2.  Collby, S.M., Alonso, W.R., Katahira, E.J., McGarvey, D.J. and Croteau, R. 4S-Limonene synthase from the oil glands of spearmint (Mentha spicata). cDNA isolation, characterization, and bacterial expression of the catalytically active monoterpene cyclase. J. Biol. Chem. 268 (1993) 23016–23024. [PMID: 8226816]
3.  Yuba, A., Yazaki, K., Tabata, M., Honda, G. and Croteau, R. cDNA cloning, characterization, and functional expression of 4S-(-)-limonene synthase from Perilla frutescens. Arch. Biochem. Biophys. 332 (1996) 280–287. [PMID: 8806736]
[EC 4.2.3.16 created 2000 as EC 4.1.99.10, transferred 2000 to EC 4.2.3.16, modified 2003]
 
 
EC 1.1.3.7     Relevance: 42.4%
Accepted name: aryl-alcohol oxidase
Reaction: an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
Other name(s): aryl alcohol oxidase; veratryl alcohol oxidase; arom. alcohol oxidase
Systematic name: aryl-alcohol:oxygen oxidoreductase
Comments: Oxidizes many primary alcohols containing an aromatic ring; best substrates are (2-naphthyl)methanol and 3-methoxybenzyl alcohol.
References:
1.  Farmer, V.C., Henderson, M.E.K. and Russell, J.D. Aromatic-alcohol-oxidase activity in the growth medium of Polystictus versicolor. Biochem. J. 74 (1960) 257–262. [PMID: 13821599]
[EC 1.1.3.7 created 1965]
 
 
EC 1.1.1.347     Relevance: 41.4%
Accepted name: geraniol dehydrogenase (NAD+)
Reaction: geraniol + NAD+ = geranial + NADH + H+
Other name(s): GeDH; geoA (gene name)
Systematic name: geraniol:NAD+ oxidoreductase
Comments: The enzyme from the bacterium Castellaniella defragrans is most active in vitro with perillyl alcohol [2]. The enzyme from the prune mite Carpoglyphus lactis also acts (more slowly) on farnesol but not on nerol [1].
References:
1.  Noge, K., Kato, M., Mori, N., Kataoka, M., Tanaka, C., Yamasue, Y., Nishida, R. and Kuwahara, Y. Geraniol dehydrogenase, the key enzyme in biosynthesis of the alarm pheromone, from the astigmatid mite Carpoglyphus lactis (Acari: Carpoglyphidae). FEBS J. 275 (2008) 2807–2817. [PMID: 18422649]
2.  Lüddeke, F., Wülfing, A., Timke, M., Germer, F., Weber, J., Dikfidan, A., Rahnfeld, T., Linder, D., Meyerdierks, A. and Harder, J. Geraniol and geranial dehydrogenases induced in anaerobic monoterpene degradation by Castellaniella defragrans. Appl. Environ. Microbiol. 78 (2012) 2128–2136. [PMID: 22286981]
[EC 1.1.1.347 created 2013]
 
 
EC 1.14.13.104      
Transferred entry: (+)-menthofuran synthase. Now EC 1.14.14.143, (+)-menthofuran synthase
[EC 1.14.13.104 created 2008, deleted 2018]
 
 
EC 1.1.1.1     Relevance: 41%
Accepted name: alcohol dehydrogenase
Reaction: (1) a primary alcohol + NAD+ = an aldehyde + NADH + H+
(2) a secondary alcohol + NAD+ = a ketone + NADH + H+
Other name(s): aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase
Systematic name: alcohol:NAD+ oxidoreductase
Comments: A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
References:
1.  Brändén, G.-I., Jörnvall, H., Eklund, H. and Furugren, B. Alcohol dehydrogenase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 11, Academic Press, New York, 1975, pp. 103–190.
2.  Jörnvall, H. Differences between alcohol dehydrogenases. Structural properties and evolutionary aspects. Eur. J. Biochem. 72 (1977) 443–452. [PMID: 320001]
3.  Negelein, E. and Wulff, H.-J. Diphosphopyridinproteid ackohol, acetaldehyd. Biochem. Z. 293 (1937) 351–389.
4.  Sund, H. and Theorell, H. Alcohol dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 25–83.
5.  Theorell, H. Kinetics and equilibria in the liver alcohol dehydrogenase system. Adv. Enzymol. Relat. Subj. Biochem. 20 (1958) 31–49. [PMID: 13605979]
[EC 1.1.1.1 created 1961, modified 2011]
 
 
EC 1.1.1.90     Relevance: 40.7%
Accepted name: aryl-alcohol dehydrogenase
Reaction: an aromatic alcohol + NAD+ = an aromatic aldehyde + NADH + H+
Other name(s): p-hydroxybenzyl alcohol dehydrogenase; benzyl alcohol dehydrogenase; coniferyl alcohol dehydrogenase
Systematic name: aryl-alcohol:NAD+ oxidoreductase
Comments: A group of enzymes with broad specificity towards primary alcohols with an aromatic or cyclohex-1-ene ring, but with low or no activity towards short-chain aliphatic alcohols.
References:
1.  Suhara, K., Takemori, S. and Katagiri, M. The purification and properties of benzylalcohol dehydrogenase from Pseudomonas sp. Arch. Biochem. Biophys. 130 (1969) 422–429. [PMID: 5778658]
2.  Yamanaka, K. and Minoshima, R. Identification and characterization of a nicotinamide adenine dinucleotide-dependent para-hydroxybenzyl alcohol-dehydrogenase from Rhodopseudomonas acidophila M402. Agric. Biol. Chem. 48 (1984) 1161–1171.
[EC 1.1.1.90 created 1972, modified 1989]
 
 
EC 1.1.3.30     Relevance: 40.4%
Accepted name: polyvinyl-alcohol oxidase
Reaction: polyvinyl alcohol + O2 = oxidized polyvinyl alcohol + H2O2
Other name(s): dehydrogenase, polyvinyl alcohol; PVA oxidase
Systematic name: polyvinyl-alcohol:oxygen oxidoreductase
References:
1.  Shimao, M., Nishimura, Y., Kato, N. and Sakazawa, C. Localization of polyvinyl alcohol oxidase produced by a bacterial symbiont Pseudomonas sp strain VM 15C. Appl. Environ. Microbiol. 49 (1985) 8–10. [PMID: 16346711]
2.  Shimao, M., Onishi, S., Kato, N. and Sakazawa, C. Pyrroloquinoline quinone-dependent cytochrome reduction in polyvinyl alcohol-degrading Pseudomonas sp strain VM15C. Appl. Environ. Microbiol. 55 (1989) 275–278. [PMID: 16347841]
[EC 1.1.3.30 created 1992]
 
 
EC 1.1.2.6     Relevance: 39.8%
Accepted name: polyvinyl alcohol dehydrogenase (cytochrome)
Reaction: polyvinyl alcohol + ferricytochrome c = oxidized polyvinyl alcohol + ferrocytochrome c + H+
Other name(s): PVA dehydrogenase; PVADH
Systematic name: polyvinyl alcohol:ferricytochrome-c oxidoreductase
Comments: A quinoprotein. The enzyme is involved in bacterial polyvinyl alcohol degradation. Some Gram-negative bacteria degrade polyvinyl alcohol by importing it into the periplasmic space, where it is oxidized by polyvinyl alcohol dehydrogenase, an enzyme that is coupled to the respiratory chain via cytochrome c. The enzyme contains a pyrroloquinoline quinone cofactor.
References:
1.  Shimao, M., Ninomiya, K., Kuno, O., Kato, N. and Sakazawa, C. Existence of a novel enzyme, pyrroloquinoline quinone-dependent polyvinyl alcohol dehydrogenase, in a bacterial symbiont, Pseudomonas sp. strain VM15C. Appl. Environ. Microbiol. 51 (1986) 268. [PMID: 3513704]
2.  Shimao, M., Onishi, S., Kato, N. and Sakazawa, C. Pyrroloquinoline quinone-dependent cytochrome reduction in polyvinyl alcohol-degrading Pseudomonas sp strain VM15C. Appl. Environ. Microbiol. 55 (1989) 275–278. [PMID: 16347841]
3.  Mamoto, R., Hu, X., Chiue, H., Fujioka, Y. and Kawai, F. Cloning and expression of soluble cytochrome c and its role in polyvinyl alcohol degradation by polyvinyl alcohol-utilizing Sphingopyxis sp. strain 113P3. J. Biosci. Bioeng. 105 (2008) 147–151. [PMID: 18343342]
4.  Hirota-Mamoto, R., Nagai, R., Tachibana, S., Yasuda, M., Tani, A., Kimbara, K. and Kawai, F. Cloning and expression of the gene for periplasmic poly(vinyl alcohol) dehydrogenase from Sphingomonas sp. strain 113P3, a novel-type quinohaemoprotein alcohol dehydrogenase. Microbiology 152 (2006) 1941–1949. [PMID: 16804170]
5.  Hu, X., Mamoto, R., Fujioka, Y., Tani, A., Kimbara, K. and Kawai, F. The pva operon is located on the megaplasmid of Sphingopyxis sp. strain 113P3 and is constitutively expressed, although expression is enhanced by PVA. Appl. Microbiol. Biotechnol. 78 (2008) 685–693. [PMID: 18214469]
6.  Kawai, F. and Hu, X. Biochemistry of microbial polyvinyl alcohol degradation. Appl. Microbiol. Biotechnol. 84 (2009) 227–237. [PMID: 19590867]
[EC 1.1.2.6 created 1989 as EC 1.1.99.23, transferred 2010 to EC 1.1.2.6]
 
 
EC 2.4.1.111     Relevance: 39.6%
Accepted name: coniferyl-alcohol glucosyltransferase
Reaction: UDP-glucose + coniferyl alcohol = UDP + coniferin
Other name(s): uridine diphosphoglucose-coniferyl alcohol glucosyltransferase; UDP-glucose coniferyl alcohol glucosyltransferase
Systematic name: UDP-glucose:coniferyl-alcohol 4′-β-D-glucosyltransferase
Comments: Sinapyl alcohol can also act as acceptor.
References:
1.  Ibrahim, R.K. and Grisebach, H. Purification and properties of UDP-glucose: coniferyl alcohol glucosyltransferase from suspension cultures of Paul's scarlet rose. Arch. Biochem. Biophys. 176 (1976) 700–708. [PMID: 10853]
[EC 2.4.1.111 created 1984]
 
 
EC 1.1.99.8      
Transferred entry: alcohol dehydrogenase (acceptor). Now EC 1.1.2.7, methanol dehydrogenase (cytochrome c) and EC 1.1.2.8, alcohol dehydrogenase (cytochrome c).
[EC 1.1.99.8 created 1972, modified 1982, deleted 2010]
 
 
EC 1.1.1.91     Relevance: 38.7%
Accepted name: aryl-alcohol dehydrogenase (NADP+)
Reaction: an aromatic alcohol + NADP+ = an aromatic aldehyde + NADPH + H+
Other name(s): aryl alcohol dehydrogenase (nicotinamide adenine dinucleotide phosphate); coniferyl alcohol dehydrogenase; NADPH-linked benzaldehyde reductase; aryl-alcohol dehydrogenase (NADP)
Systematic name: aryl-alcohol:NADP+ oxidoreductase
Comments: Also acts on some aliphatic aldehydes, but cinnamaldehyde was the best substrate found.
References:
1.  Gross, G.G. and Zenk, M.H. Reduktionaromatische Säuren zu Aldehyden und Alkoholen im zellfreien System. 2. Reinigung und Eigenschaften von Aryl Alkohol:NADP-Oxidoreductase aus Neurospora crassa. Eur. J. Biochem. 8 (1969) 420–425. [PMID: 4389864]
[EC 1.1.1.91 created 1972]
 
 
EC 1.1.3.38     Relevance: 38.7%
Accepted name: vanillyl-alcohol oxidase
Reaction: vanillyl alcohol + O2 = vanillin + H2O2
Other name(s): 4-hydroxy-2-methoxybenzyl alcohol oxidase
Systematic name: vanillyl alcohol:oxygen oxidoreductase
Comments: Vanillyl-alcohol oxidase from Penicillium simplicissimum contains covalently bound FAD. It converts a wide range of 4-hydroxybenzyl alcohols and 4-hydroxybenzylamines into the corresponding aldehydes. The allyl group of 4-allylphenols is also converted into the -CH=CH-CH2OH group.
References:
1.  de Jong, E., van Berkel, W.J.H., van der Zwan, R.P. and de Bont, J.A.M. Purification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum, a novel aromatic alcohol oxidase containing covalently bound FAD. Eur. J. Biochem. 208 (1992) 651–657. [PMID: 1396672]
2.  Fraaije, M.W., Veeger, C. and van Berkel, W.J.H. Substrate specificity of flavin-dependent vanillyl-alcohol oxidase from Penicillium simplicissimum. Evidence for the production of 4-hydroxycinnamyl alcohols from 4-allylphenols. Eur. J. Biochem. 234 (1995) 271–277. [PMID: 8529652]
[EC 1.1.3.38 created 1999]
 
 
EC 1.1.99.23      
Transferred entry: polyvinyl-alcohol dehydrogenase (acceptor). Now EC 1.1.2.6, polyvinyl alcohol dehydrogenase (cytochrome)
[EC 1.1.99.23 created 1989, deleted 2010]
 
 
EC 1.1.3.18     Relevance: 38.2%
Accepted name: secondary-alcohol oxidase
Reaction: a secondary alcohol + O2 = a ketone + H2O2
Other name(s): polyvinyl alcohol oxidase; secondary alcohol oxidase
Systematic name: secondary-alcohol:oxygen oxidoreductase
Comments: Acts on secondary alcohols with five or more carbons, and polyvinyl alcohols with molecular mass over 300 Da. The Pseudomonas enzyme contains one atom of non-heme iron per molecule.
References:
1.  Morita, M., Hamada, N., Sakai, K. and Watanabe, Y. Purification and properties of secondary alcohol oxidase from a strain of Pseudomonas. Agric. Biol. Chem. 43 (1979) 1225–1235.
2.  Sakai, K., Hamada, N. and Watanabe, Y. Separation of secondary alcohol oxidase and oxidized poly(vinyl alcohol) hydrolase by hydrophobic and dye-ligand chromatographies. Agric. Biol. Chem. 47 (1983) 153–155.
3.  Suzuki, T. Purification and some properties of polyvinyl alcohol-degrading enzyme produced by Pseudomonas O-3. Agric. Biol. Chem. 40 (1976) 497–504.
4.  Suzuki, T. Oxidation of secondary alcohols by polyvinyl alcohol-degrading enzyme produced by Pseudomonas O-3. Agric. Biol. Chem. 42 (1977) 1187–1194.
[EC 1.1.3.18 created 1981]
 
 
EC 2.3.1.84     Relevance: 38.1%
Accepted name: alcohol O-acetyltransferase
Reaction: acetyl-CoA + an alcohol = CoA + an acetyl ester
Other name(s): alcohol acetyltransferase
Systematic name: acetyl-CoA:alcohol O-acetyltransferase
Comments: Acts on a range of short-chain aliphatic alcohols, including methanol and ethanol
References:
1.  Yoshioka, K. and Hashimoto, N. Ester formation by alcohol acetyltransferase from brewers' yeast. Agric. Biol. Chem. 45 (1981) 2183–2190.
[EC 2.3.1.84 created 1984]
 
 
EC 1.14.19.48     Relevance: 38.1%
Accepted name: tert-amyl alcohol desaturase
Reaction: tert-amyl alcohol + NADPH + H+ + O2 = isoprenyl alcohol + NADP+ + 2 H2O
Glossary: isoprenyl alcohol = 3-methylbut-1-en-3-ol
tert-amyl alcohol = 2-methylbutan-2-ol
Other name(s): mdpJK (gene names)
Systematic name: tert-amyl alcohol,NADPH:oxygen oxidoreductase (1,2-dehydrogenating)
Comments: The enzyme, characterized from the bacterium Aquincola tertiaricarbonis, is a Rieske nonheme mononuclear iron oxygenase. It can also act, with lower efficiency, on butan-2-ol, converting it to but-1-en-3-ol. Depending on the substrate, the enzyme also catalyses EC 1.14.13.229, tert-butanol monooxygenase.
References:
1.  Schafer, F., Schuster, J., Wurz, B., Hartig, C., Harms, H., Muller, R.H. and Rohwerder, T. Synthesis of short-chain diols and unsaturated alcohols from secondary alcohol substrates by the Rieske nonheme mononuclear iron oxygenase MdpJ. Appl. Environ. Microbiol. 78 (2012) 6280–6284. [PMID: 22752178]
2.  Schuster, J., Schafer, F., Hubler, N., Brandt, A., Rosell, M., Hartig, C., Harms, H., Muller, R.H. and Rohwerder, T. Bacterial degradation of tert-amyl alcohol proceeds via hemiterpene 2-methyl-3-buten-2-ol by employing the tertiary alcohol desaturase function of the Rieske nonheme mononuclear iron oxygenase MdpJ. J. Bacteriol. 194 (2012) 972–981. [PMID: 22194447]
[EC 1.14.19.48 created 2016]
 
 
EC 2.7.1.66     Relevance: 37.6%
Accepted name: undecaprenol kinase
Reaction: ATP + undecaprenol = ADP + undecaprenyl phosphate
Other name(s): isoprenoid alcohol kinase; isoprenoid alcohol phosphokinase; C55-isoprenoid alcohol phosphokinase; isoprenoid alcohol kinase (phosphorylating); C55-isoprenoid alcohol kinase; C55-isoprenyl alcohol phosphokinase; polyisoprenol kinase
Systematic name: ATP:undecaprenol phosphotransferase
References:
1.  Higashi, Y., Siewert, G. and Strominger, J.L. Biosynthesis of the peptidoglycan of bacterial cell walls. XIX. Isoprenoid alcohol phosphokinase. J. Biol. Chem. 245 (1970) 3683–3690. [PMID: 4248528]
[EC 2.7.1.66 created 1972]
 
 
EC 2.4.1.172     Relevance: 36.8%
Accepted name: salicyl-alcohol β-D-glucosyltransferase
Reaction: UDP-glucose + salicyl alcohol = UDP + salicin
Other name(s): uridine diphosphoglucose-salicyl alcohol 2-glucosyltransferase; UDPglucose:salicyl alcohol phenyl-glucosyltransferase
Systematic name: UDP-glucose:salicyl-alcohol β-D-glucosyltransferase
References:
1.  Mizukami, H., Terao, T. and Ohashi, H. Partial-purification and characterization of UDP-glucose-salicyl alcohol glucosyltransferase from Gardeni jasminoides cell-cultures. Planta Med. 1985 (1985) 104–107.
[EC 2.4.1.172 created 1989]
 
 
EC 1.1.1.192     Relevance: 36.7%
Accepted name: long-chain-alcohol dehydrogenase
Reaction: a long-chain alcohol + 2 NAD+ + H2O = a long-chain carboxylate + 2 NADH + 2 H+
Other name(s): long-chain alcohol dehydrogenase; fatty alcohol oxidoreductase
Systematic name: long-chain-alcohol:NAD+ oxidoreductase
Comments: Hexadecanol is a good substrate.
References:
1.  Lee, T.-C. Characterization of fatty alcohol:NAD+ oxidoreductase from rat liver. J. Biol. Chem. 254 (1979) 2892–2896. [PMID: 34610]
[EC 1.1.1.192 created 1984]
 
 
EC 1.1.1.97     Relevance: 36.5%
Accepted name: 3-hydroxybenzyl-alcohol dehydrogenase
Reaction: 3-hydroxybenzyl alcohol + NADP+ = 3-hydroxybenzaldehyde + NADPH + H+
Other name(s): m-hydroxybenzyl alcohol dehydrogenase; m-hydroxybenzyl alcohol (NADP) dehydrogenase; m-hydroxybenzylalcohol dehydrogenase
Systematic name: 3-hydroxybenzyl-alcohol:NADP+ oxidoreductase
References:
1.  Forrester, P.I. and Gaucher, G.M. m-Hydroxybenzyl alcohol dehydrogenase from Penicillium urticae. Biochemistry 11 (1972) 1108–1114. [PMID: 4335290]
[EC 1.1.1.97 created 1972]
 
 
EC 1.1.3.20     Relevance: 36.4%
Accepted name: long-chain-alcohol oxidase
Reaction: a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
Other name(s): long-chain fatty alcohol oxidase; fatty alcohol oxidase; fatty alcohol:oxygen oxidoreductase; long-chain fatty acid oxidase
Systematic name: long-chain-alcohol:oxygen oxidoreductase
Comments: Oxidizes long-chain fatty alcohols; best substrate is dodecyl alcohol.
References:
1.  Moreau, R.A. and Huang, A.H.C. Oxidation of fatty alcohol in the cotyledons of jojoba seedlings. Arch. Biochem. Biophys. 194 (1979) 422–430. [PMID: 36040]
2.  Moreau, R.A. and Huang, A.H.C. Enzymes of wax ester catabolism in jojoba. Methods Enzymol. 71 (1981) 804–813.
3.  Cheng, Q., Liu, H.T., Bombelli, P., Smith, A. and Slabas, A.R. Functional identification of AtFao3, a membrane bound long chain alcohol oxidase in Arabidopsis thaliana. FEBS Lett. 574 (2004) 62–68. [PMID: 15358540]
4.  Zhao, S., Lin, Z., Ma, W., Luo, D. and Cheng, Q. Cloning and characterization of long-chain fatty alcohol oxidase LjFAO1 in Lotus japonicus. Biotechnol. Prog. 24 (2008) 773–779. [PMID: 18396913]
5.  Cheng, Q., Sanglard, D., Vanhanen, S., Liu, H.T., Bombelli, P., Smith, A. and Slabas, A.R. Candida yeast long chain fatty alcohol oxidase is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism. Biochim. Biophys. Acta 1735 (2005) 192–203. [PMID: 16046182]
[EC 1.1.3.20 created 1984, modified 2010]
 
 
EC 1.1.1.54     Relevance: 34.7%
Accepted name: allyl-alcohol dehydrogenase
Reaction: allyl alcohol + NADP+ = acrolein + NADPH + H+
Systematic name: allyl-alcohol:NADP+ oxidoreductase
Comments: Also acts on saturated primary alcohols.
References:
1.  Otsuka, K. Triphosphopyridine nucleotide-allyl and -ethyl alcohol dehydrogenases from Escherichia coli. J. Gen. Appl. Microbiol. 4 (1958) 211–215.
[EC 1.1.1.54 created 1965]
 
 
EC 1.14.14.99     Relevance: 34.5%
Accepted name: (S)-limonene 3-monooxygenase
Reaction: (S)-limonene + [reduced NADPH—hemoprotein reductase] + O2 = (–)-trans-isopiperitenol + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: limonene = a monoterpenoid
(S)-limonene = (–)-limonene
Other name(s): (–)-limonene 3-hydroxylase; (–)-limonene 3-monooxygenase; CYP71D15 (gene name)
Systematic name: (S)-limonene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from peppermint (Mentha piperita).
References:
1.  Karp, F., Mihaliak, C.A., Harris, J.L. and Croteau, R. Monoterpene biosynthesis: specificity of the hydroxylations of (-)-limonene by enzyme preparations from peppermint (Mentha piperita), spearmint (Mentha spicata), and perilla (Perilla frutescens) leaves. Arch. Biochem. Biophys. 276 (1990) 219–226. [PMID: 2297225]
2.  Lupien, S., Karp, F., Wildung, M. and Croteau, R. Regiospecific cytochrome P450 limonene hydroxylases from mint (Mentha) species: cDNA isolation, characterization, and functional expression of (–)-4S-limonene-3-hydroxylase and (–)-4S-limonene-6-hydroxylase. Arch. Biochem. Biophys. 368 (1999) 181–192. [PMID: 10415126]
3.  Wust, M., Little, D.B., Schalk, M. and Croteau, R. Hydroxylation of limonene enantiomers and analogs by recombinant (–)-limonene 3- and 6-hydroxylases from mint (Mentha) species: evidence for catalysis within sterically constrained active sites. Arch. Biochem. Biophys. 387 (2001) 125–136. [PMID: 11368174]
[EC 1.14.14.99 created 1992 as EC 1.14.13.47, modified 2003, transferred 2018 1.14.14.99]
 
 
EC 1.1.1.71     Relevance: 34.4%
Accepted name: alcohol dehydrogenase [NAD(P)+]
Reaction: an alcohol + NAD(P)+ = an aldehyde + NAD(P)H + H+
Other name(s): retinal reductase (ambiguous); aldehyde reductase (NADPH/NADH); alcohol dehydrogenase [NAD(P)]
Systematic name: alcohol:NAD(P)+ oxidoreductase
Comments: Reduces aliphatic aldehydes of carbon chain length from 2 to 14, with greatest activity on C4, C6 and C8 aldehydes; also reduces retinal to retinol.
References:
1.  Fidge, N.H. and Goodman, D.S. The enzymatic reduction of retinal to retinol in rat intestine. J. Biol. Chem. 243 (1968) 4372–4379. [PMID: 4300551]
[EC 1.1.1.71 created 1972]
 
 
EC 1.1.5.7     Relevance: 33.7%
Accepted name: cyclic alcohol dehydrogenase (quinone)
Reaction: a cyclic alcohol + a quinone = a cyclic ketone + a quinol
Other name(s): cyclic alcohol dehydrogenase; MCAD
Systematic name: cyclic alcohol:quinone oxidoreductase
Comments: This enzyme oxidizes a wide variety of cyclic alcohols. Some minor enzyme activity is found with aliphatic secondary alcohols and sugar alcohols, but not primary alcohols. The enzyme is unable to catalyse the reverse reaction of cyclic ketones or aldehydes to cyclic alcohols. This enzyme differs from EC 1.1.5.5, alcohol dehydrogenase (quinone), which shows activity with ethanol [1].
References:
1.  Moonmangmee, D., Fujii, Y., Toyama, H., Theeragool, G., Lotong, N., Matsushita, K. and Adachi, O. Purification and characterization of membrane-bound quinoprotein cyclic alcohol dehydrogenase from Gluconobacter frateurii CHM 9. Biosci. Biotechnol. Biochem. 65 (2001) 2763–2772. [PMID: 11826975]
[EC 1.1.5.7 created 2010]
 
 
EC 1.1.98.5     Relevance: 33.3%
Accepted name: secondary-alcohol dehydrogenase (coenzyme-F420)
Reaction: R-CHOH-R′ + oxidized coenzyme F420 = R-CO-R′ + reduced coenzyme F420
Glossary: oxidized coenzyme F420 = N-(N-{O-[5-(8-hydroxy-2,4-dioxo-2,3,4,10-tetrahydropyrimido[4,5-b]quinolin-10-yl)-5-deoxy-L-ribityl-1-phospho]-(S)-lactyl}-γ-L-glutamyl)-L-glutamate
Other name(s): F420-dependent alcohol dehydrogenase; secondary alcohol:F420 oxidoreductase; F420-dependent secondary alcohol dehydrogenase
Systematic name: secondary-alcohol:coenzyme F420 oxidoreductase
Comments: The enzyme isolated from the methanogenic archaea Methanogenium liminatans catalyses the reversible oxidation of various secondary and cyclic alcohols to the corresponding ketones.
References:
1.  Bleicher, K. and Winter, J. Purification and properties of F420- and NADP+-dependent alcohol dehydrogenases of Methanogenium liminatans and Methanobacterium palustre, specific for secondary alcohols. Eur. J. Biochem. 200 (1991) 43–51. [PMID: 1879431]
2.  Aufhammer, S.W., Warkentin, E., Berk, H., Shima, S., Thauer, R.K. and Ermler, U. Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family. Structure 12 (2004) 361–370. [PMID: 15016352]
[EC 1.1.98.5 created 2013]
 
 
EC 1.1.9.1     Relevance: 33.1%
Accepted name: alcohol dehydrogenase (azurin)
Reaction: a primary alcohol + azurin = an aldehyde + reduced azurin
Other name(s): type II quinoprotein alcohol dehydrogenase; quinohaemoprotein ethanol dehydrogenase; QHEDH; ADHIIB
Systematic name: alcohol:azurin oxidoreductase
Comments: A soluble, periplasmic PQQ-containing quinohemoprotein. Also contains a single heme c. Occurs in Comamonas and Pseudomonas. Does not require an amine activator. Oxidizes a wide range of primary and secondary alcohols, and also aldehydes and large substrates such as sterols; methanol is not a substrate. Usually assayed with phenazine methosulfate or ferricyanide. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed ‘propeller’ structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ.
References:
1.  Groen, B.W., van Kleef, M.A. and Duine, J.A. Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni. Biochem. J. 234 (1986) 611–615. [PMID: 3521592]
2.  de Jong, G.A., Caldeira, J., Sun, J., Jongejan, J.A., de Vries, S., Loehr, T.M., Moura, I., Moura, J.J. and Duine, J.A. Characterization of the interaction between PQQ and heme c in the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni. Biochemistry 34 (1995) 9451–9458. [PMID: 7626615]
3.  Toyama, H., Fujii, A., Matsushita, K., Shinagawa, E., Ameyama, M. and Adachi, O. Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols. J. Bacteriol. 177 (1995) 2442–2450. [PMID: 7730276]
4.  Matsushita, K., Yamashita, T., Aoki, N., Toyama, H. and Adachi, O. Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5. Biochemistry 38 (1999) 6111–6118. [PMID: 10320337]
5.  Chen, Z.W., Matsushita, K., Yamashita, T., Fujii, T.A., Toyama, H., Adachi, O., Bellamy, H.D. and Mathews, F.S. Structure at 1.9 Å resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5. Structure 10 (2002) 837–849. [PMID: 12057198]
6.  Oubrie, A., Rozeboom, H.J., Kalk, K.H., Huizinga, E.G. and Dijkstra, B.W. Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer. J. Biol. Chem. 277 (2002) 3727–3732. [PMID: 11714714]
[EC 1.1.9.1 created 2010 as EC 1.1.98.1; transferred 2011 to EC 1.1.9.1]
 
 
EC 1.1.98.1      
Transferred entry: Now EC 1.1.9.1, alcohol dehydrogenase (azurin)
[EC 1.1.98.1 created 2010, deleted 2011]
 
 
EC 1.14.13.229     Relevance: 32.5%
Accepted name: tert-butyl alcohol monooxygenase
Reaction: tert-butyl alcohol + NADPH + H+ + O2 = 2-methylpropane-1,2-diol + NADP+ + H2O
Other name(s): mdpJK (gene names); tert-butanol monooxygenase
Systematic name: tert-butyl alcohol,NADPH:oxygen oxidoreductase
Comments: The enzyme, characterized from the bacterium Aquincola tertiaricarbonis, is a Rieske nonheme mononuclear iron oxygenase. It can also act, with lower efficiency, on propan-2-ol, converting it to propane-1,2-diol. Depending on the substrate, the enzyme also catalyses EC 1.14.19.48, tert-amyl alcohol desaturase.
References:
1.  Schafer, F., Breuer, U., Benndorf, D., von Bergen, M., Harms, H. and Muller, R.H. Growth of Aquincola tertiaricarbonis L108 on tert-butyl alcohol leads to the induction of a phthalate dioxygenase-related protein and its associated oxidoreductase subunit. Eng. Life Sci. 7 (2007) 512–519.
2.  Schuster, J., Schafer, F., Hubler, N., Brandt, A., Rosell, M., Hartig, C., Harms, H., Muller, R.H. and Rohwerder, T. Bacterial degradation of tert-amyl alcohol proceeds via hemiterpene 2-methyl-3-buten-2-ol by employing the tertiary alcohol desaturase function of the Rieske nonheme mononuclear iron oxygenase MdpJ. J. Bacteriol. 194 (2012) 972–981. [PMID: 22194447]
[EC 1.14.13.229 created 2016]
 
 
EC 2.3.1.196     Relevance: 32.3%
Accepted name: benzyl alcohol O-benzoyltransferase
Reaction: benzoyl-CoA + benzyl alcohol = CoA + benzyl benzoate
Glossary: benzyl benzoate = benzoic acid benzyl ester
Other name(s): benzoyl-CoA:benzyl alcohol benzoyltransferase; benzoyl-CoA:benzyl alcohol/phenylethanol benzoyltransferase; benzoyl-coenzyme A:benzyl alcohol benzoyltransferase; benzoyl-coenzyme A:phenylethanol benzoyltransferase
Systematic name: benzoyl-CoA:benzyl alcohol O-benzoyltransferase
Comments: The enzyme is involved in volatile benzenoid and benzoic acid biosynthesis. The enzyme from Petunia hybrida also catalyses the formation of 2-phenylethyl benzoate from benzoyl-CoA and 2-phenylethanol. The apparent catalytic efficiency of the enzyme from Petunia hybrida with benzoyl-CoA is almost 6-fold higher than with acetyl-CoA [1].
References:
1.  Boatright, J., Negre, F., Chen, X., Kish, C.M., Wood, B., Peel, G., Orlova, I., Gang, D., Rhodes, D. and Dudareva, N. Understanding in vivo benzenoid metabolism in Petunia petal tissue. Plant Physiol. 135 (2004) 1993–2011. [PMID: 15286288]
2.  D'Auria, J.C., Chen, F. and Pichersky, E. Characterization of an acyltransferase capable of synthesizing benzylbenzoate and other volatile esters in flowers and damaged leaves of Clarkia breweri. Plant Physiol. 130 (2002) 466–476. [PMID: 12226525]
[EC 2.3.1.196 created 2011]
 
 
EC 1.1.1.2     Relevance: 31.9%
Accepted name: alcohol dehydrogenase (NADP+)
Reaction: an alcohol + NADP+ = an aldehyde + NADPH + H+
Other name(s): aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP)
Systematic name: alcohol:NADP+ oxidoreductase
Comments: A zinc protein. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. May be identical with EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate reductase (NADPH)] and EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. Re-specific with respect to NADPH.
References:
1.  Bosron, W.F. and Prairie, R.L. Triphosphopyridine nucleotide-linked aldehyde reductase. I. Purification and properties of the enzyme from pig kidney cortex. J. Biol. Chem. 247 (1972) 4480–4485. [PMID: 4402936]
2.  DeMoss, R. Triphosphopyridine nucleotide-specific ethanol dehydrogenase from Leuconostoc mesenteroides. Bacteriol. Proc. (1953) 81.
3.  Reeves, R.E., Montalvo, F.E. and Lushbaugh, T.S. Nicotinamide-adenine dinucleotide phosphate-dependent alcohol dehydrogenase. Enzyme from Entamoeba histolytica and some enzyme inhibitors. Int. J. Biochem. 2 (1971) 55–64.
4.  Tabakoff, B. and Erwin, V.G. Purification and characterization of a reduced nicotinamide adenine dinucleotide phosphate-linked aldehyde reductase from brain. J. Biol. Chem. 245 (1970) 3263–3268. [PMID: 4393513]
[EC 1.1.1.2 created 1961]
 
 
EC 1.1.2.7     Relevance: 31.7%
Accepted name: methanol dehydrogenase (cytochrome c)
Reaction: a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
Other name(s): methanol dehydrogenase; MDH (ambiguous)
Systematic name: methanol:cytochrome c oxidoreductase
Comments: A periplasmic quinoprotein alcohol dehydrogenase that only occurs in methylotrophic bacteria. It uses the novel specific cytochrome cL as acceptor. Acts on a wide range of primary alcohols, including ethanol, duodecanol, chloroethanol, cinnamyl alcohol, and also formaldehyde. Activity is stimulated by ammonia or methylamine. It is usually assayed with phenazine methosulfate. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed ’propeller’ structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ. It differs from EC 1.1.2.8, alcohol dehydrogenase (cytochrome c), in having a high affinity for methanol and in having a second essential small subunit (no known function).
References:
1.  Anthony, C. and Zatman, L.J. The microbial oxidation of methanol. 2. The methanol-oxidizing enzyme of Pseudomonas sp. M 27. Biochem. J. 92 (1964) 614–621. [PMID: 4378696]
2.  Anthony, C. and Zatman, L.J. The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group. Biochem. J. 104 (1967) 960–969. [PMID: 6049934]
3.  Duine, J.A., Frank, J. and Verweil, P.E.J. Structure and activity of the prosthetic group of methanol dehydrogenase. Eur. J. Biochem. 108 (1980) 187–192. [PMID: 6250827]
4.  Salisbury, S.A., Forrest, H.S., Cruse, W.B.T. and Kennard, O. A novel coenzyme from bacterial primary alcohol dehydrogenases. Nature (Lond.) 280 (1979) 843–844. [PMID: 471057]
5.  Cox, J.M., Day, D.J. and Anthony, C. The interaction of methanol dehydrogenase and its electron acceptor, cytochrome cL in methylotrophic bacteria. Biochim. Biophys. Acta 1119 (1992) 97–106. [PMID: 1311606]
6.  Blake, C.C., Ghosh, M., Harlos, K., Avezoux, A. and Anthony, C. The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues. Nat. Struct. Biol. 1 (1994) 102–105. [PMID: 7656012]
7.  Xia, Z.X., He, Y.N., Dai, W.W., White, S.A., Boyd, G.D. and Mathews, F.S. Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 Å resolution. Biochemistry 38 (1999) 1214–1220. [PMID: 9930981]
8.  Afolabi, P.R., Mohammed, F., Amaratunga, K., Majekodunmi, O., Dales, S.L., Gill, R., Thompson, D., Cooper, J.B., Wood, S.P., Goodwin, P.M. and Anthony, C. Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome cL. Biochemistry 40 (2001) 9799–9809. [PMID: 11502173]
9.  Anthony, C. and Williams, P. The structure and mechanism of methanol dehydrogenase. Biochim. Biophys. Acta 1647 (2003) 18–23. [PMID: 12686102]
10.  Williams, P.A., Coates, L., Mohammed, F., Gill, R., Erskine, P.T., Coker, A., Wood, S.P., Anthony, C. and Cooper, J.B. The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens. Acta Crystallogr. D Biol. Crystallogr. 61 (2005) 75–79. [PMID: 15608378]
[EC 1.1.2.7 created 1972 as EC 1.1.99.8, modified 1982, part transferred 2010 to EC 1.1.2.7]
 
 
EC 2.8.2.2     Relevance: 31.6%
Accepted name: alcohol sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + an alcohol = adenosine 3′,5′-bisphosphate + an alkyl sulfate
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): hydroxysteroid sulfotransferase; 3β-hydroxy steroid sulfotransferase; Δ5-3β-hydroxysteroid sulfokinase; 3-hydroxysteroid sulfotransferase; HST; 5α-androstenol sulfotransferase; cholesterol sulfotransferase; dehydroepiandrosterone sulfotransferase; estrogen sulfokinase; estrogen sulfotransferase; steroid alcohol sulfotransferase; steroid sulfokinase; steroid sulfotransferase; sterol sulfokinase; sterol sulfotransferase; alcohol/hydroxysteroid sulfotransferase; 3β-hydroxysteroid sulfotransferase; 3′-phosphoadenylyl-sulfate:alcohol sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:alcohol sulfonotransferase
Comments: Primary and secondary alcohols, including aliphatic alcohols, ascorbic acid, chloramphenicol, ephedrine and hydroxysteroids, but not phenolic steroids, can act as acceptors (cf. EC 2.8.2.15 steroid sulfotransferase).
References:
1.  Lyon, E.S. and Jakoby, W.B. The identity of alcohol sulfotransferases with hydroxysteroid sulfotransferases. Arch. Biochem. Biophys. 202 (1980) 474–481. [PMID: 6935986]
2.  Lyon, E.S., Marcus, C.J., Wang, J.-L. and Jakoby, W.B. Hydroxysteroid sulfotransferase. Methods Enzymol. 77 (1981) 206–213. [PMID: 6173569]
[EC 2.8.2.2 created 1961, modified 1980]
 
 
EC 1.1.3.13     Relevance: 31.6%
Accepted name: alcohol oxidase
Reaction: a primary alcohol + O2 = an aldehyde + H2O2
Other name(s): ethanol oxidase; alcohol:oxygen oxidoreductase
Systematic name: alcohol:oxygen oxidoreductase (H2O2-forming)
Comments: The enzymes from the fungi Candida methanosorbosa and several Basidiomycetes species contain an FAD cofactor [1,3]. The enzyme from the phytopathogenic fungi Colletotrichum graminicola and Colletotrichum gloeosporioides utilize a mononuclear copper-radical mechanism [4]. The enzyme acts on primary alcohols and unsaturated alcohols, and has much lower activity with branched-chain and secondary alcohols.
References:
1.  Janssen, F.W. and Ruelius, H.W. Alcohol oxidase, a flavoprotein from several Basidiomycetes species. Crystallization by fractional precipitation with polyethylene glycol. Biochim. Biophys. Acta 151 (1968) 330–342. [PMID: 5636370]
2.  Nishida, A., Ishihara, T. and Hiroi, T. Studies on enzymes related to lignan biodegradation. Baiomasu Henkan Keikaku Kenkyu Hokoku (1987) 38–59. (in Japanese)
3.  Suye, S. Purification and properties of alcohol oxidase from Candida methanosorbosa M-2003. Curr. Microbiol. 34 (1997) 374–377. [PMID: 9142745]
4.  Yin, D.T., Urresti, S., Lafond, M., Johnston, E.M., Derikvand, F., Ciano, L., Berrin, J.G., Henrissat, B., Walton, P.H., Davies, G.J. and Brumer, H. Structure-function characterization reveals new catalytic diversity in the galactose oxidase and glyoxal oxidase family. Nat. Commun. 6:10197 (2015). [PMID: 26680532]
[EC 1.1.3.13 created 1972]
 
 
EC 1.1.2.8     Relevance: 30.9%
Accepted name: alcohol dehydrogenase (cytochrome c)
Reaction: a primary alcohol + 2 ferricytochrome c = an aldehyde + 2 ferrocytochrome c + 2 H+
Other name(s): type I quinoprotein alcohol dehydrogenase; quinoprotein ethanol dehydrogenase
Systematic name: alcohol:cytochrome c oxidoreductase
Comments: A periplasmic PQQ-containing quinoprotein. Occurs in Pseudomonas and Rhodopseudomonas. The enzyme from Pseudomonas aeruginosa uses a specific inducible cytochrome c550 as electron acceptor. Acts on a wide range of primary and secondary alcohols, but not methanol. It has a homodimeric structure [contrasting with the heterotetrameric structure of EC 1.1.2.7, methanol dehydrogenase (cytochrome c)]. It is routinely assayed with phenazine methosulfate as electron acceptor. Activity is stimulated by ammonia or amines. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed ’propeller’ structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ.
References:
1.  Rupp, M. and Gorisch, H. Purification, crystallisation and characterization of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa. Biol. Chem. Hoppe-Seyler 369 (1988) 431–439. [PMID: 3144289]
2.  Toyama, H., Fujii, A., Matsushita, K., Shinagawa, E., Ameyama, M. and Adachi, O. Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols. J. Bacteriol. 177 (1995) 2442–2450. [PMID: 7730276]
3.  Schobert, M. and Gorisch, H. Cytochrome c550 is an essential component of the quinoprotein ethanol oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the genes encoding cytochrome c550 and an adjacent acetaldehyde dehydrogenase. Microbiology 145 (1999) 471–481. [PMID: 10075429]
4.  Keitel, T., Diehl, A., Knaute, T., Stezowski, J.J., Hohne, W. and Gorisch, H. X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity. J. Mol. Biol. 297 (2000) 961–974. [PMID: 10736230]
5.  Kay, C.W., Mennenga, B., Gorisch, H. and Bittl, R. Characterisation of the PQQ cofactor radical in quinoprotein ethanol dehydrogenase of Pseudomonas aeruginosa by electron paramagnetic resonance spectroscopy. FEBS Lett. 564 (2004) 69–72. [PMID: 15094044]
6.  Mennenga, B., Kay, C.W. and Gorisch, H. Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the unusual disulfide ring formed by adjacent cysteine residues is essential for efficient electron transfer to cytochrome c550. Arch. Microbiol. 191 (2009) 361–367. [PMID: 19224199]
[EC 1.1.2.8 created 1972 as EC 1.1.99.8, modified 1982, part transferred 2010 to EC 1.1.2.8]
 
 
EC 1.1.99.36     Relevance: 30.8%
Accepted name: alcohol dehydrogenase (nicotinoprotein)
Reaction: ethanol + acceptor = acetaldehyde + reduced acceptor
Other name(s): NDMA-dependent alcohol dehydrogenase; nicotinoprotein alcohol dehydrogenase; np-ADH; ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase
Systematic name: ethanol:acceptor oxidoreductase
Comments: Contains Zn2+. Nicotinoprotein alcohol dehydrogenases are unique medium-chain dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a tightly bound NAD+/NADH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro. The enzyme from the Gram-positive bacterium Amycolatopsis methanolica can accept many primary alcohols as substrates, including benzylalcohol [1].
References:
1.  Van Ophem, P.W., Van Beeumen, J. and Duine, J.A. Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. Purification and characterization of a novel type from Amycolatopsis methanolica. Eur. J. Biochem. 212 (1993) 819–826. [PMID: 8385013]
2.  Piersma, S.R., Visser, A.J., de Vries, S. and Duine, J.A. Optical spectroscopy of nicotinoprotein alcohol dehydrogenase from Amycolatopsis methanolica: a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase. Biochemistry 37 (1998) 3068–3077. [PMID: 9485460]
3.  Schenkels, P. and Duine, J.A. Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes. Microbiology 146 (2000) 775–785. [PMID: 10784035]
4.  Piersma, S.R., Norin, A., de Vries, S., Jornvall, H. and Duine, J.A. Inhibition of nicotinoprotein (NAD+-containing) alcohol dehydrogenase by trans-4-(N,N-dimethylamino)-cinnamaldehyde binding to the active site. J. Protein Chem. 22 (2003) 457–461. [PMID: 14690248]
5.  Norin, A., Piersma, S.R., Duine, J.A. and Jornvall, H. Nicotinoprotein (NAD+ -containing) alcohol dehydrogenase: structural relationships and functional interpretations. Cell. Mol. Life Sci. 60 (2003) 999–1006. [PMID: 12827287]
[EC 1.1.99.36 created 2010]
 
 
EC 2.5.1.26     Relevance: 30.7%
Accepted name: alkylglycerone-phosphate synthase
Reaction: 1-acyl-glycerone 3-phosphate + a long-chain alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid anion
Glossary: a long-chain alcohol = an alcohol derived from a fatty acid with an aliphatic chain of 13-22 carbons.
Other name(s): alkyldihydroxyacetonephosphate synthase; alkyldihydroxyacetone phosphate synthetase; alkyl DHAP synthetase; alkyl-DHAP; dihydroxyacetone-phosphate acyltransferase (ambiguous); DHAP-AT
Systematic name: 1-acyl-glycerone-3-phosphate:long-chain-alcohol O-3-phospho-2-oxopropanyltransferase
Comments: The ester-linked fatty acid of the substrate is cleaved and replaced by a long-chain alcohol in an ether linkage.
References:
1.  Brown, A.J. and Snyder, F. Alkyldihydroxyacetone-P synthase. Solubilization, partial purification, new assay method, and evidence for a ping-pong mechanism. J. Biol. Chem. 257 (1982) 8835–8839. [PMID: 7096336]
2.  Wykle, R.L., Piantadosi, C. and Snyder, F. The role of acyldihydroxyacetone phosphate, reduced nicotinamide adenine dinucleotide, and reduced nicotinamide adenine dinucleotide phosphate in the biosynthesis of O-alkyl glycerolipids by microsomal enzymes of Ehrlich ascites tumor. J. Biol. Chem. 247 (1972) 2944–2948. [PMID: 4401994]
[EC 2.5.1.26 created 1984]
 
 
EC 2.3.1.224     Relevance: 29%
Accepted name: acetyl-CoA-benzylalcohol acetyltransferase
Reaction: (1) acetyl-CoA + benzyl alcohol = CoA + benzyl acetate
(2) acetyl-CoA + cinnamyl alcohol = CoA + cinnamyl acetate
Other name(s): BEAT
Systematic name: acetyl-CoA:benzylalcohol O-acetyltransferase
Comments: The enzyme is found in flowers like Clarkia breweri, where it is important for floral scent production. Unlike EC 2.3.1.84, alcohol O-acetyltransferase, this enzyme is active with alcohols that contain a benzyl ring.
References:
1.  Dudareva, N., D'Auria, J.C., Nam, K.H., Raguso, R.A. and Pichersky, E. Acetyl-CoA:benzylalcohol acetyltransferase - an enzyme involved in floral scent production in Clarkia breweri. Plant J. 14 (1998) 297–304. [PMID: 9628024]
[EC 2.3.1.224 created 2013]
 
 
EC 2.3.1.75     Relevance: 28.8%
Accepted name: long-chain-alcohol O-fatty-acyltransferase
Reaction: acyl-CoA + a long-chain alcohol = CoA + a long-chain ester
Other name(s): wax synthase; wax-ester synthase
Systematic name: acyl-CoA:long-chain-alcohol O-acyltransferase
Comments: Transfers saturated or unsaturated acyl residues of chain-length C18 to C20 to long-chain alcohols, forming waxes. The best acceptor is cis-icos-11-en-1-ol.
References:
1.  Wu, X.-Y., Moreau, R.A. and Stumpf, P.K. Studies of biosynthesis of waxes by developing jojoba seed. 3. Biosynthesis of wax esters from acyl-CoA and long-chain alcohols. Lipids 16 (1981) 897–902.
[EC 2.3.1.75 created 1984]
 
 
EC 1.1.1.184     Relevance: 27.9%
Accepted name: carbonyl reductase (NADPH)
Reaction: R-CHOH-R′ + NADP+ = R-CO-R′ + NADPH + H+
Other name(s): aldehyde reductase 1; prostaglandin 9-ketoreductase; xenobiotic ketone reductase; NADPH-dependent carbonyl reductase; ALR3; carbonyl reductase; nonspecific NADPH-dependent carbonyl reductase; carbonyl reductase (NADPH2)
Systematic name: secondary-alcohol:NADP+ oxidoreductase
Comments: Acts on a wide range of carbonyl compounds, including quinones, aromatic aldehydes, ketoaldehydes, daunorubicin and prostaglandins E and F, reducing them to the corresponding alcohol. Si-specific with respect to NADPH [cf. EC 1.1.1.2 alcohol dehydrogenase (NADP+)].
References:
1.  Ahmed, N.K., Felsted, R.L. and Bachur, N.R. Heterogeneity of anthracycline antibiotic carbonyl reductases in mammalian livers. Biochem. Pharmacol. 27 (1978) 2713–2719. [PMID: 31888]
2.  Lin, Y.M. and Jarabak, J. Isolation of two proteins with 9-ketoprostaglandin reductase and NADP-linked 15-hydroxyprostaglandin dehydrogenase activities and studies on their inhibition. Biochem. Biophys. Res. Commun. 81 (1978) 1227–1234. [PMID: 666816]
3.  Wermuth, B. Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase. J. Biol. Chem. 256 (1981) 1206–1213. [PMID: 7005231]
[EC 1.1.1.184 created 1983]
 
 
EC 1.1.5.5     Relevance: 27.7%
Accepted name: alcohol dehydrogenase (quinone)
Reaction: ethanol + ubiquinone = acetaldehyde + ubiquinol
Other name(s): type III ADH; membrane associated quinohaemoprotein alcohol dehydrogenase
Systematic name: alcohol:quinone oxidoreductase
Comments: Only described in acetic acid bacteria where it is involved in acetic acid production. Associated with membrane. Electron acceptor is membrane ubiquinone. A model structure suggests that, like all other quinoprotein alcohol dehydrogenases, the catalytic subunit has an 8-bladed ‘propeller’ structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ; the catalytic subunit also has a heme c in the C-terminal domain. The enzyme has two additional subunits, one of which contains three molecules of heme c. It does not require amines for activation. It has a restricted substrate specificity, oxidizing a few primary alcohols (C2 to C6), but not methanol, secondary alcohols and some aldehydes. It is assayed with phenazine methosulfate or with ferricyanide.
References:
1.  Gomez-Manzo, S., Contreras-Zentella, M., Gonzalez-Valdez, A., Sosa-Torres, M., Arreguin-Espinoza, R. and Escamilla-Marvan, E. The PQQ-alcohol dehydrogenase of Gluconacetobacter diazotrophicus. Int. J. Food Microbiol. 125 (2008) 71–78. [PMID: 18321602]
2.  Shinagawa, E., Toyama, H., Matsushita, K., Tuitemwong, P., Theeragool, G. and Adachi, O. A novel type of formaldehyde-oxidizing enzyme from the membrane of Acetobacter sp. SKU 14. Biosci. Biotechnol. Biochem. 70 (2006) 850–857. [PMID: 16636451]
3.  Chinnawirotpisan, P., Theeragool, G., Limtong, S., Toyama, H., Adachi, O.O. and Matsushita, K. Quinoprotein alcohol dehydrogenase is involved in catabolic acetate production, while NAD-dependent alcohol dehydrogenase in ethanol assimilation in Acetobacter pasteurianus SKU1108. J. Biosci. Bioeng. 96 (2003) 564–571. [PMID: 16233574]
4.  Frebortova, J., Matsushita, K., Arata, H. and Adachi, O. Intramolecular electron transport in quinoprotein alcohol dehydrogenase of Acetobacter methanolicus: a redox-titration stud. Biochim. Biophys. Acta 1363 (1998) 24–34. [PMID: 9526036]
5.  Matsushita, K., Kobayashi, Y., Mizuguchi, M., Toyama, H., Adachi, O., Sakamoto, K. and Miyoshi, H. A tightly bound quinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase of an acetic acid bacterium, Gluconobacter suboxydans. Biosci. Biotechnol. Biochem. 72 (2008) 2723–2731. [PMID: 18838797]
6.  Matsushita, K., Yakushi, T., Toyama, H., Shinagawa, E. and Adachi, O. Function of multiple heme c moieties in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter suboxydans. J. Biol. Chem. 271 (1996) 4850–4857. [PMID: 8617755]
7.  Matsushita, K., Takaki, Y., Shinagawa, E., Ameyama, M. and Adachi, O. Ethanol oxidase respiratory chain of acetic acid bacteria. Reactivity with ubiquinone of pyrroloquinoline quinone-dependent alcohol dehydrogenases purified from Acetobacter aceti and Gluconobacter suboxydans. Biosci. Biotechnol. Biochem. 56 (1992) 304–310.
8.  Matsushita, K., Toyama, H. and Adachi, O. Respiratory chains and bioenergetics of acetic acid bacteria. Adv. Microb. Physiol. 36 (1994) 247–301. [PMID: 7942316]
9.  Cozier, G.E., Giles, I.G. and Anthony, C. The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens. Biochem. J. 308 (1995) 375–379. [PMID: 7772016]
[EC 1.1.5.5 created 2009, modified 2010]
 
 
EC 1.1.1.225     Relevance: 27.7%
Accepted name: chlordecone reductase
Reaction: chlordecone alcohol + NADP+ = chlordecone + NADPH + H+
Other name(s): CDR
Systematic name: chlordecone-alcohol:NADP+ 2-oxidoreductase
Comments: Chlordecone is an organochlorine pesticide.
References:
1.  Molowa, D.T., Shayne, A.G. and Guzelian, P.S. Purification and characterization of chlordecone reductase from human liver. J. Biol. Chem. 261 (1986) 12624–12627. [PMID: 2427522]
[EC 1.1.1.225 created 1989]
 
 
EC 3.7.1.7     Relevance: 26.7%
Accepted name: β-diketone hydrolase
Reaction: nonane-4,6-dione + H2O = pentan-2-one + butanoate
Other name(s): oxidized PVA hydrolase
Systematic name: nonane-4,6-dione acylhydrolase
Comments: Also acts on the product of the action of EC 1.1.3.18 secondary-alcohol oxidase, on polyvinyl alcohols; involved in the bacterial degradation of polyvinyl alcohol.
References:
1.  Sakai, K., Hamada, N. and Watanabe, Y. Separation of secondary alcohol oxidase and oxidized poly(vinyl alcohol) hydrolase by hydrophobic and dye-ligand chromatographies. Agric. Biol. Chem. 47 (1983) 153–155.
2.  Sakai, K., Hamada, N. and Watanabe, Y. A new enzyme, β-diketone hydrolase: a component of a poly(vinyl alcohol)-degrading enzyme preparation. Agric. Biol. Chem. 49 (1985) 1901–1902.
[EC 3.7.1.7 created 1989]
 
 
EC 1.2.1.84     Relevance: 25.9%
Accepted name: alcohol-forming fatty acyl-CoA reductase
Reaction: a long-chain acyl-CoA + 2 NADPH + 2 H+ = a long-chain alcohol + 2 NADP+ + CoA
Glossary: a long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 13 to 22 carbon atoms.
Other name(s): FAR (gene name); long-chain acyl-CoA:NADPH reductase
Systematic name: NADPH:long-chain acyl-CoA reductase
Comments: The enzyme has been characterized from the plant Simmondsia chinensis (jojoba). The alcohol is formed by a four-electron reduction of fatty acyl-CoA. Although the reaction proceeds through an aldehyde intermediate, a free aldehyde is not released. The recombinant enzyme was shown to accept saturated and mono-unsaturated fatty acyl-CoAs of 16 to 22 carbons.
References:
1.  Metz, J.G., Pollard, M.R., Anderson, L., Hayes, T.R. and Lassner, M.W. Purification of a jojoba embryo fatty acyl-coenzyme A reductase and expression of its cDNA in high erucic acid rapeseed. Plant Physiol. 122 (2000) 635–644. [PMID: 10712526]
[EC 1.2.1.84 created 2012]
 
 
EC 1.1.99.20     Relevance: 23.2%
Accepted name: alkan-1-ol dehydrogenase (acceptor)
Reaction: primary alcohol + acceptor = aldehyde + reduced acceptor
Other name(s): polyethylene glycol dehydrogenase; alkan-1-ol:(acceptor) oxidoreductase
Systematic name: alkan-1-ol:acceptor oxidoreductase
Comments: A quinoprotein. Acts on C3-C16 linear-chain saturated primary alcohols, C4-C7 aldehydes and on non-ionic surfactants containing polyethylene glycol residues, such as Tween 40 and 60, but not on methanol and only very slowly on ethanol. 2,6-Dichloroindophenol can act as acceptor. cf. EC 1.1.99.8 alcohol dehydrogenase (acceptor).
References:
1.  Kawai, F., Kimura, T., Tani, Y., Yamada, H., Ueno, T. and Fukami, H. Identification of reaction-products of polyethylene-glycol dehydrogenase. Agric. Biol. Chem. 47 (1983) 1669–1671.
2.  Kawai, F., Yamanaka, H., Ameyama, M., Shinagawa, E., Matsushita, K. and Adachi, O. Identification of the prosthetic group and further characterization of a novel enzyme, polyethylene-glycol dehydrogenase. Agric. Biol. Chem. 49 (1985) 1071–1076.
[EC 1.1.99.20 created 1989]
 
 
EC 3.6.1.53     Relevance: 23%
Accepted name: Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase
Reaction: (1) CDP-choline + H2O = CMP + phosphocholine
(2) ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate
Other name(s): Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase; ADPRibase-Mn
Systematic name: CDP-choline phosphohydrolase
Comments: Requires Mn2+. Unlike EC 3.6.1.13, ADP-ribose diphosphatase, it cannot utilize Mg2+. ADP-D-ribose, CDP-choline, CDP-ethanolamine and ADP are substrates for this enzyme but ADP-D-glucose, UDP-D-glucose, CDP-D-glucose, CDP, CMP and AMP are not hydrolysed [2]. The mammalian enzyme hydrolyses cyclic ADP-ribose to 1-(5-phospho-β-D-ribosyl)-AMP with ~100-fold lower efficiency than ADP-D-ribose [3]. In rat, the enzyme is found predominantly in thymus and spleen.
References:
1.  Canales, J., Pinto, R.M., Costas, M.J., Hernández, M.T., Miró, A., Bernet, D., Fernández, A. and Cameselle, J.C. Rat liver nucleoside diphosphosugar or diphosphoalcohol pyrophosphatases different from nucleotide pyrophosphatase or phosphodiesterase I: substrate specificities of Mg2+-and/or Mn2+-dependent hydrolases acting on ADP-ribose. Biochim. Biophys. Acta 1246 (1995) 167–177. [PMID: 7819284]
2.  Canales, J., Fernández, A., Ribeiro, J.M., Cabezas, A., Rodrigues, J.R., Cameselle, J.C. and Costas, M.J. Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase: a novel metallophosphoesterase family preferentially expressed in rodent immune cells. Biochem. J. 413 (2008) 103–113. [PMID: 18352857]
3.  Canales, J., Fernandez, A., Rodrigues, J.R., Ferreira, R., Ribeiro, J.M., Cabezas, A., Costas, M.J. and Cameselle, J.C. Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn(2+)-dependent ADP-ribose/CDP-alcohol pyrophosphatase. FEBS Lett. 583 (2009) 1593–1598. [PMID: 19379742]
4.  Rodrigues, J.R., Fernandez, A., Canales, J., Cabezas, A., Ribeiro, J.M., Costas, M.J. and Cameselle, J.C. Characterization of Danio rerio Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase, the structural prototype of the ADPRibase-Mn-like protein family. PLoS One 7:e42249 (2012). [PMID: 22848751]
[EC 3.6.1.53 created 2008]
 
 
EC 2.3.1.152     Relevance: 22.9%
Accepted name: alcohol O-cinnamoyltransferase
Reaction: 1-O-trans-cinnamoyl-β-D-glucopyranose + ROH = alkyl cinnamate + glucose
Systematic name: 1-O-trans-cinnamoyl-β-D-glucopyranose:alcohol O-cinnamoyltransferase
Comments: Acceptor alcohols (ROH) include methanol, ethanol and propanol. No cofactors are required as 1-O-trans-cinnamoyl-β-D-glucopyranose itself is an "energy-rich" (activated) acyl-donor, comparable to CoA-thioesters. 1-O-trans-Cinnamoyl-β-D-gentobiose can also act as the acyl donor, but with much less affinity.
References:
1.  Mock, H.-P., Strack, D. Energetics of uridine 5′-diphosphoglucose-hydroxy-cinnamic acid acyl-glucotransferase reaction. Phytochemistry 32 (1993) 575–579.
2.  Latza, S., Gansser, D., Berger, R.G. Carbohydrate esters of cinnamic acid from fruits of Physalis peruviana, Psidium guajava and Vaccinium vitis IDAEA. Phytochemistry 43 (1996) 481–485.
[EC 2.3.1.152 created 1999]
 
 
EC 1.1.1.223     Relevance: 22.9%
Accepted name: isopiperitenol dehydrogenase
Reaction: (-)-trans-isopiperitenol + NAD+ = (-)-isopiperitenone + NADH + H+
Systematic name: (-)-trans-isopiperitenol:NAD+ oxidoreductase
Comments: Acts on (-)-trans-isopiperitenol, (+)-trans-piperitenol and (+)-trans-pulegol. Involved in the biosynthesis of menthol and related monoterpenes in peppermint (Mentha piperita) leaves.
References:
1.  Kjonaas, R.B., Venkatachalam, K.V. and Croteau, R. Metabolism of monoterpenes: oxidation of isopiperitenol to isopiperitenone, and subsequent isomerization to piperitenone by soluble enzyme preparations from peppermint (Mentha piperita) leaves. Arch. Biochem. Biophys. 238 (1985) 49–60. [PMID: 3885858]
[EC 1.1.1.223 created 1989]
 
 
EC 2.8.2.15     Relevance: 22.3%
Accepted name: steroid sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + a phenolic steroid = adenosine 3′,5′-bisphosphate + steroid O-sulfate
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): steroid alcohol sulfotransferase; 3′-phosphoadenylyl-sulfate:phenolic-steroid sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:phenolic-steroid sulfonotransferase
Comments: Broad specificity resembling EC 2.8.2.2 alcohol sulfotransferase, but also acts on estrone.
References:
1.  Adams, J.B. and McDonald, D. Enzymic synthesis of steroid sulphates. XIII. Isolation and properties of dehydroepiandrosterone sulphotransferase from human foetal adrenals. Biochim. Biophys. Acta 615 (1980) 275–278. [PMID: 6932974]
[EC 2.8.2.15 created 1984]
 
 
EC 1.17.9.1     Relevance: 22.2%
Accepted name: 4-methylphenol dehydrogenase (hydroxylating)
Reaction: 4-methylphenol + 4 oxidized azurin + H2O = 4-hydroxybenzaldehyde + 4 reduced azurin + 4 H+ (overall reaction)
(1a) 4-methylphenol + 2 oxidized azurin + H2O = 4-hydroxybenzyl alcohol + 2 reduced azurin + 2 H+
(1b) 4-hydroxybenzyl alcohol + 2 oxidized azurin = 4-hydroxybenzaldehyde + 2 reduced azurin + 2 H+
Glossary: 4-methylphenol = 4-cresol = p-cresol
Other name(s): pchCF (gene names); p-cresol-(acceptor) oxidoreductase (hydroxylating); p-cresol methylhydroxylase; 4-cresol dehydrogenase (hydroxylating)
Systematic name: 4-methylphenol:oxidized azurin oxidoreductase (methyl-hydroxylating)
Comments: This bacterial enzyme contains a flavin (FAD) subunit and a cytochrome c subunit. The flavin subunit abstracts two hydrogen atoms from the substrate, forming a quinone methide intermediate, then hydrates the latter at the benzylic carbon with a hydroxyl group derived from water. The protons are lost to the bulk solvent, while the electrons are passed to the heme on the cytochrome subunit, and from there to azurin, a small copper-binding protein that is co-localized with the enzyme in the periplasm. The first hydroxylation forms 4-hydroxybenzyl alcohol; a second hydroxylation converts this into 4-hydroxybenzaldehyde.
References:
1.  Hopper, D.J. and Taylor, D.G. The purification and properties of p-cresol-(acceptor) oxidoreductase (hydroxylating), a flavocytochrome from Pseudomonas putida. Biochem. J. 167 (1977) 155–162. [PMID: 588247]
2.  McIntire, W., Edmondson, D.E. and Singer, T.P. 8α-O-Tyrosyl-FAD: a new form of covalently bound flavin from p-cresol methylhydroxylase. J. Biol. Chem. 255 (1980) 6553–6555. [PMID: 7391034]
3.  Hopper, D.J., Jones, M.R. and Causer, M.J. Periplasmic location of p-cresol methylhydroxylase in Pseudomonas putida. FEBS Lett. 182 (1985) 485–488. [PMID: 3920077]
4.  Bossert, I.D., Whited, G., Gibson, D.T. and Young, L.Y. Anaerobic oxidation of p-cresol mediated by a partially purified methylhydroxylase from a denitrifying bacterium. J. Bacteriol. 171 (1989) 2956–2962. [PMID: 2722739]
5.  Reeve, C.D., Carver, M.A. and Hopper, D.J. Stereochemical aspects of the oxidation of 4-ethylphenol by the bacterial enzyme 4-ethylphenol methylenehydroxylase. Biochem. J. 269 (1990) 815–819. [PMID: 1697166]
6.  Peters, F., Heintz, D., Johannes, J., van Dorsselaer, A. and Boll, M. Genes, enzymes, and regulation of para-cresol metabolism in Geobacter metallireducens. J. Bacteriol. 189 (2007) 4729–4738. [PMID: 17449613]
7.  Johannes, J., Bluschke, A., Jehmlich, N., von Bergen, M. and Boll, M. Purification and characterization of active-site components of the putative p-cresol methylhydroxylase membrane complex from Geobacter metallireducens. J. Bacteriol. 190 (2008) 6493–6500. [PMID: 18658262]
[EC 1.17.9.1 created 1983 as EC 1.17.99.1, modified 2001, modified 2011, modified 2015, transferred 2018 to EC 1.17.9.1]
 
 
EC 1.14.15.26     Relevance: 22%
Accepted name: toluene methyl-monooxygenase
Reaction: (1) toluene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = benzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(2) p-xylene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = 4-methylbenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(3) m-xylene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = 3-methylbenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Glossary: toluene = methylbenzene
p-xylene = 1,4-dimethylbenzene
m-xylene = 1,3-dimethylbenzene
Other name(s): xylM (gene names); ntnM (gene names)
Systematic name: methylbenzene,ferredoxin:oxygen oxidoreductase (methyl-hydroxylating)
Comments: The enzyme, characterized from several Pseudomonas strains, catalyses the first step in the degradation of toluenes and xylenes. It has a broad substrate specificity and is also active with substituted compounds, such as chlorotoluenes. The electrons are provided by a reductase (EC 1.18.1.3, ferredoxin—NAD+ reductase) that transfers electrons from NADH via FAD and an [2Fe-2S] cluster. The enzyme can also act on its products, producing gem-diols that spontaneously dehydrate to form aldehydes.
References:
1.  Suzuki, M., Hayakawa, T., Shaw, J.P., Rekik, M. and Harayama, S. Primary structure of xylene monooxygenase: similarities to and differences from the alkane hydroxylation system. J. Bacteriol. 173 (1991) 1690–1695. [PMID: 1999388]
2.  Shaw, J.P. and Harayama, S. Purification and characterisation of the NADH:acceptor reductase component of xylene monooxygenase encoded by the TOL plasmid pWW0 of Pseudomonas putida mt-2. Eur. J. Biochem. 209 (1992) 51–61. [PMID: 1327782]
3.  Brinkmann, U. and Reineke, W. Degradation of chlorotoluenes by in vivo constructed hybrid strains: problems of enzyme specificity, induction and prevention of meta-pathway. FEMS Microbiol. Lett. 75 (1992) 81–87. [PMID: 1526468]
4.  James, K.D. and Williams, P.A. ntn genes determining the early steps in the divergent catabolism of 4-nitrotoluene and toluene in Pseudomonas sp. strain TW3. J. Bacteriol. 180 (1998) 2043–2049. [PMID: 9555884]
[EC 1.14.15.26 created 2018]
 
 
EC 4.2.3.186     Relevance: 21.8%
Accepted name: ent-13-epi-manoyl oxide synthase
Reaction: ent-8α-hydroxylabd-13-en-15-yl diphosphate = ent-13-epi-manoyl oxide + diphosphate
Glossary: Ent-13-epi-manoyl oxide = (13R)-ent-8,13-epoxylabd-14-ene
Other name(s): SmKSL2; ent-LDPP synthase
Systematic name: ent-8α-hydroxylabd-13-en-15-yl-diphosphate diphosphate-lyase (cyclizing, ent-13-epi-manoyl-oxide-forming)
Comments: Isolated from the plant Salvia miltiorrhiza (red sage).
References:
1.  Cui, G., Duan, L., Jin, B., Qian, J., Xue, Z., Shen, G., Snyder, J.H., Song, J., Chen, S., Huang, L., Peters, R.J. and Qi, X. Functional divergence of diterpene syntheses in the medicinal plant Salvia miltiorrhiza. Plant Physiol. 169 (2015) 1607–1618. [PMID: 26077765]
[EC 4.2.3.186 created 2017]
 
 
EC 5.5.1.28     Relevance: 21.8%
Accepted name: (–)-kolavenyl diphosphate synthase
Reaction: geranylgeranyl diphosphate = (–)-kolavenyl diphosphate
Glossary: (–)-kolavenyl diphosphate = (2E)-5-[(1R,2S,4aS,8aS)-1,2,4a,5-tetramethyl-1,2,3,4,4a,7,8,8a-octahydronaphthalen-1-yl]-3-methylpent-2-en-1-yl diposphate
Other name(s): SdKPS; TwTPS14; TwTPS10/KPS; SdCPS2; clerodienyl diphosphate synthase; CLPP
Systematic name: (–)-kolavenyl diphosphate lyase (ring-opening)
Comments: Isolated from the hallucinogenic plant Salvia divinorum (seer’s sage) and the medicinal plant Tripterygium wilfordii (thunder god vine).
References:
1.  Hansen, N.L., Heskes, A.M., Hamberger, B., Olsen, C.E., Hallstrom, B.M., Andersen-Ranberg, J. and Hamberger, B. The terpene synthase gene family in Tripterygium wilfordii harbors a labdane-type diterpene synthase among the monoterpene synthase TPS-b subfamily. Plant J. 89 (2017) 429–441. [PMID: 27801964]
2.  Chen, X., Berim, A., Dayan, F.E. and Gang, D.R. A (–)-kolavenyl diphosphate synthase catalyzes the first step of salvinorin A biosynthesis in Salvia divinorum. J. Exp. Bot. 68 (2017) 1109–1122. [PMID: 28204567]
[EC 5.5.1.28 created 2017]
 
 
EC 1.14.13.158      
Transferred entry: amorpha-4,11-diene 12-monooxygenase. Now EC 1.14.14.114, amorpha-4,11-diene 12-monooxygenase.
[EC 1.14.13.158 created 2012, deleted 2018]
 
 
EC 4.2.3.95     Relevance: 21.7%
Accepted name: (-)-α-cuprenene synthase
Reaction: (2E,6E)-farnesyl diphosphate = (-)-α-cuprenene + diphosphate
Other name(s): Cop6
Systematic name: (-)-α-cuprenene hydrolase [cyclizing, (-)-α-cuprenene-forming]
Comments: The enzyme from the fungus Coprinopsis cinerea produces (-)-α-cuprenene with high selectivity.
References:
1.  Lopez-Gallego, F., Agger, S.A., Abate-Pella, D., Distefano, M.D. and Schmidt-Dannert, C. Sesquiterpene synthases Cop4 and Cop6 from Coprinus cinereus: catalytic promiscuity and cyclization of farnesyl pyrophosphate geometric isomers. ChemBioChem 11 (2010) 1093–1106. [PMID: 20419721]
[EC 4.2.3.95 created 2012]
 
 
EC 4.2.3.6     Relevance: 21%
Accepted name: trichodiene synthase
Reaction: (2E,6E)-farnesyl diphosphate = trichodiene + diphosphate
Other name(s): trichodiene synthetase; sesquiterpene cyclase; trans,trans-farnesyl-diphosphate sesquiterpenoid-lyase
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, trichodiene-forming)
References:
1.  Hohn, T.M. and Vanmiddlesworth, F. Purification and characterization of the sesquiterpene cyclase trichodiene synthetase from Fusarium sporotrichioides. Arch. Biochem. Biophys. 251 (1986) 756–761. [PMID: 3800398]
2.  Hohn, T.M. and Beremand, P.D. Isolation and nucleotide sequence of a sesquiterpene cyclase gene from the trichothecene-producing fungus Fusarium sporotrichioides. Gene 79 (1989) 131–138. [PMID: 2777086]
3.  Rynkiewicz, M.J., Cane, D.E. and Christianson, D.W. Structure of trichodiene synthase from Fusarium sporotrichioides provides mechanistic inferences on the terpene cyclization cascade. Proc. Natl. Acad. Sci. USA 98 (2001) 13543–13548. [PMID: 11698643]
[EC 4.2.3.6 created 1989 as EC 4.1.99.6, transferred 2000 to EC 4.2.3.6]
 
 
EC 1.3.99.25     Relevance: 20.7%
Accepted name: carvone reductase
Reaction: (1) (+)-dihydrocarvone + acceptor = (–)-carvone + reduced acceptor
(2) (–)-isodihydrocarvone + acceptor = (+)-carvone + reduced acceptor
Glossary: (+)-dihydrocarvone = (1S,4R)-menth-8-en-2-one
(+)-isodihydrocarvone = (1S,4R)-menth-8-en-2-one
(–)-carvone = (4R)-mentha-1(6),8-dien-6-one = (5R)-2-methyl-5-(prop-1-en-2-yl)cyclohex-2-en-1-one
Systematic name: (+)-dihydrocarvone:acceptor 1,6-oxidoreductase
Comments: This enzyme participates in the carveol and dihydrocarveol degradation pathway of the Gram-positive bacterium Rhodococcus erythropolis DCL14. The enzyme has not been purified, and requires an unknown cofactor, which is different from NAD+, NADP+ or a flavin.
References:
1.  van der Werf, M.J. and Boot, A.M. Metabolism of carveol and dihydrocarveol in Rhodococcus erythropolis DCL14. Microbiology 146 (2000) 1129–1141. [PMID: 10832640]
[EC 1.3.99.25 created 2008]
 
 
EC 1.1.1.296     Relevance: 20.5%
Accepted name: dihydrocarveol dehydrogenase
Reaction: menth-8-en-2-ol + NAD+ = menth-8-en-2-one + NADH + H+
Glossary: (+)-dihydrocarveol = (1S,2S,4S)-menth-8-en-2-ol
(+)-isodihydrocarveol = (1S,2S,4R)-menth-8-en-2-ol
(+)-neoisodihydrocarveol = (1S,2R,4R)-menth-8-en-2-ol
(–)-dihydrocarvone = (1S,4S)-menth-8-en-2-one
(+)-isodihydrocarvone = (1S,4R)-menth-8-en-2-one
Other name(s): carveol dehydrogenase (ambiguous)
Systematic name: menth-8-en-2-ol:NAD+ oxidoreductase
Comments: This enzyme from the Gram-positive bacterium Rhodococcus erythropolis DCL14 forms part of the carveol and dihydrocarveol degradation pathway. The enzyme accepts all eight stereoisomers of menth-8-en-2-ol as substrate, although some isomers are converted faster than others. The preferred substrates are (+)-neoisodihydrocarveol, (+)-isodihydrocarveol, (+)-dihydrocarveol and (–)-isodihydrocarveol.
References:
1.  van der Werf, M.J. and Boot, A.M. Metabolism of carveol and dihydrocarveol in Rhodococcus erythropolis DCL14. Microbiology 146 (2000) 1129–1141. [PMID: 10832640]
[EC 1.1.1.296 created 2008]
 
 
EC 1.23.1.3     Relevance: 19.8%
Accepted name: (–)-pinoresinol reductase
Reaction: (–)-lariciresinol + NADP+ = (–)-pinoresinol + NADPH + H+
Glossary: (–)-lariciresinol = 4-[(2R,3S,4S)-4-[(4-hydroxy-3-methoxyphenyl)methyl]-3-(hydroxymethyl)oxolan-2-yl]-2-methoxyphenol
(–)-pinoresinol = (1R,3aS,4R,6aS)-4,4′-(tetrahydro-1H,3H-furo[3,4-c]furan-1,4-diyl)bis(2-methoxyphenol)
Other name(s): pinoresinol/lariciresinol reductase; pinoresinol-lariciresinol reductases; (–)-pinoresinol-(–)-lariciresinol reductase; PLR
Systematic name: (–)-lariciresinol:NADP+ oxidoreductase
Comments: The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that usually further reduces the product to (+)-secoisolariciresinol [EC 1.23.1.4, (–)-lariciresinol reductase]. Isolated from the plants Thuja plicata (western red cedar) [1], Linum perenne (perennial flax) [2] and Arabidopsis thaliana (thale cress) [3].
References:
1.  Fujita, M., Gang, D.R., Davin, L.B. and Lewis, N.G. Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions. J. Biol. Chem. 274 (1999) 618–627. [PMID: 9872995]
2.  Hemmati, S., Schmidt, T.J. and Fuss, E. (+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B. FEBS Lett. 581 (2007) 603–610. [PMID: 17257599]
3.  Nakatsubo, T., Mizutani, M., Suzuki, S., Hattori, T. and Umezawa, T. Characterization of Arabidopsis thaliana pinoresinol reductase, a new type of enzyme involved in lignan biosynthesis. J. Biol. Chem. 283 (2008) 15550–15557. [PMID: 18347017]
[EC 1.23.1.3 created 2013]
 
 
EC 1.1.1.284     Relevance: 19.7%
Accepted name: S-(hydroxymethyl)glutathione dehydrogenase
Reaction: S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H + H+
Other name(s): NAD-linked formaldehyde dehydrogenase (incorrect); formaldehyde dehydrogenase (incorrect); formic dehydrogenase (incorrect); class III alcohol dehydrogenase; ADH3; χ-ADH; FDH (incorrect); formaldehyde dehydrogenase (glutathione) (incorrect); GS-FDH (incorrect); glutathione-dependent formaldehyde dehydrogenase (incorrect); GD-FALDH; NAD- and glutathione-dependent formaldehyde dehydrogenase; NAD-dependent formaldehyde dehydrogenase (incorrect)
Systematic name: S-(hydroxymethyl)glutathione:NAD+ oxidoreductase
Comments: The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC 4.4.1.22, S-(hydroxymethyl)glutathione synthase. This enzyme forms part of the pathway that detoxifies formaldehyde, since the product is hydrolysed by EC 3.1.2.12, S-formylglutathione hydrolase. The human enzyme belongs to the family of zinc-dependent alcohol dehydrogenases. Also specifically reduces S-nitrosylglutathione.
References:
1.  Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 203–221.
2.  Rose, Z.B. and Racker, E. Formaldehyde dehydrogenase. Methods Enzymol. 9 (1966) 357–360.
3.  Liu, L., Hausladen, A., Zeng, M., Que, L., Heitman, J. and Stamler, J.S. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410 (2001) 490–494. [PMID: 11260719]
4.  Sanghani, P.C., Stone, C.L., Ray, B.D., Pindel, E.V., Hurley, T.D. and Bosron, W.F. Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase. Biochemistry 39 (2000) 10720–10729. [PMID: 10978156]
5.  van Ophem, P.W. and Duine, J.A. NAD- and co-substrate (GSH or factor)-dependent formaldehyde dehydrogenases from methylotrophic microorganisms act as a class III alcohol dehydrogenase. FEMS Microbiol. Lett. 116 (1994) 87–94.
6.  Ras, J., van Ophem, P.W., Reijnders, W.N., Van Spanning, R.J., Duine, J.A., Stouthamer, A.H. and Harms, N. Isolation, sequencing, and mutagenesis of the gene encoding NAD- and glutathione-dependent formaldehyde dehydrogenase (GD-FALDH) from Paracoccus denitrificans, in which GD-FALDH is essential for methylotrophic growth. J. Bacteriol. 177 (1995) 247–251. [PMID: 7798140]
7.  Barber, R.D., Rott, M.A. and Donohue, T.J. Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides. J. Bacteriol. 178 (1996) 1386–1393. [PMID: 8631716]
[EC 1.1.1.284 created 2005 (EC 1.2.1.1 created 1961, modified 1982, modified 2002, part transferred 2005 to EC 1.1.1.284)]
 
 
EC 1.3.1.82     Relevance: 19.7%
Accepted name: (-)-isopiperitenone reductase
Reaction: (+)-cis-isopulegone + NADP+ = (-)-isopiperitenone + NADPH + H+
Systematic name: (+)-cis-isopulegone:NADP+ oxidoreductase
Comments: The reaction occurs in the opposite direction to that shown above. The enzyme participates in the menthol-biosynthesis pathway of Mentha plants. (+)-Pulegone, (+)-cis-isopulegone and (-)-menthone are not substrates. The enzyme has a preference for NADPH as the reductant, with NADH being a poor substitute [2]. The enzyme is highly regioselective for the reduction of the endocyclic 1,2-double bond, and is stereoselective, producing only the 1R-configured product. It is a member of the short-chain dehydrogenase/reductase superfamily.
References:
1.  Croteau, R. and Venkatachalam, K.V. Metabolism of monoterpenes: demonstration that (+)-cis-isopulegone, not piperitenone, is the key intermediate in the conversion of (-)-isopiperitenone to (+)-pulegone in peppermint (Mentha piperita). Arch. Biochem. Biophys. 249 (1986) 306–315. [PMID: 3755881]
2.  Ringer, K.L., McConkey, M.E., Davis, E.M., Rushing, G.W. and Croteau, R. Monoterpene double-bond reductases of the (-)-menthol biosynthetic pathway: isolation and characterization of cDNAs encoding (-)-isopiperitenone reductase and (+)-pulegone reductase of peppermint. Arch. Biochem. Biophys. 418 (2003) 80–92. [PMID: 13679086]
[EC 1.3.1.82 created 2008]
 
 
EC 2.3.1.232     Relevance: 19.5%
Accepted name: methanol O-anthraniloyltransferase
Reaction: anthraniloyl-CoA + methanol = CoA + O-methyl anthranilate
Glossary: anthraniloyl-CoA = 2-aminobenzoyl-CoA
Other name(s): AMAT; anthraniloyl-coenzyme A (CoA):methanol acyltransferase
Systematic name: anthraniloyl-CoA:methanol O-anthraniloyltransferase
Comments: The enzyme from Concord grape (Vitis labrusca) is solely responsible for the production of O-methyl anthranilate, an important aroma and flavor compound in the grape. The enzyme has a broad substrate specificity, and can use a range of alcohols with substantial activity, the best being butanol, benzyl alcohol, iso-pentanol, octanol and 2-propanol. It can use benzoyl-CoA and acetyl-CoA as acyl donors with lower efficiency. In addition to O-methyl anthranilate, the enzyme might be responsible for the production of ethyl butanoate, methyl-3-hydroxy butanoate and ethyl-3-hydroxy butanoate, which are present in large quantities in the grapes. Also catalyses EC 2.3.1.196, benzyl alcohol O-benzoyltransferase.
References:
1.  Wang, J. and De Luca, V. The biosynthesis and regulation of biosynthesis of Concord grape fruit esters, including ’foxy’ methylanthranilate. Plant J. 44 (2005) 606–619. [PMID: 16262710]
[EC 2.3.1.232 created 2014]
 
 
EC 2.7.8.34     Relevance: 19.4%
Accepted name: CDP-L-myo-inositol myo-inositolphosphotransferase
Reaction: CDP-1L-myo-inositol + 1L-myo-inositol 1-phosphate = CMP + bis(1L-myo-inositol) 3,1′-phosphate 1-phosphate
Glossary: 1L-myo-inositol 1-phosphate = 1D-myo-inositol 3-phosphate
Other name(s): CDP-inositol:inositol-1-phosphate transferase (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)); DIPPS (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS))
Systematic name: CDP-1L-myo-inositol:1L-myo-inositol 1-phosphate myo-inositolphosphotransferase
Comments: In many organisms this activity is catalysed by a bifunctional enzyme. The di-myo-inositol-1,3′-phosphate-1′-phosphate synthase domain of the bifunctional EC 2.7.7.74/EC 2.7.8.34 (CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase) uses only 1L-myo-inositol 1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-1L-myo-inositol and CDP-D-myo-inositol, are recognized as alcohol donors. The enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3-phosphate, a widespread organic solute in microorganisms adapted to hot environments.
References:
1.  Rodrigues, M.V., Borges, N., Henriques, M., Lamosa, P., Ventura, R., Fernandes, C., Empadinhas, N., Maycock, C., da Costa, M.S. and Santos, H. Bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase, the key enzyme for di-myo-inositol-phosphate synthesis in several (hyper)thermophiles. J. Bacteriol. 189 (2007) 5405–5412. [PMID: 17526717]
[EC 2.7.8.34 created 2011]
 
 
EC 3.1.1.83     Relevance: 19.4%
Accepted name: monoterpene ε-lactone hydrolase
Reaction: (1) isoprop(en)ylmethyloxepan-2-one + H2O = 6-hydroxyisoprop(en)ylmethylhexanoate (general reaction)
(2) 4-isopropenyl-7-methyloxepan-2-one + H2O = 6-hydroxy-3-isopropenylheptanoate
(3) 7-isopropyl-4-methyloxepan-2-one + H2O = 6-hydroxy-3,7-dimethyloctanoate
Other name(s): MLH
Systematic name: isoprop(en)ylmethyloxepan-2-one lactonohydrolase
Comments: The enzyme catalyses the ring opening of ε-lactones which are formed during degradation of dihydrocarveol by the Gram-positive bacterium Rhodococcus erythropolis DCL14. The enzyme also acts on ethyl caproate, indicating that it is an esterase with a preference for lactones (internal cyclic esters). The enzyme is not stereoselective.
References:
1.  van der Vlugt-Bergmans , C.J. and van der Werf , M.J. Genetic and biochemical characterization of a novel monoterpene ε-lactone hydrolase from Rhodococcus erythropolis DCL14. Appl. Environ. Microbiol. 67 (2001) 733–741. [PMID: 11157238]
[EC 3.1.1.83 created 2008]
 
 
EC 1.14.14.114     Relevance: 19%
Accepted name: amorpha-4,11-diene 12-monooxygenase
Reaction: amorpha-4,11-diene + 3 O2 + 3 [reduced NADPH—hemoprotein reductase] = artemisinate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) amorpha-4,11-diene + O2 + [reduced NADPH—hemoprotein reductase] = artemisinic alcohol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) artemisinic alcohol + O2 + [reduced NADPH—hemoprotein reductase] = artemisinic aldehyde + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) artemisinic aldehyde + O2 + [reduced NADPH—hemoprotein reductase] = artemisinate + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): CYP71AV1
Systematic name: amorpha-4,11-diene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. Cloned from the plant Artemisia annua (sweet wormwood). Part of the biosynthetic pathway of artemisinin.
References:
1.  Teoh, K.H., Polichuk, D.R., Reed, D.W., Nowak, G. and Covello, P.S. Artemisia annua L. (Asteraceae) trichome-specific cDNAs reveal CYP71AV1, a cytochrome P450 with a key role in the biosynthesis of the antimalarial sesquiterpene lactone artemisinin. FEBS Lett. 580 (2006) 1411–1416. [PMID: 16458889]
[EC 1.14.14.114 created 2012 as EC 1.14.13.158, transferred 2018 to EC 1.14.14.114]
 
 
EC 1.1.3.47     Relevance: 18.6%
Accepted name: 5-(hydroxymethyl)furfural oxidase
Reaction: 5-(hydroxymethyl)furfural + 3 O2 + 2 H2O = furan-2,5-dicarboxylate + 3 H2O2 (overall reaction)
(1a) 5-(hydroxymethyl)furfural + O2 = furan-2,5-dicarbaldehyde + H2O2
(1b) furan-2,5-dicarbaldehyde + H2O = 5-(dihydroxymethyl)furan-2-carbaldehyde (spontaneous)
(1c) 5-(dihydroxymethyl)furan-2-carbaldehyde + O2 = 5-formylfuran-2-carboxylate + H2O2
(1d) 5-formylfuran-2-carboxylate + H2O = 5-(dihydroxymethyl)furan-2-carboxylate (spontaneous)
(1e) 5-(dihydroxymethyl)furan-2-carboxylate + O2 = furan-2,5-dicarboxylate + H2O2
Glossary: 5-(hydroxymethyl)furfural = 5-(hydroxymethyl)furan-2-carbaldehyde
Systematic name: 5-(hydroxymethyl)furfural:oxygen oxidoreductase
Comments: The enzyme, characterized from the bacterium Methylovorus sp. strain MP688, is involved in the degradation and detoxification of 5-(hydroxymethyl)furfural. The enzyme acts only on alcohol groups and requires the spontaneous hydration of aldehyde groups for their oxidation [3]. The enzyme has a broad substrate range that overlaps with EC 1.1.3.7, aryl-alcohol oxidase.
References:
1.  Koopman, F., Wierckx, N., de Winde, J.H. and Ruijssenaars, H.J. Identification and characterization of the furfural and 5-(hydroxymethyl)furfural degradation pathways of Cupriavidus basilensis HMF14. Proc. Natl. Acad. Sci. USA 107 (2010) 4919–4924. [PMID: 20194784]
2.  Dijkman, W.P. and Fraaije, M.W. Discovery and characterization of a 5-hydroxymethylfurfural oxidase from Methylovorus sp. strain MP688. Appl. Environ. Microbiol. 80 (2014) 1082–1090. [PMID: 24271187]
3.  Dijkman, W.P., Groothuis, D.E. and Fraaije, M.W. Enzyme-catalyzed oxidation of 5-hydroxymethylfurfural to furan-2,5-dicarboxylic acid. Angew. Chem. Int. Ed. Engl. 53 (2014) 6515–6518. [PMID: 24802551]
[EC 1.1.3.47 created 2014]
 
 
EC 1.14.14.143     Relevance: 18.5%
Accepted name: (+)-menthofuran synthase
Reaction: (+)-pulegone + [reduced NADPH—hemoprotein reductase] + O2 = (+)-menthofuran + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): menthofuran synthase; (+)-pulegone 9-hydroxylase; (+)-MFS; cytochrome P450 menthofuran synthase
Systematic name: (+)-pulegone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (9-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The conversion of substrate into product involves the hydroxylation of the syn-methyl (C9), intramolecular cyclization to the hemiketal and dehydration to the furan [1]. This is the second cytochrome P-450-mediated step of monoterpene metabolism in peppermint, with the other step being catalysed by EC 1.14.14.99, (S)-limonene 3-monooxygenase [1].
References:
1.  Bertea, C.M., Schalk, M., Karp, F., Maffei, M. and Croteau, R. Demonstration that menthofuran synthase of mint (Mentha) is a cytochrome P450 monooxygenase: cloning, functional expression, and characterization of the responsible gene. Arch. Biochem. Biophys. 390 (2001) 279–286. [PMID: 11396930]
2.  Mahmoud, S.S. and Croteau, R.B. Menthofuran regulates essential oil biosynthesis in peppermint by controlling a downstream monoterpene reductase. Proc. Natl. Acad. Sci. USA 100 (2003) 14481–14486. [PMID: 14623962]
[EC 1.14.14.143 created 2008 as EC 1.14.13.104, transferred 2018 to EC 1.14.14.143]
 
 
EC 1.11.1.14     Relevance: 18.2%
Accepted name: lignin peroxidase
Reaction: (1) 1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
(2) 2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O
Glossary: veratryl alcohol = (3,4-dimethoxyphenyl)methanol
veratraldehyde = 3,4-dimethoxybenzaldehyde
2-methoxyphenol = guaiacol
Other name(s): diarylpropane oxygenase; ligninase I; diarylpropane peroxidase; LiP; diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving); 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol:hydrogen-peroxide oxidoreductase (incorrect); (3,4-dimethoxyphenyl)methanol:hydrogen-peroxide oxidoreductase
Systematic name: 1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol:hydrogen-peroxide oxidoreductase
Comments: A hemoprotein, involved in the oxidative breakdown of lignin by white-rot basidiomycete fungi. The reaction involves an initial oxidation of the heme iron by hydrogen peroxide, forming compound I (FeIV=O radical cation) at the active site. A single one-electron reduction of compound I by an electron derived from a substrate molecule yields compound II (FeIV=O non-radical cation), followed by a second one-electron transfer that returns the enzyme to the ferric oxidation state. The electron transfer events convert the substrate molecule into a transient cation radical intermediate that fragments spontaneously. The enzyme can act on a wide range of aromatic compounds, including methoxybenzenes and nonphenolic β-O-4 linked arylglycerol β-aryl ethers, but cannot act directly on the lignin molecule, which is too large to fit into the active site. However larger lignin molecules can be degraded in the presence of veratryl alcohol. It has been suggested that the free radical that is formed when the enzyme acts on veratryl alcohol can diffuse into the lignified cell wall, where it oxidizes lignin and other organic substrates. In the presence of high concentration of hydrogen peroxide and lack of substrate, the enzyme forms a catalytically inactive form (compound III). This form can be rescued by interaction with two molecules of the free radical products. In the case of veratryl alcohol, such an interaction yields two molecules of veratryl aldehyde.
References:
1.  Kersten, P.J., Tien, M., Kalyanaraman, B. and Kirk, T.K. The ligninase of Phanerochaete chrysosporium generates cation radicals from methoxybenzenes. J. Biol. Chem. 260 (1985) 2609–2612. [PMID: 2982828]
2.  Paszczynski, A., Huynh, V.-B. and Crawford, R. Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium. Arch. Biochem. Biophys. 244 (1986) 750–765. [PMID: 3080953]
3.  Harvey, P.J., Schoemaker, H.E. and Palmer, J.M. Veratryl alcohol as a mediator and the role of radical cations in lignin biodegradation by Phanerochaete chrysosporium. FEBS Lett. 195 (1986) 242–246.
4.  Wariishi, H., Marquez, L., Dunford, H.B. and Gold, M.H. Lignin peroxidase compounds II and III. Spectral and kinetic characterization of reactions with peroxides. J. Biol. Chem. 265 (1990) 11137–11142. [PMID: 2162833]
5.  Cai, D.Y. and Tien, M. Characterization of the oxycomplex of lignin peroxidases from Phanerochaete chrysosporium: equilibrium and kinetics studies. Biochemistry 29 (1990) 2085–2091. [PMID: 2328240]
6.  Khindaria, A., Yamazaki, I. and Aust, S.D. Veratryl alcohol oxidation by lignin peroxidase. Biochemistry 34 (1995) 16860–16869. [PMID: 8527462]
7.  Khindaria, A., Yamazaki, I. and Aust, S.D. Stabilization of the veratryl alcohol cation radical by lignin peroxidase. Biochemistry 35 (1996) 6418–6424. [PMID: 8639588]
8.  Khindaria, A., Nie, G. and Aust, S.D. Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex. Biochemistry 36 (1997) 14181–14185. [PMID: 9369491]
9.  Doyle, W.A., Blodig, W., Veitch, N.C., Piontek, K. and Smith, A.T. Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis. Biochemistry 37 (1998) 15097–15105. [PMID: 9790672]
10.  Pollegioni, L., Tonin, F. and Rosini, E. Lignin-degrading enzymes. FEBS J. 282 (2015) 1190–1213. [PMID: 25649492]
[EC 1.11.1.14 created 1992, modified 2006, modified 2011, modified 2016]
 
 
EC 1.14.14.161     Relevance: 18%
Accepted name: nepetalactol monooxygenase
Reaction: (+)-cis,trans-nepetalactol + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = 7-deoxyloganetate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) (+)-cis,trans-nepetalactol + [reduced NADPH—hemoprotein reductase] + O2 = 7-deoxyloganetic alcohol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 7-deoxyloganetic alcohol + [reduced NADPH—hemoprotein reductase] + O2 = iridotrial + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) iridotrial + [reduced NADPH—hemoprotein reductase] + O2 = 7-deoxyloganetate + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: (+)-cis,trans-nepetalactol = (4aS,7S,7aR)-4,7-dimethyl-1,4a,5,6,7,7a-hexahydrocyclopenta[c]pyran-1-ol
7-deoxyloganetate = (1S,4aS,7S,7aR)-1-hydroxy-7-methyl-1,4a,5,6,7,7a-hexahydrocyclopenta[c]pyran-4-carboxylate
Other name(s): CYP76A26 (gene name); iridoid oxidase (misleading)
Systematic name: (+)-cis,trans-nepetalactol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (hydroxylating)
Comments: The enzyme, characterized from the plant Catharanthus roseus, is a cytochrome P-450 (heme thiolate) protein. It catalyses three successive reactions in the pathway leading to biosynthesis of monoterpenoid indole alkaloids.
References:
1.  Miettinen, K., Dong, L., Navrot, N., Schneider, T., Burlat, V., Pollier, J., Woittiez, L., van der Krol, S., Lugan, R., Ilc, T., Verpoorte, R., Oksman-Caldentey, K.M., Martinoia, E., Bouwmeester, H., Goossens, A., Memelink, J. and Werck-Reichhart, D. The seco-iridoid pathway from Catharanthus roseus. Nat. Commun. 5:3606 (2014). [PMID: 24710322]
[EC 1.14.14.161 created 2018]
 
 
EC 3.1.6.19     Relevance: 17.6%
Accepted name: (R)-specific secondary-alkylsulfatase (type III)
Reaction: an (R)-secondary-alkyl sulfate + H2O = an (S)-secondary-alcohol + sulfate
Other name(s): S3 secondary alkylsulphohydrolase; Pisa1; secondary alkylsulphohydrolase; (R)-specific sec-alkylsulfatase; sec-alkylsulfatase; (R)-specific secondary-alkylsulfatase; type III (R)-specific secondary-alkylsulfatase
Systematic name: (R)-secondary-alkyl sulfate sulfohydrolase [(S)-secondary-alcohol-forming]
Comments: Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-β-lactamase fold and binds two zinc ions as cofactors. This enzyme belongs to the type III sulfatase family. The enzyme from the bacterium Rhodococcus ruber prefers linear secondary-alkyl sulfate esters, particularly octan-2-yl, octan-3-yl, and octan-4-yl sulfates [1]. The enzyme from the bacterium Pseudomonas sp. DSM6611 utilizes a range of secondary-alkyl sulfate esters bearing aromatic, olefinic and acetylenic moieties. Hydrolysis proceeds through inversion of the configuration at the stereogenic carbon atom, resulting in perfect enantioselectivity. cf. EC 3.1.6.1, arylsulfatase (type I), and EC 1.14.11.77, alkyl sulfatase (type II).
References:
1.  Pogorevc, M. and Faber, K. Purification and characterization of an inverting stereo- and enantioselective sec-alkylsulfatase from the gram-positive bacterium Rhodococcus ruber DSM 44541. Appl. Environ. Microbiol. 69 (2003) 2810–2815. [PMID: 12732552]
2.  Wallner, S.R., Nestl, B.M. and Faber, K. Highly enantioselective sec-alkyl sulfatase activity of Sulfolobus acidocaldarius DSM 639. Org. Lett. 6 (2004) 5009–5010. [PMID: 15606122]
3.  Knaus, T., Schober, M., Kepplinger, B., Faccinelli, M., Pitzer, J., Faber, K., Macheroux, P. and Wagner, U. Structure and mechanism of an inverting alkylsulfatase from Pseudomonas sp. DSM6611 specific for secondary alkyl sulfates. FEBS J. 279 (2012) 4374–4384. [PMID: 23061549]
4.  Schober, M., Knaus, T., Toesch, M., Macheroux, P., Wagner, U. and Faber, K. The substrate spectrum of the inverting sec-alkylsulfatase Pisa1. Adv. Synth. Catal. 354 (2012) 1737–1742.
[EC 3.1.6.19 created 2013, modified 2021]
 
 
EC 3.2.1.139     Relevance: 17.1%
Accepted name: α-glucuronidase
Reaction: an α-D-glucuronoside + H2O = an alcohol + D-glucuronate
Other name(s): α-glucosiduronase
Systematic name: α-D-glucosiduronate glucuronohydrolase
Comments: Considerable differences in the specificities of the enzymes from different fungi for α-D-glucosiduronates have been reported. Activity is also found in the snail.
References:
1.  Puls, J. α-Glucuronidases in the hydrolysis of wood xylans. In: Visser, J., Kusters van Someren, M.A., Beldman, G. and Voragen, A.G.J. (Ed.), Xylans and Xylanases, Elsevier, Amsterdam, 1992, pp. 213–224.
2.  Uchida, H., Nanri, T., Kawabata, Y., Kusakabe, I., Murakami, K. Purification and characterization of intracellular α-glucuronidase from Aspergillus niger. Biosci. Biotechnol. Biochem. 56 (1992) 1608–1615.
[EC 3.2.1.139 created 1999]
 
 
EC 3.8.1.5     Relevance: 16.5%
Accepted name: haloalkane dehalogenase
Reaction: 1-haloalkane + H2O = a primary alcohol + halide
Other name(s): 1-chlorohexane halidohydrolase; 1-haloalkane dehalogenase
Systematic name: 1-haloalkane halidohydrolase
Comments: Acts on a wide range of 1-haloalkanes, haloalcohols, haloalkenes and some haloaromatic compounds.
References:
1.  Keuning, S., Janssen, D.B. and Witholt, B. Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ10. J. Bacteriol. 163 (1985) 635–639. [PMID: 4019411]
2.  Scholtz, R., Leisinger, T., Suter, F. and Cook, A.M. Characterization of 1-chlorohexane halidohydrolase, a dehalogenase of wide substrate range from an Arthrobacter sp. J. Bacteriol. 169 (1987) 5016–5021. [PMID: 3667524]
3.  Yokota, T., Omori, T. and Kodama, T. Purification and properties of haloalkane dehalogenase from Corynebacterium sp. strain m15-3. J. Bacteriol. 169 (1987) 4049–4054. [PMID: 3624201]
[EC 3.8.1.5 created 1989]
 
 
EC 1.14.13.105     Relevance: 16.4%
Accepted name: monocyclic monoterpene ketone monooxygenase
Reaction: (1) (–)-menthone + NADPH + H+ + O2 = (4R,7S)-7-isopropyl-4-methyloxepan-2-one + NADP+ + H2O
(2) dihydrocarvone + NADPH + H+ + O2 = 4-isopropenyl-7-methyloxepan-2-one + NADP+ + H2O
(3) (iso)-dihydrocarvone + NADPH + H+ + O2 = 6-isopropenyl-3-methyloxepan-2-one + NADP+ + H2O
(4a) 1-hydroxymenth-8-en-2-one + NADPH + H+ + O2 = 7-hydroxy-4-isopropenyl-7-methyloxepan-2-one + NADP+ + H2O
(4b) 7-hydroxy-4-isopropenyl-7-methyloxepan-2-one = 3-isopropenyl-6-oxoheptanoate (spontaneous)
Other name(s): 1-hydroxy-2-oxolimonene 1,2-monooxygenase; dihydrocarvone 1,2-monooxygenase; MMKMO
Systematic name: (–)-menthone,NADPH:oxygen oxidoreductase
Comments: A flavoprotein (FAD). This Baeyer-Villiger monooxygenase enzyme from the Gram-positive bacterium Rhodococcus erythropolis DCL14 has wide substrate specificity, catalysing the lactonization of a large number of monocyclic monoterpene ketones and substituted cyclohexanones [2]. Both (1R,4S)- and (1S,4R)-1-hydroxymenth-8-en-2-one are metabolized, with the lactone product spontaneously rearranging to form 3-isopropenyl-6-oxoheptanoate [1].
References:
1.  van der Werf, M.J., Swarts, H.J. and de Bont, J.A. Rhodococcus erythropolis DCL14 contains a novel degradation pathway for limonene. Appl. Environ. Microbiol. 65 (1999) 2092–2102. [PMID: 10224006]
2.  Van Der Werf, M.J. Purification and characterization of a Baeyer-Villiger mono-oxygenase from Rhodococcus erythropolis DCL14 involved in three different monocyclic monoterpene degradation pathways. Biochem. J. 347 (2000) 693–701. [PMID: 10769172]
3.  van der Werf, M.J. and Boot, A.M. Metabolism of carveol and dihydrocarveol in Rhodococcus erythropolis DCL14. Microbiology 146 (2000) 1129–1141. [PMID: 10832640]
[EC 1.14.13.105 created 2008]
 
 
EC 3.2.1.51     Relevance: 16.4%
Accepted name: α-L-fucosidase
Reaction: an α-L-fucoside + H2O = L-fucose + an alcohol
Other name(s): α-fucosidase
Systematic name: α-L-fucoside fucohydrolase
References:
1.  Levvy, G.A. and McAllan, A. Mammalian fucosidases. 2. α-L-Fucosidase. Biochem. J. 80 (1961) 435–439. [PMID: 13761578]
2.  Reglero, A. and Cabezas, J.A. Glycosidases of molluscs. Purification and properties of α-L-fucosidase from Chamelea gallina L. Eur. J. Biochem. 66 (1976) 379–387. [PMID: 7458]
3.  Tanaka, K., Nakano, T., Noguchi, S. and Pigman, W. Purification of α-L-fucosidase of abalone livers. Arch. Biochem. Biophys. 126 (1968) 624–633. [PMID: 5672520]
[EC 3.2.1.51 created 1972]
 
 
EC 3.1.1.50     Relevance: 16.2%
Accepted name: wax-ester hydrolase
Reaction: a wax ester + H2O = a long-chain alcohol + a long-chain carboxylate
Other name(s): jojoba wax esterase; WEH
Systematic name: wax-ester acylhydrolase
Comments: Also acts on long-chain acylglycerol, but not diacyl- or triacylglycerols.
References:
1.  Huang, A.H.C., Moreau, R.A. and Liu, K.D.F. Development and properties of a wax ester hydrolase in the cotyledons of jojoba seedlings. Plant Physiol. 61 (1978) 339–341. [PMID: 16660288]
2.  Moreau, R.A. and Huang, A.H.C. Enzymes of wax ester catabolism in jojoba. Methods Enzymol. 71 (1981) 804–813.
[EC 3.1.1.50 created 1984]
 
 
EC 3.2.1.31     Relevance: 16%
Accepted name: β-glucuronidase
Reaction: a β-D-glucuronoside + H2O = D-glucuronate + an alcohol
Other name(s): β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase
Systematic name: β-D-glucuronoside glucuronosohydrolase
References:
1.  Diez, T. and Cabezas, J.A. Properties of two molecular forms of β-glucuronidase from the mollusc Littorina littorea L. Eur. J. Biochem. 93 (1978) 301–311.
2.  Doyle, M.L., Katzman, P.A. and Doisy, E.A. Production and properties of bacterial β-glucuronidase. J. Biol. Chem. 217 (1955) 921–930. [PMID: 13271452]
3.  Fishman, W.H. Beta-glucuronidase. Adv. Enzymol. Relat. Subj. Biochem. 16 (1955) 361–409. [PMID: 14376216]
4.  Levvy, G.A. and Marsh, C.A. β-Glucuronidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 397–407.
5.  Wakabayashi, M. and Fishman, W.H. The comparative ability of β-glucuronidase preparations (liver, Escherichia coli, Helix pomatia, and Patella vulgata) to hydrolyze certain steroid glucosiduronic acids. J. Biol. Chem. 236 (1961) 996–1001. [PMID: 13782588]
[EC 3.2.1.31 created 1961]
 
 
EC 3.1.4.46     Relevance: 16%
Accepted name: glycerophosphodiester phosphodiesterase
Reaction: a glycerophosphodiester + H2O = an alcohol + sn-glycerol 3-phosphate
Other name(s): gene hpd protein; glycerophosphoryl diester phosphodiesterase; IgD-binding protein D
Systematic name: glycerophosphodiester glycerophosphohydrolase
Comments: Broad specificity for glycerophosphodiesters; glycerophosphocholine, glycerophosphoethanolamine, glycerophosphoglycerol and bis(glycerophospho)-glycerol are hydrolysed.
References:
1.  Larson, T.J., Ehrmann, M. and Boos, W. Periplasmic glycerophosphodiester phosphodiesterase of Escherichia coli, a new enzyme of the glp regulon. J. Biol. Chem. 258 (1983) 5428–5432. [PMID: 6304089]
[EC 3.1.4.46 created 1986]
 
 
EC 1.14.13.123      
Transferred entry: germacrene A hydroxylase. Now EC 1.14.14.95, germacrene A hydroxylase
[EC 1.14.13.123 created 2011, deleted 2018]
 
 
EC 1.1.5.11     Relevance: 15.6%
Accepted name: 1-butanol dehydrogenase (quinone)
Reaction: butan-1-ol + a quinone = butanal + a quinol
Other name(s): BOH
Systematic name: butan-1-ol:quinone oxidoreductase
Comments: This periplasmic quinoprotein alcohol dehydrogenase, characterized from the bacterium Thauera butanivorans, is involved in butane degradation. It contains a pyrroloquinoline quinone (PQQ) prosthetic group. cf. EC 1.1.2.9, 1-butanol dehydrogenase (cytochrome c).
References:
1.  Vangnai, A.S., Arp, D.J. and Sayavedra-Soto, L.A. Two distinct alcohol dehydrogenases participate in butane metabolism by Pseudomonas butanovora. J. Bacteriol. 184 (2002) 1916–1924. [PMID: 11889098]
2.  Vangnai, A.S., Sayavedra-Soto, L.A. and Arp, D.J. Roles for the two 1-butanol dehydrogenases of Pseudomonas butanovora in butane and 1-butanol metabolism. J. Bacteriol. 184 (2002) 4343–4350. [PMID: 12142403]
[EC 1.1.5.11 created 2016]
 
 
EC 1.1.2.9     Relevance: 15.4%
Accepted name: 1-butanol dehydrogenase (cytochrome c)
Reaction: butan-1-ol + 2 ferricytochrome c = butanal + 2 ferrocytochrome c + 2 H+
Other name(s): BDH
Systematic name: butan-1-ol:ferricytochrome c oxidoreductase
Comments: This periplasmic quinoprotein alcohol dehydrogenase, characterized from the bacterium Thauera butanivorans, is involved in butane degradation. It contains both pyrroloquinoline quinone (PQQ) and heme c prosthetic groups. cf. EC 1.1.5.11, 1-butanol dehydrogenase (quinone).
References:
1.  Vangnai, A.S. and Arp, D.J. An inducible 1-butanol dehydrogenase, a quinohaemoprotein, is involved in the oxidation of butane by ’Pseudomonas butanovora’. Microbiology 147 (2001) 745–756. [PMID: 11238982]
2.  Vangnai, A.S., Arp, D.J. and Sayavedra-Soto, L.A. Two distinct alcohol dehydrogenases participate in butane metabolism by Pseudomonas butanovora. J. Bacteriol. 184 (2002) 1916–1924. [PMID: 11889098]
3.  Vangnai, A.S., Sayavedra-Soto, L.A. and Arp, D.J. Roles for the two 1-butanol dehydrogenases of Pseudomonas butanovora in butane and 1-butanol metabolism. J. Bacteriol. 184 (2002) 4343–4350. [PMID: 12142403]
[EC 1.1.2.9 created 2016]
 
 
EC 3.1.1.70     Relevance: 15.4%
Accepted name: cetraxate benzylesterase
Reaction: cetraxate benzyl ester + H2O = cetraxate + benzyl alcohol
Systematic name: cetraxate-benzyl-ester benzylhydrolase
Comments: Acts on a number of benzyl esters of substituted phenyl propanoates, and on the benzyl esters of phenylalanine and tyrosine.
References:
1.  Kuroda, H., Miyadera, A., Imura, A. and Suzuki, A. Partial purification, and some properties and reactivities of cetraxate benzyl ester hydrochloride-hydrolyzing enzyme. Chem. Pharm. Bull. 37 (1989) 2929–2932. [PMID: 2632040]
[EC 3.1.1.70 created 1992]
 
 
EC 3.1.1.6     Relevance: 15.4%
Accepted name: acetylesterase
Reaction: an acetic ester + H2O = an alcohol + acetate
Other name(s): C-esterase (in animal tissues); acetic ester hydrolase; chloroesterase; p-nitrophenyl acetate esterase; Citrus acetylesterase
Systematic name: acetic-ester acetylhydrolase
References:
1.  Aldridge, W.N. Serum esterases. I. Two types of esterase (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate and a method for their determination. Biochem. J. 53 (1953) 110–117. [PMID: 13032041]
2.  Bergmann, F. and Rimon, S. Fractionation of C-esterase from the hog's kidney extract. Biochem. J. 77 (1960) 209–214. [PMID: 16748846]
3.  Jansen, E.F., Nutting, M.-D.F. and Balls, A.K. The reversible inhibition of acetylesterase by diisopropyl fluorophosphate and tetraethyl pyrophosphate. J. Biol. Chem. 175 (1948) 975–987. [PMID: 18880795]
[EC 3.1.1.6 created 1961]
 
 
EC 3.2.1.126     Relevance: 15.4%
Accepted name: coniferin β-glucosidase
Reaction: coniferin + H2O = D-glucose + coniferol
Other name(s): coniferin-hydrolyzing β-glucosidase
Systematic name: coniferin β-D-glucosidase
Comments: Also hydrolyses syringin, 4-cinnamyl alcohol β-glucoside and, more slowly, some other aryl β-glycosides. A plant cell-wall enzyme involved in the biosynthesis of lignin.
References:
1.  Hösel, W., Surholt, E. and Borgmann, E. Characterization of β-glucosidase isoenzymes possibly involved in lignification from chick pea (Cicer arietinum L.) cell suspension cultures. Eur. J. Biochem. 84 (1978) 487–492. [PMID: 25181]
2.  Marcinowski, S. and Grisebach, H. Enzymology of lignification. Cell-wall bound β-glucosidase for coniferin from spruce (Picea abies) seedlings. Eur. J. Biochem. 87 (1978) 37–44. [PMID: 27355]
[EC 3.2.1.126 created 1989]
 
 
EC 4.2.3.157     Relevance: 15.4%
Accepted name: (+)-isoafricanol synthase
Reaction: (2E,6E)-farnesyl diphosphate + H2O = (+)-isoafricanol + diphosphate
Glossary: (+)-isoafricanol = (1aS,4aR,5R,7aS,7bR)-3,3,5,7b-tetramethyldecahydro-4aH-cyclopropa[e]azulen-4a-ol
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase [cyclizing, (+)-isoafricanol-forming]
Comments: (+)-Isoafricanol is a sesquiterpene alcohol. Its synthesis has been shown to occur in the bacteria Streptomyces violaceusniger and Streptomyces malaysiensis.
References:
1.  Riclea, R., Citron, C.A., Rinkel, J. and Dickschat, J.S. Identification of isoafricanol and its terpene cyclase in Streptomyces violaceusniger using CLSA-NMR. Chem. Commun. (Camb.) 50 (2014) 4228–4230. [PMID: 24626486]
2.  Rabe, P., Samborskyy, M., Leadlay, P.F. and Dickschat, J.S. Isoafricanol synthase from Streptomyces malaysiensis. Org. Biomol. Chem. 15 (2017) 2353–2358. [PMID: 28247907]
[EC 4.2.3.157 created 2017]
 
 
EC 1.1.1.16     Relevance: 15.3%
Accepted name: galactitol 2-dehydrogenase
Reaction: galactitol + NAD+ = D-tagatose + NADH + H+
Other name(s): dulcitol dehydrogenase; AtuSorbD (gene name); galactitol:NAD+ 2-oxidoreductase
Systematic name: galactitol:NAD+ 2-oxidoreductase (D-tagatose-forming)
Comments: Also converts other alditols containing an L-threo-configuration adjacent to a primary alcohol group into the corresponding sugars. The enzyme from Agrobacterium fabrum C58 is part of D-altritol and galactitol degradation pathways.
References:
1.  Shaw, D.R.D. Polyol dehydrogenases. 3. Galactitol dehydrogenase and D-iditol dehydrogenase. Biochem. J. 64 (1956) 394–405. [PMID: 13373783]
2.  Wichelecki, D.J., Vetting, M.W., Chou, L., Al-Obaidi, N., Bouvier, J.T., Almo, S.C. and Gerlt, J.A. ATP-binding cassette (ABC) transport system solute-binding protein-guided identification of novel D-altritol and galactitol catabolic pathways in Agrobacterium tumefaciens C58. J. Biol. Chem. 290 (2015) 28963–28976. [PMID: 26472925]
[EC 1.1.1.16 created 1961]
 
 
EC 4.1.99.11     Relevance: 15.2%
Accepted name: benzylsuccinate synthase
Reaction: benzylsuccinate = toluene + fumarate
Other name(s): benzylsuccinate fumarate-lyase
Systematic name: benzylsuccinate fumarate-lyase (toluene-forming)
Comments: A glycyl radical enzyme that is inhibited by benzyl alcohol, benzaldehyde, phenylhydrazine and is inactivated by oxygen.
References:
1.  Beller, H.R. and Spormann, A.M. Analysis of the novel benzylsuccinate synthase reaction for anaerobic toluene activation based on structural studies of the product. J. Bacteriol. 180 (1998) 5454–5457. [PMID: 9765580]
2.  Leuthner, B., Leutwein, C., Schultz, H., Hörth, P., Haehnel, W., Schiltz, E., Schägger, H. and Heider, J. Biochemical and genetic characterisation of benzylsuccinate synthase from Thauera aromatica: a new glycyl radical enzyme catalysing the first step in anaerobic toluene metabolism. Mol. Microbiol. 28 (1998) 615–628. [PMID: 9632263]
[EC 4.1.99.11 created 2000]
 
 
EC 3.2.1.112     Relevance: 15.1%
Accepted name: 2-deoxyglucosidase
Reaction: a 2-deoxy-α-D-glucoside + H2O = 2-deoxy-D-glucose + an alcohol
Other name(s): 2-deoxy-α-glucosidase; 2-deoxy-α-D-glucosidase
Systematic name: 2-deoxy-α-D-glucoside deoxyglucohydrolase
References:
1.  Canellakis, Z.N., Bondy, P.K., May, J.A., Jr., Myers-Robfogel, M.K. and Sartorelli, A.C. Identification of a glycosidase activity with apparent specificity for 2-deoxy-D-glucose in glycosidic linkage. Eur. J. Biochem. 143 (1984) 159–163. [PMID: 6468386]
[EC 3.2.1.112 created 1986]
 
 
EC 1.3.1.92     Relevance: 14.8%
Accepted name: artemisinic aldehyde Δ11(13)-reductase
Reaction: (11R)-dihydroartemisinic aldehyde + NADP+ = artemisinic aldehyde + NADPH + H+
Other name(s): Dbr2
Systematic name: artemisinic aldehyde:NADP+ oxidoreductase
Comments: Cloned from Artemisia annua. In addition to the reduction of artemisinic aldehyde it is also able to a lesser extent to reduce artemisinic alcohol and artemisinic acid. Part of the biosyntheis of artemisinin.
References:
1.  Bertea, C.M., Freije, J.R., van der Woude, H., Verstappen, F.W., Perk, L., Marquez, V., De Kraker, J.W., Posthumus, M.A., Jansen, B.J., de Groot, A., Franssen, M.C. and Bouwmeester, H.J. Identification of intermediates and enzymes involved in the early steps of artemisinin biosynthesis in Artemisia annua. Planta Med. 71 (2005) 40–47. [PMID: 15678372]
2.  Zhang, Y., Teoh, K.H., Reed, D.W., Maes, L., Goossens, A., Olson, D.J., Ross, A.R. and Covello, P.S. The molecular cloning of artemisinic aldehyde Δ11(13) reductase and its role in glandular trichome-dependent biosynthesis of artemisinin in Artemisia annua. J. Biol. Chem. 283 (2008) 21501–21508. [PMID: 18495659]
[EC 1.3.1.92 created 2012]
 
 
EC 1.1.1.33     Relevance: 14.8%
Accepted name: mevaldate reductase (NADPH)
Reaction: (R)-mevalonate + NADP+ = mevaldate + NADPH + H+
Other name(s): mevaldate (reduced nicotinamide adenine dinucleotide phosphate) reductase; mevaldate reductase (NADPH2)
Systematic name: (R)-mevalonate:NADP+ oxidoreductase
Comments: May be identical with EC 1.1.1.2 [alcohol dehydrogenase (NADP+)].
References:
1.  Coon, M.J., Kupiecki, F.P., Dekker, E.E., Schlesinger, M.J. and del Campillo, A. The enzymic synthesis of branched-chain acids. In: Wolstenholme, G.E.W. and O'Connor, M. (Ed.), CIBA Symposium on the Biosynthesis of Terpenes and Sterols, CIBA Symposium on the Biosynthesis of Terpenes and Sterols, London, 1959, pp. 62–74.
2.  von Wartburg, J.P. and Wermoth, B. Aldehyde reductase. In: Jakoby, W.B. (Ed.), Enzymatic Basis of Detoxication, vol. 1, Academic Press, New York, 1980, pp. 249–260.
[EC 1.1.1.33 created 1961]
 
 
EC 1.14.14.28     Relevance: 14.6%
Accepted name: long-chain alkane monooxygenase
Reaction: a long-chain alkane + FMNH2 + O2 = a long-chain primary alcohol + FMN + H2O
Systematic name: long-chain-alkane,FMNH2:oxygen oxidoreductase
Comments: The enzyme, characterized from the bacterium Geobacillus thermodenitrificans NG80-2, is capable of converting alkanes ranging from C15 to C36 into their corresponding primary alcohols [1,2]. The FMNH2 cofactor is provided by an FMN reductase [3].
References:
1.  Feng, L., Wang, W., Cheng, J., Ren, Y., Zhao, G., Gao, C., Tang, Y., Liu, X., Han, W., Peng, X., Liu, R. and Wang, L. Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir. Proc. Natl. Acad. Sci. USA 104 (2007) 5602–5607. [PMID: 17372208]
2.  Li, L., Liu, X., Yang, W., Xu, F., Wang, W., Feng, L., Bartlam, M., Wang, L. and Rao, Z. Crystal structure of long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN: unveiling the long-chain alkane hydroxylase. J. Mol. Biol. 376 (2008) 453–465. [PMID: 18164311]
3.  Dong, Y., Yan, J., Du, H., Chen, M., Ma, T. and Feng, L. Engineering of LadA for enhanced hexadecane oxidation using random- and site-directed mutagenesis. Appl. Microbiol. Biotechnol. 94 (2012) 1019–1029. [PMID: 22526792]
[EC 1.14.14.28 created 2016]
 
 
EC 2.3.1.160     Relevance: 14.5%
Accepted name: vinorine synthase
Reaction: acetyl-CoA + 16-epivellosimine = CoA + vinorine
Systematic name: acyl-CoA:16-epivellosimine O-acetyltransferase (cyclizing)
Comments: The reaction proceeds in two stages. The indole nitrogen of 16-epivellosimine interacts with its aldehyde group giving an hydroxy-substituted new ring. This alcohol is then acetylated. Also acts on gardneral (11-methoxy-16-epivellosimine). Generates the ajmalan skeleton, which forms part of the route to ajmaline.
References:
1.  Pfitzner, A., Polz, L. and Stöckligt, J. Properties of vinorine synthase the Rauwolfia enzyme involved in the formation of the ajmaline skeleton. Z. Naturforsch. C: Biosci. 41 (1986) 103–114.
2.  Bayer, A., Ma, X. and Stöckigt, J. Acetyltransfer in natural product biosynthesis—functional cloning and molecular analysis of vinorine synthase. Bioorg. Med. Chem. 12 (2004) 2787–2795. [PMID: 15110860]
3.  Ma, X., Koepke, J., Bayer, A., Linhard, V., Fritzsch, G., Zhang, B., Michel, H. and Stöckigt, J. Vinorine synthase from Rauvolfia: the first example of crystallization and preliminary X-ray diffraction analysis of an enzyme of the BAHD superfamily. Biochim. Biophys. Acta 1701 (2004) 129–132. [PMID: 15450182]
4.  Ma, X., Koepke, J., Panjikar, S., Fritzsch, G. and Stöckigt, J. Crystal structure of vinorine synthase, the first representative of the BAHD superfamily. J. Biol. Chem. 280 (2005) 13576–13583. [PMID: 15665331]
[EC 2.3.1.160 created 2002]
 
 
EC 3.1.1.43     Relevance: 14.4%
Accepted name: α-amino-acid esterase
Reaction: an α-amino acid ester + H2O = an α-amino acid + an alcohol
Other name(s): α-amino acid ester hydrolase
Systematic name: α-amino-acid-ester aminoacylhydrolase
Comments: Also catalyses α-aminoacyl transfer to a number of amine nucleophiles.
References:
1.  Kato, K., Kawahara, K., Takahashi, T. and Kakinuma, A. Purification of an α-amino acid ester hydrolase from Xanthomonas citri. Agric. Biol. Chem. 44 (1980) 1069–1074.
2.  Kato, K., Kawahara, K., Takahashi, T. and Kakinuma, A. Substrate specificity of an α-amino acid ester hydrolase from Xanthomonas citri. Agric. Biol. Chem. 44 (1980) 1075–1081.
3.  Takahashi, T., Yamazaki, Y. and Kato, K. Substrate specificity of an α-amino acid ester hydrolase produced by Acetobacter turbidans A. T.C.C. 9325. Biochem. J. 137 (1974) 497–503. [PMID: 4424889]
[EC 3.1.1.43 created 1983]
 
 
EC 3.1.1.48     Relevance: 14.2%
Accepted name: fusarinine-C ornithinesterase
Reaction: N5-acyl-L-ornithine ester + H2O = N5-acyl-L-ornithine + an alcohol
Other name(s): ornithine esterase; 5-N-acyl-L-ornithine-ester hydrolase
Systematic name: N5-acyl-L-ornithine-ester hydrolase
Comments: Hydrolyses the three ornithine ester bonds in fusarinine C. Also acts on N5-dinitrophenyl-L-ornithine methyl ester.
References:
1.  Emery, T. Fungal ornithine esterases: relationship to iron transport. Biochemistry 15 (1976) 2723–2728. [PMID: 949472]
[EC 3.1.1.48 created 1984]
 
 
EC 1.3.1.94     Relevance: 14.2%
Accepted name: polyprenol reductase
Reaction: ditrans,polycis-dolichol + NADP+ = ditrans,polycis-polyprenol + NADPH + H+
Other name(s): SRD5A3 (gene name); DFG10 (gene name)
Systematic name: ditrans,polycis-dolichol:NADP+ 2,3-oxidoreductase
Comments: The reaction occurs in the reverse direction with reduction of the terminal double bond next to the alcohol group. Isolated from human fetal brain tissue but present in all eukaryotes. In mammalian cells dolichols are predominantly 18-21 isoprene units in length.
References:
1.  Sagami, H., Kurisaki, A. and Ogura, K. Formation of dolichol from dehydrodolichol is catalyzed by NADPH-dependent reductase localized in microsomes of rat liver. J. Biol. Chem. 268 (1993) 10109–10113. [PMID: 8486680]
2.  Cantagrel, V., Lefeber, D.J., Ng, B.G., Guan, Z., Silhavy, J.L., Bielas, S.L., Lehle, L., Hombauer, H., Adamowicz, M., Swiezewska, E., De Brouwer, A.P., Blumel, P., Sykut-Cegielska, J., Houliston, S., Swistun, D., Ali, B.R., Dobyns, W.B., Babovic-Vuksanovic, D., van Bokhoven, H., Wevers, R.A., Raetz, C.R., Freeze, H.H., Morava, E., Al-Gazali, L. and Gleeson, J.G. SRD5A3 is required for converting polyprenol to dolichol and is mutated in a congenital glycosylation disorder. Cell 142 (2010) 203–217. [PMID: 20637498]
[EC 1.3.1.94 created 2012]
 
 
EC 2.3.1.268     Relevance: 14%
Accepted name: ethanol O-acetyltransferase
Reaction: ethanol + acetyl-CoA = ethyl acetate + CoA
Other name(s): eat1 (gene name); ethanol acetyltransferase
Systematic name: acetyl-CoA:ethanol O-acetyltransferase
Comments: The enzyme, characterized from the yeast Wickerhamomyces anomalus, is responsible for most ethyl acetate synthesis in known ethyl acetate-producing yeasts. It is only distantly related to enzymes classified as EC 2.3.1.84, alcohol O-acetyltransferase. The enzyme also possesses thioesterase and esterase activities, which are inhibited by high ethanol concentrations.
References:
1.  Kruis, A.J., Levisson, M., Mars, A.E., van der Ploeg, M., Garces Daza, F., Ellena, V., Kengen, S.WM., van der Oost, J. and Weusthuis, R.A. Ethyl acetate production by the elusive alcohol acetyltransferase from yeast. Metab. Eng. 41 (2017) 92–101. [PMID: 28356220]
[EC 2.3.1.268 created 2018]
 
 
EC 3.2.1.85     Relevance: 14%
Accepted name: 6-phospho-β-galactosidase
Reaction: a 6-phospho-β-D-galactoside + H2O = 6-phospho-D-galactose + an alcohol
Other name(s): phospho-β-galactosidase; β-D-phosphogalactoside galactohydrolase; phospho-β-D-galactosidase; 6-phospho-β-D-galactosidase
Systematic name: 6-phospho-β-D-galactoside 6-phosphogalactohydrolase
References:
1.  Hengstenberg, W., Penberthy, W.K. and Morse, M.L. Purification of the staphylococcal 6-phospho-β-D-galactosidase. Eur. J. Biochem. 14 (1970) 27–32. [PMID: 5447434]
[EC 3.2.1.85 created 1976]
 
 
EC 1.1.1.19     Relevance: 13.9%
Accepted name: glucuronate reductase
Reaction: L-gulonate + NADP+ = D-glucuronate + NADPH + H+
Other name(s): L-hexonate:NADP dehydrogenase; TPN-L-gulonate dehydrogenase; NADP-L-gulonate dehydrogenase; D-glucuronate dehydrogenase; D-glucuronate reductase; L-glucuronate reductase (incorrect)
Systematic name: L-gulonate:NADP+ 6-oxidoreductase
Comments: Also reduces D-galacturonate. May be identical with EC 1.1.1.2 [alcohol dehydrogenase (NADP+)].
References:
1.  Sivak, A. and Hoffmann-Ostenhof, O. Enzymes of meso-inositol catabolism in the yeast Schwanniomyces occidentalis. Biochim. Biophys. Acta 53 (1961) 426–428. [PMID: 13913518]
2.  von Wartburg, J.P. and Wermoth, B. Aldehyde reductase. In: Jakoby, W.B. (Ed.), Enzymatic Basis of Detoxication, vol. 1, Academic Press, New York, 1980, pp. 249–260.
3.  York, J.L., Grollman, A.P. and Bublitz, C. TPN-L-gulonate dehydrogenase. Biochim. Biophys. Acta 47 (1961) 298–306. [PMID: 13787380]
[EC 1.1.1.19 created 1961]
 
 
EC 3.1.3.1     Relevance: 13.9%
Accepted name: alkaline phosphatase
Reaction: a phosphate monoester + H2O = an alcohol + phosphate
Other name(s): alkaline phosphomonoesterase; phosphomonoesterase; glycerophosphatase; alkaline phosphohydrolase; alkaline phenyl phosphatase; orthophosphoric-monoester phosphohydrolase (alkaline optimum)
Systematic name: phosphate-monoester phosphohydrolase (alkaline optimum)
Comments: Wide specificity. Also catalyses transphosphorylations. The human placental enzyme is a zinc protein. Some enzymes hydrolyse diphosphate (cf. EC 3.6.1.1 inorganic diphosphatase)
References:
1.  Engström, L. Studies on calf-intestinal alkaline phosphatase. I. Chromatographic purification, microheterogeneity and some other properties of the purified enzyme. Biochim. Biophys. Acta 52 (1961) 36–48. [PMID: 13890304]
2.  Harkness, D.R. Studies on human placental alkaline phosphatase. II. Kinetic properties and studies on the apoenzyme. Arch. Biochem. Biophys. 126 (1968) 513–523. [PMID: 4970479]
3.  Malamy, M.H. and Horecker, B.L. Purification and crystallization of the alkaline phosphatase of Escherichia coli. Biochemistry 3 (1964) 1893–1897. [PMID: 14269306]
4.  Morton, R.K. Alkaline phosphatase of milk. 2. Purification of the enzyme. Biochem. J. 55 (1953) 795–800. [PMID: 13115375]
5.  Stadtman, T.C. Alkaline phosphatases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 55–71.
[EC 3.1.3.1 created 1961]
 
 
EC 3.5.1.64     Relevance: 13.9%
Accepted name: Nα-benzyloxycarbonylleucine hydrolase
Reaction: Nα-benzyloxycarbonyl-L-leucine + H2O = benzyl alcohol + CO2 + L-leucine
Other name(s): benzyloxycarbonylleucine hydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase IV; α-N-benzyloxycarbonyl-L-leucine urethanehydrolase
Systematic name: Nα-benzyloxycarbonyl-L-leucine urethanehydrolase
Comments: Also acts on Nα-t-butoxycarbonyl-L-leucine, and, more slowly, on the corresponding derivatives of L-aspartate, L-methionine, L-glutamate and L-alanine. cf. EC 3.5.1.58 N-benzyloxycarbonylglycine hydrolase.
References:
1.  Matsumura, E., Shin, T., Murao, S., Sakaguchi, M. and Kawano, T. A novel enzyme, Nα-benzyloxycarbonyl amino acid urethane hydrolase IV. Agric. Biol. Chem. 49 (1985) 3643–3645.
[EC 3.5.1.64 created 1989]
 
 
EC 3.1.3.2     Relevance: 13.8%
Accepted name: acid phosphatase
Reaction: a phosphate monoester + H2O = an alcohol + phosphate
Other name(s): acid phosphomonoesterase; phosphomonoesterase; glycerophosphatase; acid monophosphatase; acid phosphohydrolase; acid phosphomonoester hydrolase; uteroferrin; acid nucleoside diphosphate phosphatase; orthophosphoric-monoester phosphohydrolase (acid optimum)
Systematic name: phosphate-monoester phosphohydrolase (acid optimum)
Comments: Wide specificity. Also catalyses transphosphorylations.
References:
1.  Joyce, B.K. and Grisolia, S. Purification and properties of a nonspecific acid phosphatase from wheat germ. J. Biol. Chem. 235 (1960) 2278–2281. [PMID: 14408027]
2.  Kuo, M.-H. and Blumenthal, H.J. Purification and properties of an acid phosphomonoesterase from Neurospora crassa. Biochim. Biophys. Acta 52 (1961) 13–29. [PMID: 14460641]
3.  Tsuboi, K.K., Wiener, G. and Hudson, P.B. Acid phosphatase. VII. Yeast phosphomonoesterase; isolation procedure and stability characteristics. J. Biol. Chem. 224 (1957) 621–635. [PMID: 13405892]
[EC 3.1.3.2 created 1961]
 
 
EC 1.1.1.314      
Deleted entry: germacrene A alcohol dehydrogenase. Now known to be catalyzed by EC 1.14.14.95, germacrene A hydroxylase
[EC 1.1.1.314 created 2011, deleted 2018]
 
 
EC 1.2.99.4      
Transferred entry: formaldehyde dismutase. Now EC 1.2.98.1, formaldehyde dismutase.
[EC 1.2.99.4 created 1986, modified 2012, deleted 2015]
 
 
EC 3.5.1.58     Relevance: 13.6%
Accepted name: N-benzyloxycarbonylglycine hydrolase
Reaction: N-benzyloxycarbonylglycine + H2O = benzyl alcohol + CO2 + glycine
Other name(s): benzyloxycarbonylglycine hydrolase; Nα-carbobenzoxyamino acid amidohydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase I
Systematic name: N-benzyloxycarbonylglycine urethanehydrolase
Comments: Also acts, more slowly, on N-benzyloxycarbonylalanine, but not on the corresponding derivatives of other amino acids or on N-benzyloxycarbonylpeptides. Requires Co2+ or Zn2+. cf. EC 3.5.1.64, Nα-benzyloxycarbonylleucine hydrolase.
References:
1.  Murao, S., Matsumura, E. and Kawano, T. Isolation and characterization of a novel enzyme, N α-benzyloxycarbonyl amino acid urethane hydrolase, from Streptococcus faecalis R ATCC 8043. Agric. Biol. Chem. 49 (1985) 967–972.
[EC 3.5.1.58 created 1989]
 
 
EC 3.1.1.117     Relevance: 13.5%
Accepted name: (4-O-methyl)-D-glucuronate—lignin esterase
Reaction: a 4-O-methyl-D-glucopyranuronate ester + H2O = 4-O-methyl-D-glucuronic acid + an alcohol
Other name(s): glucuronoyl esterase (ambiguous); 4-O-methyl-glucuronoyl methylesterase; glucuronoyl-lignin ester hydrolase
Systematic name: (4-O-methyl)-D-glucuronate—lignin ester hydrolase
Comments: The enzyme occurs in microorganisms and catalyses the cleavage of the ester bonds between glucuronoyl or 4-O-methyl-glucuronoyl groups attached to xylan and aliphatic or aromatic alcohols in lignin polymers.
References:
1.  Spanikova, S. and Biely, P. Glucuronoyl esterase--novel carbohydrate esterase produced by Schizophyllum commune. FEBS Lett. 580 (2006) 4597–4601. [PMID: 16876163]
2.  Charavgi, M.D., Dimarogona, M., Topakas, E., Christakopoulos, P. and Chrysina, E.D. The structure of a novel glucuronoyl esterase from Myceliophthora thermophila gives new insights into its role as a potential biocatalyst. Acta Crystallogr. D Biol. Crystallogr. 69 (2013) 63–73. [PMID: 23275164]
3.  Arnling Baath, J., Giummarella, N., Klaubauf, S., Lawoko, M. and Olsson, L. A glucuronoyl esterase from Acremonium alcalophilum cleaves native lignin-carbohydrate ester bonds. FEBS Lett. 590 (2016) 2611–2618. [PMID: 27397104]
4.  Huttner, S., Klaubauf, S., de Vries, R.P. and Olsson, L. Characterisation of three fungal glucuronoyl esterases on glucuronic acid ester model compounds. Appl. Microbiol. Biotechnol. 101 (2017) 5301–5311. [PMID: 28429057]
5.  Huynh, H.H. and Arioka, M. Functional expression and characterization of a glucuronoyl esterase from the fungus Neurospora crassa: identification of novel consensus sequences containing the catalytic triad. J. Gen. Appl. Microbiol. 62 (2016) 217–224. [PMID: 27600355]
6.  Arnling Baath, J., Mazurkewich, S., Knudsen, R.M., Poulsen, J.N., Olsson, L., Lo Leggio, L. and Larsbrink, J. Biochemical and structural features of diverse bacterial glucuronoyl esterases facilitating recalcitrant biomass conversion. Biotechnol Biofuels 11:213 (2018). [PMID: 30083226]
7.  Mazurkewich, S., Poulsen, J.N., Lo Leggio, L. and Larsbrink, J. Structural and biochemical studies of the glucuronoyl esterase OtCE15A illuminate its interaction with lignocellulosic components. J. Biol. Chem. 294 (2019) 19978–19987. [PMID: 31740581]
8.  Ernst, H.A., Mosbech, C., Langkilde, A.E., Westh, P., Meyer, A.S., Agger, J.W. and Larsen, S. The structural basis of fungal glucuronoyl esterase activity on natural substrates. Nat. Commun. 11:1026 (2020). [PMID: 32094331]
[EC 3.1.1.117 created 2021]
 
 
EC 4.2.3.2     Relevance: 13.5%
Accepted name: ethanolamine-phosphate phospho-lyase
Reaction: ethanolamine phosphate + H2O = acetaldehyde + NH3 + phosphate
Other name(s): O-phosphoethanolamine-phospholyase; amino alcohol O-phosphate phospholyase; O-phosphorylethanol-amine phospho-lyase; ethanolamine-phosphate phospho-lyase (deaminating)
Systematic name: ethanolamine-phosphate phosphate-lyase (deaminating; acetaldehyde-forming)
Comments: A pyridoxal-phosphate protein. Also acts on D(or L)-1-aminopropan-2-ol O-phosphate.
References:
1.  Fleshood, H.L. and Pitot, H.C. The metabolism of O-phosphorylethanolamine in animal tissues. I. O-Phosphorylethanolamine phospho-lyase: partial purification and characterization. J. Biol. Chem. 245 (1970) 4414–4420. [PMID: 5498429]
2.  Jones, A., Faulkner, A. and Turner, J.M. Microbial metabolism of amino alcohols. Metabolism of ethanolamine and 1-aminopropan-2-ol in species of Erwinia and the roles of amino alcohol kinase and amino alcohol o-phosphate phospho-lyase in aldehyde formation. Biochem. J. 134 (1973) 959–968. [PMID: 4357716]
[EC 4.2.3.2 created 1972 as EC 4.2.99.7, transferred 2000 to EC 4.2.3.2]
 
 
EC 1.17.99.1      
Transferred entry: 4-methylphenol dehydrogenase (hydroxylating). Now EC 1.17.9.1, 4-methylphenol dehydrogenase (hydroxylating)
[EC 1.17.99.1 created 1983, modified 2001, modified 2011, modified 2015, deleted 2018]
 
 
EC 3.2.1.149     Relevance: 13.3%
Accepted name: β-primeverosidase
Reaction: a 6-O-(β-D-xylopyranosyl)-β-D-glucopyranoside + H2O = 6-O-(β-D-xylopyranosyl)-β-D-glucopyranose + an alcohol
Glossary: primeverose = 6-O-(β-D-xylopyranosyl)-D-glucose
vicianose = 6-O-(α-L-arabinopyranosyl)-D-glucose
Systematic name: 6-O-(β-D-xylopyranosyl)-β-D-glucopyranoside 6-O-(β-D-xylosyl)-β-D-glucohydrolase
Comments: The enzyme is responsible for the formation of the alcoholic aroma in oolong and black tea. In addition to β-primeverosides [i.e. 6-O-(β-D-xylopyranosyl)-β-D-glucopyranosides], it also hydrolyses 6-O-(β-D-apiofuranosyl)-β-D-glucopyranosides and, less rapidly, β-vicianosides and 6-O-(α-L-arabinofuranosyl)-β-D-glucopyranosides, but not β-glucosides. Geranyl-, linaloyl-, benzyl- and p-nitrophenol glycosides are all hydrolysed.
References:
1.  Ijima, Y., Ogawa, K., Watanabe, N., Usui, T., Ohnishi-Kameyama, M., Nagata, T. and Sakata, K. Characterization of β-primeverosidase, being concerned with alcoholic aroma formation in tea leaves to be processed into black tea, and preliminary observations on its substrate specificity. J. Agric. Food Chem. 46 (1998) 1712–1718.
2.  Ogawa, K., Ijima, Y., Guo, W., Watanabe, N., Usui, T., Dong, S., Tong, Q. and Sakata, K. Purification of a β-primeverosidase concerned with alcoholic aroma formation in tea leaves (cv. Shuxian) to be processed to oolong tea. J. Agric. Food Chem. 45 (1997) 877–882.
[EC 3.2.1.149 created 2001]
 
 
EC 1.11.1.13     Relevance: 13.3%
Accepted name: manganese peroxidase
Reaction: 2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
Other name(s): peroxidase-M2; Mn-dependent (NADH-oxidizing) peroxidase
Systematic name: Mn(II):hydrogen-peroxide oxidoreductase
Comments: A hemoprotein. The enzyme from white rot basidiomycetes is involved in the oxidative degradation of lignin. The enzyme oxidizes a bound Mn2+ ion to Mn3+ in the presence of hydrogen peroxide. The product, Mn3+, is released from the active site in the presence of a chelator (mostly oxalate and malate) that stabilizes it against disproportionation to Mn2+ and insoluble Mn4+ [4]. The complexed Mn3+ ion can diffuse into the lignified cell wall, where it oxidizes phenolic components of lignin and other organic substrates [1]. It is inactive with veratryl alcohol or nonphenolic substrates.
References:
1.  Glenn, J.K., Akileswaran, L. and Gold, M.H. Mn(II) oxidation is the principal function of the extracellular Mn-peroxidase from Phanerochaete chrysosporium. Arch. Biochem. Biophys. 251 (1986) 688–696. [PMID: 3800395]
2.  Paszczynski, A., Huynh, V.-B. and Crawford, R. Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium. Arch. Biochem. Biophys. 244 (1986) 750–765. [PMID: 3080953]
3.  Wariishi, H., Akileswaran, L. and Gold, M.H. Manganese peroxidase from the basidiomycete Phanerochaete chrysosporium: spectral characterization of the oxidized states and the catalytic cycle. Biochemistry 27 (1988) 5365–5370. [PMID: 3167051]
4.  Kuan, I.C. and Tien, M. Stimulation of Mn peroxidase activity: a possible role for oxalate in lignin biodegradation. Proc. Natl. Acad. Sci. USA 90 (1993) 1242–1246. [PMID: 8433984]
[EC 1.11.1.13 created 1992]
 
 
EC 1.1.3.41     Relevance: 13.1%
Accepted name: alditol oxidase
Reaction: an alditol + O2 = an aldose + H2O2
Other name(s): xylitol oxidase; xylitol:oxygen oxidoreductase; AldO
Systematic name: alditol:oxygen oxidoreductase
Comments: The enzyme from Streptomyces sp. IKD472 and from Streptomyces coelicolor is a monomeric oxidase containing one molecule of FAD per molecule of protein [1,2]. While xylitol (five carbons) and sorbitol (6 carbons) are the preferred substrates, other alditols, including L-threitol (four carbons), D-arabinitol (five carbons), D-galactitol (six carbons) and D-mannitol (six carbons) can also act as substrates, but more slowly [1,2]. Belongs in the vanillyl-alcohol-oxidase family of enzymes [2].
References:
1.  Yamashita, M., Omura, H., Okamoto, E., Furuya, Y., Yabuuchi, M., Fukahi, K. and Murooka, Y. Isolation, characterization, and molecular cloning of a thermostable xylitol oxidase from Streptomyces sp. IKD472. J. Biosci. Bioeng. 89 (2000) 350–360. [PMID: 16232758]
2.  Heuts, D.P., van Hellemond, E.W., Janssen, D.B. and Fraaije, M.W. Discovery, characterization, and kinetic analysis of an alditol oxidase from Streptomyces coelicolor. J. Biol. Chem. 282 (2007) 20283–20291. [PMID: 17517896]
3.  Forneris, F., Heuts, D.P., Delvecchio, M., Rovida, S., Fraaije, M.W. and Mattevi, A. Structural analysis of the catalytic mechanism and stereoselectivity in Streptomyces coelicolor alditol oxidase. Biochemistry 47 (2008) 978–985. [PMID: 18154360]
[EC 1.1.3.41 created 2002, modified 2008]
 
 
EC 1.14.19.19     Relevance: 13.1%
Accepted name: sphingolipid 10-desaturase
Reaction: a (4E,8E)-sphinga-4,8-dienine ceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4E,8E,10E)-sphinga-4,8,10-trienine ceramide + 2 ferricytochrome b5 + 2 H2O
Other name(s): desA (gene name)
Systematic name: a (4E,8E)-sphinga-4,8-dienine ceramide,ferrocytochrome b5:oxygen oxidoreductase (10,11 trans-dehydrogenating)
Comments: The enzyme, characterized from the marine diatom Thalassiosira pseudonana, produces an all-trans product. Similar triunsaturated sphingoid bases are found in some marine invertebrates. The enzyme determines the position of the double bond by its distance from the alcohol end of the sphingoid base, and contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase.
References:
1.  Michaelson, L.V., Markham, J.E., Zäuner, S., Matsumoto, M., Chen, M., Cahoon, E.B. and Napier, J.A. Identification of a cytochrome b5-fusion desaturase responsible for the synthesis of triunsaturated sphingolipid long chain bases in the marine diatom Thalassiosira pseudonana. Phytochemistry 90 (2013) 50–55. [PMID: 23510654]
[EC 1.14.19.19 created 2015]
 
 
EC 3.1.8.1     Relevance: 12.9%
Accepted name: aryldialkylphosphatase
Reaction: an aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol
Other name(s): organophosphate hydrolase; paraoxonase; A-esterase; aryltriphosphatase; organophosphate esterase; esterase B1; esterase E4; paraoxon esterase; pirimiphos-methyloxon esterase; OPA anhydrase (ambiguous); organophosphorus hydrolase; phosphotriesterase; paraoxon hydrolase; OPH; organophosphorus acid anhydrase
Systematic name: aryltriphosphate dialkylphosphohydrolase
Comments: Acts on organophosphorus compounds (such as paraoxon) including esters of phosphonic and phosphinic acids. Inhibited by chelating agents; requires divalent cations for activity. Previously regarded as identical with EC 3.1.1.2 arylesterase.
References:
1.  Aldridge, W.N. Serum esterases. I. Two types of esterase (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate and a method for their determination. Biochem. J. 53 (1953) 110–117. [PMID: 13032041]
2.  Bosmann, H.B. Membrane marker enzymes. Characterization of an arylesterase of guinea pig cerebral cortex utilizing p-nitrophenyl acetate as substrate. Biochim. Biophys. Acta 276 (1972) 180–191. [PMID: 5047702]
3.  Mackness, M.I., Thompson, H.M., Hardy, A.R. and Walker, C.H. Distinction between 'A′-esterases and arylesterases. Implications for esterase classification. Biochem. J. 245 (1987) 293–296. [PMID: 2822017]
4.  Main, A.R. The differentiation of the A-type esterases in sheep serum. Biochem. J. 75 (1960) 188–195. [PMID: 14420012]
5.  Reiner, E., Aldridge, W.N. and Hoskin, C.G. (Ed.), Enzymes Hydrolysing Organophosphorus Compounds, Ellis Horwood, Chichester, UK, 1989.
[EC 3.1.8.1 created 1989]
 
 
EC 1.1.1.55     Relevance: 12.8%
Accepted name: lactaldehyde reductase (NADPH)
Reaction: propane-1,2-diol + NADP+ = L-lactaldehyde + NADPH + H+
Other name(s): lactaldehyde (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADP-1,2-propanediol dehydrogenase; propanediol dehydrogenase; 1,2-propanediol:NADP+ oxidoreductase; lactaldehyde reductase (NADPH2)
Systematic name: propane-1,2-diol:NADP+ oxidoreductase
Comments: May be identical with EC 1.1.1.2 alcohol dehydrogenase (NADP+).
References:
1.  Gupta, N.K. and Robinson, W.G. The enzymatic conversion of lactaldehyde to propanediol. J. Biol. Chem. 235 (1960) 1609–1612. [PMID: 13830319]
[EC 1.1.1.55 created 1965]
 
 
EC 3.1.7.10     Relevance: 12.8%
Accepted name: (13E)-labda-7,13-dien-15-ol synthase
Reaction: geranylgeranyl diphosphate + H2O = (13E)-labda-7,13-dien-15-ol + diphosphate
Other name(s): labda-7,13E-dien-15-ol synthase
Systematic name: geranylgeranyl-diphosphate diphosphohydrolase [(13E)-labda-7,13-dien-15-ol-forming]
Comments: The enzyme from the lycophyte Selaginella moellendorffii is bifunctional, initially forming (13E)-labda-7,13-dien-15-yl diphosphate, which is hydrolysed to the alcohol.
References:
1.  Mafu, S., Hillwig, M.L. and Peters, R.J. A novel labda-7,13E-dien-15-ol-producing bifunctional diterpene synthase from Selaginella moellendorffii. ChemBioChem 12 (2011) 1984–1987. [PMID: 21751328]
[EC 3.1.7.10 created 2012]
 
 
EC 3.5.1.137     Relevance: 12.7%
Accepted name: N-methylcarbamate hydrolase
Reaction: an N-methyl carbamate ester + H2O = an alcohol + methylamine + CO2
Glossary: carbaryl = N-methyl-1-naphthyl carbamate
Other name(s): mcbA (gene name); cehA (gene name); cfdJ (gene name); carbaryl hydrolase; carbofuran hydrolase
Systematic name: N-methyl carbamate ester hydrolase
Comments: The enzyme catalyses the first step in the degradation of several carbamate insecticides such as carbaryl, carbofuran, isoprocarb, propoxur, aldicarb and oxamyl. It catalyses the cleavage of the ester bond to release N-methylcarbamate, which spontaneously hydrolyses to methylamine and CO2. The enzymes from several Gram-negative bacteria were shown to be located in the periplasm.
References:
1.  Mulbry, W.W. and Eaton, R.W. Purification and characterization of the N-methylcarbamate hydrolase from Pseudomonas strain CRL-OK. Appl. Environ. Microbiol. 57 (1991) 3679–3682. [PMID: 1785941]
2.  Hayatsu, M. and Nagata, T. Purification and characterization of carbaryl hydrolase from Blastobacter sp. strain M501. Appl. Environ. Microbiol. 59 (1993) 2121–2125. [PMID: 16348989]
3.  Chapalmadugu, S. and Chaudhry, G.R. Isolation of a constitutively expressed enzyme for hydrolysis of carbaryl in Pseudomonas aeruginosa. J. Bacteriol. 175 (1993) 6711–6716. [PMID: 8407847]
4.  Hayatsu, M., Mizutani, A., Hashimoto, M., Sato, K. and Hayano, K. Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100. FEMS Microbiol. Lett. 201 (2001) 99–103. [PMID: 11445174]
5.  Hashimoto, M., Fukui, M., Hayano, K. and Hayatsu, M. Nucleotide sequence and genetic structure of a novel carbaryl hydrolase gene (cehA) from Rhizobium sp. strain AC100. Appl. Environ. Microbiol. 68 (2002) 1220–1227. [PMID: 11872471]
6.  Zhang, Q., Liu, Y. and Liu, Y.H. Purification and characterization of a novel carbaryl hydrolase from Aspergillus niger PY168. FEMS Microbiol. Lett. 228 (2003) 39–44. [PMID: 14612234]
7.  Ozturk, B., Ghequire, M., Nguyen, T.P., De Mot, R., Wattiez, R. and Springael, D. Expanded insecticide catabolic activity gained by a single nucleotide substitution in a bacterial carbamate hydrolase gene. Environ. Microbiol. 18 (2016) 4878–4887. [PMID: 27312345]
8.  Kamini, Shetty, D., Trivedi, V.D., Varunjikar, M. and Phale, P.S. Compartmentalization of the carbaryl degradation pathway: molecular characterization of inducible periplasmic carbaryl hydrolase from Pseudomonas spp. Appl. Environ. Microbiol. 84:e02115-17 (2018). [PMID: 29079626]
9.  Yan, X., Jin, W., Wu, G., Jiang, W., Yang, Z., Ji, J., Qiu, J., He, J., Jiang, J. and Hong, Q. Hydrolase CehA and monooxygenase CfdC are responsible for carbofuran degradation in Sphingomonas sp. strain CDS-1. Appl. Environ. Microbiol. 84 (2018) . [PMID: 29884759]
10.  Jiang, W., Gao, Q., Zhang, L., Wang, H., Zhang, M., Liu, X., Zhou, Y., Ke, Z., Wu, C., Qiu, J. and Hong, Q. Identification of the key amino acid sites of the carbofuran hydrolase CehA from a newly isolated carbofuran-degrading strain Sphingbium sp. CFD-1. Ecotoxicol Environ Saf 189:109938 (2020). [PMID: 31759739]
[EC 3.5.1.137 created 2021]
 
 
EC 4.2.3.39     Relevance: 12.6%
Accepted name: epi-cedrol synthase
Reaction: (2E,6E)-farnesyl diphosphate + H2O = 8-epi-cedrol + diphosphate
Other name(s): 8-epicedrol synthase; epicedrol synthase
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (8-epi-cedrol-forming)
Comments: The enzyme is activated by Mg2+ [2]. Similar to many other plant terpenoid synthases, this enzyme produces many products from a single substrate. The predominant product is the cyclic sesquiterpenoid alcohol, 8-epi-cedrol, with minor products including cedrol and the olefins α-cedrene, β-cedrene, (E)-β-farnesene and (E)-α-bisabolene [1].
References:
1.  Mercke, P., Crock, J., Croteau, R. and Brodelius, P.E. Cloning, expression, and characterization of epi-cedrol synthase, a sesquiterpene cyclase from Artemisia annua L. Arch. Biochem. Biophys. 369 (1999) 213–222. [PMID: 10486140]
2.  Hua, L. and Matsuda, S.P. The molecular cloning of 8-epicedrol synthase from Artemisia annua. Arch. Biochem. Biophys. 369 (1999) 208–212. [PMID: 10486139]
[EC 4.2.3.39 created 2009]
 
 
EC 1.2.98.1     Relevance: 12.6%
Accepted name: formaldehyde dismutase
Reaction: 2 formaldehyde + H2O = formate + methanol
Other name(s): aldehyde dismutase; cannizzanase; nicotinoprotein aldehyde dismutase
Systematic name: formaldehyde:formaldehyde oxidoreductase
Comments: The enzyme contains a tightly but noncovalently bound NADP(H) cofactor, as well as Zn2+ and Mg2+. Enzyme-bound NADPH formed by oxidation of formaldehyde to formate is oxidized back to NADP+ by reaction with a second formaldehyde, yielding methanol. The enzyme from the bacterium Mycobacterium sp. DSM 3803 also catalyses the reactions of EC 1.1.99.36, alcohol dehydrogenase (nicotinoprotein) and EC 1.1.99.37, methanol dehydrogenase (nicotinoprotein) [3]. Formaldehyde and acetaldehyde can act as donors; formaldehyde, acetaldehyde and propanal can act as acceptors [1,2].
References:
1.  Kato, N., Shirakawa, K., Kobayashi, H. and Sakazawa, C. The dismutation of aldehydes by a bacterial enzyme. Agric. Biol. Chem. 47 (1983) 39–46.
2.  Kato, N., Yamagami, T., Shimao, M. and Sakazawa, C. Formaldehyde dismutase, a novel NAD-binding oxidoreductase from Pseudomonas putida F61. Eur. J. Biochem. 156 (1986) 59–64. [PMID: 3514215]
3.  Park, H., Lee, H., Ro, Y.T. and Kim, Y.M. Identification and functional characterization of a gene for the methanol : N,N′-dimethyl-4-nitrosoaniline oxidoreductase from Mycobacterium sp. strain JC1 (DSM 3803). Microbiology 156 (2010) 463–471. [PMID: 19875438]
[EC 1.2.98.1 created 1986 as EC 1.2.99.4, modified 2012, transferred 2015 to EC 1.2.98.1]
 
 
EC 1.11.2.3     Relevance: 12.6%
Accepted name: plant seed peroxygenase
Reaction: R1H + R2OOH = R1OH + R2OH
Other name(s): plant peroxygenase; soybean peroxygenase
Systematic name: substrate:hydroperoxide oxidoreductase (RH-hydroxylating or epoxidising)
Comments: A heme protein with calcium binding motif (caleosin-type). Enzymes of this type include membrane-bound proteins found in seeds of different plants. They catalyse the direct transfer of one oxygen atom from an organic hydroperoxide, which is reduced into its corresponding alcohol to a substrate which will be oxidized. Reactions catalysed include hydroxylation, epoxidation and sulfoxidation. Preferred substrate and co-substrate are unsaturated fatty acids and fatty acid hydroperoxides, respectively. Plant seed peroxygenase is involved in the synthesis of cutin.
References:
1.  Ishimaru, A. Purification and characterization of solubilized peroxygenase from microsomes of pea seeds. J. Biol. Chem. 254 (1979) 8427–8433. [PMID: 468835]
2.  Blee, E., Wilcox, A.L., Marnett, L.J. and Schuber, F. Mechanism of reaction of fatty acid hydroperoxides with soybean peroxygenase. J. Biol. Chem. 268 (1993) 1708–1715. [PMID: 8420948]
3.  Hamberg, M. and Hamberg, G. Peroxygenase-catalyzed fatty acid epoxidation in cereal seeds (sequential oxidation of linoleic acid into 9(S),12(S),13(S)-trihydroxy-10(E)-octadecenoic acid). Plant Physiol. 110 (1996) 807–815. [PMID: 12226220]
4.  Lequeu, J., Fauconnier, M.L., Chammai, A., Bronner, R. and Blee, E. Formation of plant cuticle: evidence for the occurrence of the peroxygenase pathway. Plant J. 36 (2003) 155–164. [PMID: 14535881]
5.  Hanano, A., Burcklen, M., Flenet, M., Ivancich, A., Louwagie, M., Garin, J. and Blee, E. Plant seed peroxygenase is an original heme-oxygenase with an EF-hand calcium binding motif. J. Biol. Chem. 281 (2006) 33140–33151. [PMID: 16956885]
[EC 1.11.2.3 created 2011]
 
 
EC 2.3.1.299     Relevance: 12.2%
Accepted name: sphingoid base N-stearoyltransferase
Reaction: stearoyl-CoA + a sphingoid base = an N-(stearoyl)-sphingoid base + CoA
Glossary: a sphingoid base = an amino alcohol, composed predominantly of 18 carbon atoms, characterized by the presence of a hydroxyl group at C-1 (and often also at C-3), and an amine group at C-2.
Other name(s): mammalian ceramide synthase 1; LASS1 (gene name); UOG1 (gene name); CERS1 (gene name)
Systematic name: stearoyl-CoA:sphingoid base N-stearoyltransferase
Comments: Mammals have six ceramide synthases that exhibit relatively strict specificity regarding the chain-length of their acyl-CoA substrates. Ceramide synthase 1 (CERS1) is structurally and functionally distinctive from all other CERS enzymes, and is specific for stearoyl-CoA as the acyl donor. It can use multiple sphingoid bases including sphinganine, sphingosine, and phytosphingosine.
References:
1.  Venkataraman, K., Riebeling, C., Bodennec, J., Riezman, H., Allegood, J.C., Sullards, M.C., Merrill, A.H., Jr. and Futerman, A.H. Upstream of growth and differentiation factor 1 (uog1), a mammalian homolog of the yeast longevity assurance gene 1 (LAG1), regulates N-stearoyl-sphinganine (C18-(dihydro)ceramide) synthesis in a fumonisin B1-independent manner in mammalian cells. J. Biol. Chem. 277 (2002) 35642–35649. [PMID: 12105227]
2.  Kim, H.J., Qiao, Q., Toop, H.D., Morris, J.C. and Don, A.S. A fluorescent assay for ceramide synthase activity. J. Lipid Res. 53 (2012) 1701–1707. [PMID: 22661289]
3.  Wang, Z., Wen, L., Zhu, F., Wang, Y., Xie, Q., Chen, Z. and Li, Y. Overexpression of ceramide synthase 1 increases C18-ceramide and leads to lethal autophagy in human glioma. Oncotarget 8 (2017) 104022–104036. [PMID: 29262618]
4.  Turpin-Nolan, S.M., Hammerschmidt, P., Chen, W., Jais, A., Timper, K., Awazawa, M., Brodesser, S. and Bruning, J.C. CerS1-derived C18:0 ceramide in skeletal muscle promotes obesity-induced insulin resistance. Cell Rep. 26 (2019) 1–10.e7. [PMID: 30605666]
[EC 2.3.1.299 created 2019]
 
 
EC 1.1.5.2     Relevance: 12.1%
Accepted name: glucose 1-dehydrogenase (PQQ, quinone)
Reaction: D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
Other name(s): quinoprotein glucose dehydrogenase; membrane-bound glucose dehydrogenase; mGDH; glucose dehydrogenase (PQQ-dependent); glucose dehydrogenase (pyrroloquinoline-quinone); quinoprotein D-glucose dehydrogenase
Systematic name: D-glucose:ubiquinone oxidoreductase
Comments: Integral membrane protein containing PQQ as prosthetic group. It also contains bound ubiquinone and Mg2+ or Ca2+. Electron acceptor is membrane ubiquinone but usually assayed with phenazine methosulfate. Like in all other quinoprotein alcohol dehydrogenases the catalytic domain has an 8-bladed propeller structure. It occurs in a wide range of bacteria. Catalyses a direct oxidation of the pyranose form of D-glucose to the lactone and thence to D-gluconate in the periplasm. Oxidizes other monosaccharides including the pyranose forms of pentoses.
References:
1.  Yamada, M., Sumi, K., Matsushita, K., Adachi, O. and Yamada, Y. Topological analysis of quinoprotein glucose-dehydrogenase in Escherichia coli and its ubiquinone-binding site. J. Biol. Chem. 268 (1993) 12812–12817. [PMID: 8509415]
2.  Dewanti, A.R. and Duine, J.A. Reconstitution of membrane-integrated quinoprotein glucose dehydrogenase apoenzyme with PQQ and the holoenzyme's mechanism of action. Biochemistry 37 (1998) 6810–6818. [PMID: 9578566]
3.  Duine, J.A., Frank, J. and Van Zeeland, J.K. Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein'. FEBS Lett. 108 (1979) 443–446. [PMID: 520586]
4.  Ameyama, M., Matsushita, K., Ohno, Y., Shinagawa, E. and Adachi, O. Existence of a novel prosthetic group, PQQ, in membrane-bound, electron transport chain-linked, primary dehydrogenases of oxidative bacteria. FEBS Lett. 130 (1981) 179–183. [PMID: 6793395]
5.  Cozier, G.E. and Anthony, C. Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens. Biochem. J. 312 (1995) 679–685. [PMID: 8554505]
6.  Cozier, G.E., Salleh, R.A. and Anthony, C. Characterization of the membrane quinoprotein glucose dehydrogenase from Escherichia coli and characterization of a site-directed mutant in which histidine-262 has been changed to tyrosine. Biochem. J. 340 (1999) 639–647. [PMID: 10359647]
7.  Elias, M.D., Tanaka, M., Sakai, M., Toyama, H., Matsushita, K., Adachi, O. and Yamada, M. C-terminal periplasmic domain of Escherichia coli quinoprotein glucose dehydrogenase transfers electrons to ubiquinone. J. Biol. Chem. 276 (2001) 48356–48361. [PMID: 11604400]
8.  James, P.L. and Anthony, C. The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli. Biochim. Biophys. Acta 1647 (2003) 200–205. [PMID: 12686133]
9.  Elias, M.D., Nakamura, S., Migita, C.T., Miyoshi, H., Toyama, H., Matsushita, K., Adachi, O. and Yamada, M. Occurrence of a bound ubiquinone and its function in Escherichia coli membrane-bound quinoprotein glucose dehydrogenase. J. Biol. Chem. 279 (2004) 3078–3083. [PMID: 14612441]
10.  Mustafa, G., Ishikawa, Y., Kobayashi, K., Migita, C.T., Elias, M.D., Nakamura, S., Tagawa, S. and Yamada, M. Amino acid residues interacting with both the bound quinone and coenzyme, pyrroloquinoline quinone, in Escherichia coli membrane-bound glucose dehydrogenase. J. Biol. Chem. 283 (2008) 22215–22221. [PMID: 18550551]
[EC 1.1.5.2 created 1982 as EC 1.1.99.17, transferred 2003 to EC 1.1.5.2, modified 2010]
 
 
EC 3.1.1.1     Relevance: 12%
Accepted name: carboxylesterase
Reaction: a carboxylic ester + H2O = an alcohol + a carboxylate
Other name(s): ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase
Systematic name: carboxylic-ester hydrolase
Comments: Wide specificity. The enzymes from microsomes also catalyse the reactions of EC 3.1.1.2 (arylesterase), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.6 (acetylesterase), EC 3.1.1.23 (acylglycerol lipase), EC 3.1.1.28 (acylcarnitine hydrolase), EC 3.1.2.2 (palmitoyl-CoA hydrolase), EC 3.5.1.4 (amidase) and EC 3.5.1.13 (aryl-acylamidase). Also hydrolyses vitamin A esters.
References:
1.  Augusteyn, R.C., de Jersey, J., Webb, E.C. and Zerner, B. On the homology of the active-site peptides of liver carboxylesterases. Biochim. Biophys. Acta 171 (1969) 128–137. [PMID: 4884138]
2.  Barker, D.L. and Jencks, W.P. Pig liver esterase. Physical properties. Biochemistry 8 (1969) 3879–3889. [PMID: 4981346]
3.  Bertram, J. and Krisch, K. Hydrolysis of vitamin A acetate by unspecific carboxylesterases from liver and kidney. Eur. J. Biochem. 11 (1969) 122–126. [PMID: 5353595]
4.  Burch, J. The purification and properties of horse liver esterase. Biochem. J. 58 (1954) 415–426. [PMID: 13208632]
5.  Horgan, D.J., Stoops, J.K., Webb, E.C. and Zerner, B. Carboxylesterases (EC 3.1.1). A large-scale purification of pig liver carboxylesterase. Biochemistry 8 (1969) 2000–2006. [PMID: 5785220]
6.  Malhotra, O.P. and Philip, G. Specificity of goat intestinal esterase. Biochem. Z. 346 (1966) 386–402.
7.  Mentlein, R., Schumann, M. and Heymann, E. Comparative chemical and immunological characterization of five lipolytic enzymes (carboxylesterases) from rat liver microsomes. Arch. Biochem. Biophys. 234 (1984) 612–621. [PMID: 6208846]
8.  Runnegar, M.T.C., Scott, K., Webb, E.C. and Zerner, B. Carboxylesterases (EC 3.1.1). Purification and titration of ox liver carboxylesterase. Biochemistry 8 (1969) 2013–2018. [PMID: 5785222]
[EC 3.1.1.1 created 1961]
 
 
EC 1.1.1.324     Relevance: 11.8%
Accepted name: 8-hydroxygeraniol dehydrogenase
Reaction: (6E)-8-hydroxygeraniol + 2 NADP+ = (6E)-8-oxogeranial + 2 NADPH + 2 H+ (overall reaction)
(1a) (6E)-8-hydroxygeraniol + NADP+ = (6E)-8-hydroxygeranial + NADPH + H+
(1b) (6E)-8-hydroxygeraniol + NADP+ = (6E)-8-oxogeraniol + NADPH + H+
(1c) (6E)-8-hydroxygeranial + NADP+ = (6E)-8-oxogeranial + NADPH + H+
(1d) (6E)-8-oxogeraniol + NADP+ = (6E)-8-oxogeranial + NADPH + H+
Other name(s): 8-hydroxygeraniol oxidoreductase; CYP76B10; G10H; CrG10H; SmG10H; acyclic monoterpene primary alcohol:NADP+ oxidoreductase
Systematic name: (6E)-8-hydroxygeraniol:NADP+ oxidoreductase
Comments: Contains Zn2+. The enzyme catalyses the oxidation of (6E)-8-hydroxygeraniol to (6E)-8-oxogeranial via either (6E)-8-hydroxygeranial or (6E)-8-oxogeraniol. Also acts on geraniol, nerol and citronellol. May be identical to EC 1.1.1.183 geraniol dehydrogenase. The recommended numbering of geraniol gives 8-hydroxygeraniol as the substrate rather than 10-hydroxygeraniol as used by references 1 and 2. See prenol nomenclature Pr-1.
References:
1.  Ikeda, H., Esaki, N., Nakai, S., Hashimoto, K., Uesato, S., Soda, K. and Fujita, T. Acyclic monoterpene primary alcohol:NADP+ oxidoreductase of Rauwolfia serpentina cells: the key enzyme in biosynthesis of monoterpene alcohols. J. Biochem. 109 (1991) 341–347. [PMID: 1864846]
2.  Hallahan, D.L., West, J.M., Wallsgrove, R.M., Smiley, D.W., Dawson, G.W., Pickett, J.A. and Hamilton, J.G. Purification and characterization of an acyclic monoterpene primary alcohol:NADP+ oxidoreductase from catmint (Nepeta racemosa). Arch. Biochem. Biophys. 318 (1995) 105–112. [PMID: 7726550]
[EC 1.1.1.324 created 2012]
 
 
EC 1.14.13.221      
Transferred entry: cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming]. Now EC 1.14.15.28, cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming]
[EC 1.14.13.221 created 2016, deleted 2018]
 
 
EC 1.14.15.25     Relevance: 11.6%
Accepted name: p-cymene methyl-monooxygenase
Reaction: p-cymene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = 4-isopropylbenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Glossary: p-cymene = 4-methyl-1-(propan-2-yl)benzene
Other name(s): cymAa (gene name); cymA (gene name); p-cymene methyl hydroxylase
Systematic name: p-cymene,ferredoxin:oxygen oxidoreductase (methyl-hydroxylating)
Comments: The enzyme, characterized from several Pseudomonas strains, initiates p-cymene catabolism through hydroxylation of the methyl group. The enzyme has a distinct preference for substrates containing at least an alkyl or heteroatom substituent at the para-position of toluene. The electrons are provided by a reductase (EC 1.18.1.3, ferredoxin—NAD+ reductase) that transfers electrons from NADH via FAD and an [2Fe-2S] cluster. In Pseudomonas chlororaphis the presence of a third component of unknown function greatly increases the activity. cf. EC 1.14.15.26, toluene methyl-monooxygenase.
References:
1.  Eaton, R.W. p-Cymene catabolic pathway in Pseudomonas putida F1: cloning and characterization of DNA encoding conversion of p-cymene to p-cumate. J. Bacteriol. 179 (1997) 3171–3180. [PMID: 9150211]
2.  Dutta, T.K. and Gunsalus, I.C. Reductase gene sequences and protein structures: p-cymene methyl hydroxylase. Biochem. Biophys. Res. Commun. 233 (1997) 502–506. [PMID: 9144566]
3.  Nishio, T., Patel, A., Wang, Y. and Lau, P.C. Biotransformations catalyzed by cloned p-cymene monooxygenase from Pseudomonas putida F1. Appl. Microbiol. Biotechnol. 55 (2001) 321–325. [PMID: 11341314]
4.  Dutta, T.K., Chakraborty, J., Roy, M., Ghosal, D., Khara, P. and Gunsalus, I.C. Cloning and characterization of a p-cymene monooxygenase from Pseudomonas chlororaphis subsp. aureofaciens. Res. Microbiol. 161 (2010) 876–882. [PMID: 21035544]
[EC 1.14.15.25 created 2018]
 
 
EC 1.11.1.19     Relevance: 11.5%
Accepted name: dye decolorizing peroxidase
Reaction: Reactive Blue 5 + 2 H2O2 = phthalate + 2,2′-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
Glossary: Reactive Blue 5 = 1-amino-4-{[3-({4-chloro-6-[(3-sulfophenyl)amino]-1,3,5-triazin-2-yl}amino)-4-sulfophenyl]amino}-9,10-dihydro-9,10-dioxoanthracene-2-sulfonic acid
Other name(s): DyP; DyP-type peroxidase
Systematic name: Reactive-Blue-5:hydrogen-peroxide oxidoreductase
Comments: Heme proteins with proximal histidine secreted by basidiomycetous fungi and eubacteria. They are similar to EC 1.11.1.16 versatile peroxidase (oxidation of Reactive Black 5, phenols, veratryl alcohol), but differ from the latter in their ability to efficiently oxidize a number of recalcitrant anthraquinone dyes, and inability to oxidize Mn(II). The model substrate Reactive Blue 5 is converted with high efficiency via a so far unique mechanism that combines oxidative and hydrolytic steps and leads to the formation of phthalic acid. Bacterial TfuDyP catalyses sulfoxidation.
References:
1.  Kim, S.J. and Shoda, M. Purification and characterization of a novel peroxidase from Geotrichum candidum dec 1 involved in decolorization of dyes. Appl. Environ. Microbiol. 65 (1999) 1029–1035. [PMID: 10049859]
2.  Sugano, Y., Ishii, Y. and Shoda, M. Role of H164 in a unique dye-decolorizing heme peroxidase DyP. Biochem. Biophys. Res. Commun. 322 (2004) 126–132. [PMID: 15313183]
3.  Zubieta, C., Joseph, R., Krishna, S.S., McMullan, D., Kapoor, M., Axelrod, H.L., Miller, M.D., Abdubek, P., Acosta, C., Astakhova, T., Carlton, D., Chiu, H.J., Clayton, T., Deller, M.C., Duan, L., Elias, Y., Elsliger, M.A., Feuerhelm, J., Grzechnik, S.K., Hale, J., Han, G.W., Jaroszewski, L., Jin, K.K., Klock, H.E., Knuth, M.W., Kozbial, P., Kumar, A., Marciano, D., Morse, A.T., Murphy, K.D., Nigoghossian, E., Okach, L., Oommachen, S., Reyes, R., Rife, C.L., Schimmel, P., Trout, C.V., van den Bedem, H., Weekes, D., White, A., Xu, Q., Hodgson, K.O., Wooley, J., Deacon, A.M., Godzik, A., Lesley, S.A. and Wilson, I.A. Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA. Proteins 69 (2007) 234–243. [PMID: 17654547]
4.  Sugano, Y., Matsushima, Y., Tsuchiya, K., Aoki, H., Hirai, M. and Shoda, M. Degradation pathway of an anthraquinone dye catalyzed by a unique peroxidase DyP from Thanatephorus cucumeris Dec 1. Biodegradation 20 (2009) 433–440. [PMID: 19009358]
5.  Sugano, Y. DyP-type peroxidases comprise a novel heme peroxidase family. Cell. Mol. Life Sci. 66 (2009) 1387–1403. [PMID: 19099183]
6.  Ogola, H.J., Kamiike, T., Hashimoto, N., Ashida, H., Ishikawa, T., Shibata, H. and Sawa, Y. Molecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. strain PCC 7120. Appl. Environ. Microbiol. 75 (2009) 7509–7518. [PMID: 19801472]
7.  van Bloois, E., Torres Pazmino, D.E., Winter, R.T. and Fraaije, M.W. A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily. Appl. Microbiol. Biotechnol. 86 (2010) 1419–1430. [PMID: 19967355]
8.  Liers, C., Bobeth, C., Pecyna, M., Ullrich, R. and Hofrichter, M. DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and high-redox potential dyes. Appl. Microbiol. Biotechnol. 85 (2010) 1869–1879. [PMID: 19756587]
9.  Hofrichter, M., Ullrich, R., Pecyna, M.J., Liers, C. and Lundell, T. New and classic families of secreted fungal heme peroxidases. Appl. Microbiol. Biotechnol. 87 (2010) 871–897. [PMID: 20495915]
[EC 1.11.1.19 created 2011, modified 2015]
 
 
EC 1.14.19.18     Relevance: 11.4%
Accepted name: sphingolipid 8-(E)-desaturase
Reaction: a (4E)-sphing-4-enine ceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4E,8E)-sphing-4,8-dienine ceramide + 2 ferricytochrome b5 + 2 H2O
Other name(s): 8-sphingolipid desaturase (ambiguous); 8 fatty acid desaturase (ambiguous); DELTA8-sphingolipid desaturase (ambiguous)
Systematic name: (4E)-sphing-4-enine ceramide,ferrocytochrome b5:oxygen oxidoreductase (8,9-trans dehydrogenating)
Comments: The enzyme, characterized from the yeasts Kluyveromyces lactis and Candida albicans [1] and from the diatom Thalassiosira pseudonana [2], introduces a trans double bond at the 8-position of sphingoid bases in sphingolipids. The enzyme determines the position of the double bond by its distance from the alcohol end of the sphingoid base, and contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase [3]. The homologous enzymes from higher plants, EC 1.14.19.29, sphingolipid 8-(E/Z)-desaturase, act on phytosphinganine (4-hydroxysphinganine) and produces a mixture of trans and cis isomers.
References:
1.  Takakuwa, N., Kinoshita, M., Oda, Y. and Ohnishi, M. Isolation and characterization of the genes encoding Δ8-sphingolipid desaturase from Saccharomyces kluyveri and Kluyveromyces lactis. Curr. Microbiol. 45 (2002) 459–461. [PMID: 12402089]
2.  Tonon, T., Sayanova, O., Michaelson, L.V., Qing, R., Harvey, D., Larson, T.R., Li, Y., Napier, J.A. and Graham, I.A. Fatty acid desaturases from the microalga Thalassiosira pseudonana. FEBS J. 272 (2005) 3401–3412. [PMID: 15978045]
3.  Oura, T. and Kajiwara, S. Disruption of the sphingolipid Δ8-desaturase gene causes a delay in morphological changes in Candida albicans. Microbiology 154 (2008) 3795–3803. [PMID: 19047747]
[EC 1.14.19.18 created 2015]
 
 
EC 1.14.15.28     Relevance: 11.1%
Accepted name: cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming]
Reaction: cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 = (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O (overall reaction)
(1a) cholest-4-en-3-one + 2 reduced [2Fe-2S] ferredoxin + O2 = (25R)-26-hydroxycholest-4-en-3-one + 2 oxidized [2Fe-2S] ferredoxin + H2O
(1b) (25R)-26-hydroxycholest-4-en-3-one + 2 reduced [2Fe-2S] ferredoxin + O2 = (25R)-26-oxocholest-4-en-3-one + 2 oxidized [2Fe-2S] ferredoxin + 2 H2O
(1c) (25R)-26-oxocholest-4-en-3-one + 2 reduced [2Fe-2S] ferredoxin + O2 = (25R)-3-oxocholest-4-en-26-oate + 2 oxidized [2Fe-2S] ferredoxin + H2O
Other name(s): CYP142
Systematic name: cholest-4-en-3-one,reduced [2Fe-2S] ferredoxin:oxygen oxidoreductase [(25R)-3-oxocholest-4-en-26-oate-forming]
Comments: This cytochrome P-450 (heme-thiolate) enzyme, found in several bacterial pathogens, is involved in degradation of the host cholesterol. It catalyses the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol. The products are exclusively in the (25R) conformation. The enzyme also accepts cholesterol as a substrate. cf. EC 1.14.15.29, cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]. The enzyme can receive electrons from ferredoxin reductase in vitro, its natural electron donor is not known yet.
References:
1.  Driscoll, M.D., McLean, K.J., Levy, C., Mast, N., Pikuleva, I.A., Lafite, P., Rigby, S.E., Leys, D. and Munro, A.W. Structural and biochemical characterization of Mycobacterium tuberculosis CYP142: evidence for multiple cholesterol 27-hydroxylase activities in a human pathogen. J. Biol. Chem. 285 (2010) 38270–38282. [PMID: 20889498]
2.  Johnston, J.B., Ouellet, H. and Ortiz de Montellano, P.R. Functional redundancy of steroid C26-monooxygenase activity in Mycobacterium tuberculosis revealed by biochemical and genetic analyses. J. Biol. Chem. 285 (2010) 36352–36360. [PMID: 20843794]
[EC 1.14.15.28 created 2016 as EC 1.14.13.221, transferred 2018 to EC 1.14.15.28]
 
 
EC 3.1.6.21     Relevance: 11.1%
Accepted name: linear primary-alkylsulfatase
Reaction: a primary alkyl sulfate ester + H2O = an alcohol + sulfate
Other name(s): sdsA1 (gene name); yjcS (gene name); type III linear primary-alkylsulfatase
Systematic name: primary alkyl sulfate ester sulfohydrolase
Comments: Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-β-lactamase fold and binds two zinc ions as cofactors. This enzyme belongs to the type III sulfatase family. It is active against linear primary-alkyl sulfate esters, such as dodecyl sulfate, decyl sulfate, octyl sulfate, and hexyl sulfate. The enzyme from Pseudomonas aeruginosa is secreted out of the cell. The catalytic mechanism begins with activation of a water molecule by the binuclear Zn2+ cluster, resulting in a nucleophilic attack on the carbon atom. cf. EC 3.1.6.22, branched primary-alkylsulfatase, and EC 3.1.6.19, (R)-specific secondary-alkylsulfatase (type III).
References:
1.  Hagelueken, G., Adams, T.M., Wiehlmann, L., Widow, U., Kolmar, H., Tummler, B., Heinz, D.W. and Schubert, W.D. The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, defines a third class of sulfatases. Proc. Natl. Acad. Sci. USA 103 (2006) 7631–7636. [PMID: 16684886]
2.  Long, M., Ruan, L., Li, F., Yu, Z. and Xu, X. Heterologous expression and characterization of a recombinant thermostable alkylsulfatase (sdsAP). Extremophiles 15 (2011) 293–301. [PMID: 21318560]
3.  Liang, Y., Gao, Z., Dong, Y. and Liu, Q. Structural and functional analysis show that the Escherichia coli uncharacterized protein YjcS is likely an alkylsulfatase. Protein Sci. 23 (2014) 1442–1450. [PMID: 25066955]
4.  Sun, L., Chen, P., Su, Y., Cai, Z., Ruan, L., Xu, X. and Wu, Y. Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9. Biosci Rep 37 (2017) . [PMID: 28442601]
[EC 3.1.6.21 created 2021]
 
 
EC 1.14.13.141      
Transferred entry: cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]. Now EC 1.14.15.29, cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]..
[EC 1.14.13.141 created 2012, modified 2016, deleted 2018]
 
 
EC 2.7.8.13     Relevance: 11%
Accepted name: phospho-N-acetylmuramoyl-pentapeptide-transferase
Reaction: UDP-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
Other name(s): MraY transferase; UDP-MurNAc-L-Ala-D-γ-Glu-L-Lys-D-Ala-D-Ala:C55-isoprenoid alcohol transferase; UDP-MurNAc-Ala-γDGlu-Lys-DAla-DAla:undecaprenylphosphate transferase; phospho-N-acetylmuramoyl pentapeptide translocase; phospho-MurNAc-pentapeptide transferase; phospho-NAc-muramoyl-pentapeptide translocase (UMP); phosphoacetylmuramoylpentapeptide translocase; phosphoacetylmuramoylpentapeptidetransferase
Systematic name: UDP-MurAc(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala):undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide-transferase
Comments: In Gram-negative and some Gram-positive organisms the L-lysine is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm), which is combined with adjacent residues through its L-centre. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here).
References:
1.  Heydanek, M.G., Jr. and Neuhaus, F.C. The initial stage in peptidoglycan synthesis. IV. Solubilization of phospho-N-acetylmuramyl-pentapeptide translocase. Biochemistry 8 (1969) 1474–1481. [PMID: 5805290]
2.  Higashi, Y., Strominger, J.L. and Sweeley, C.C. Structure of a lipid intermediate in cell wall peptidoglycan synthesis: a derivative of a C55 isoprenoid alcohol. Proc. Natl. Acad. Sci. USA 57 (1967) 1878–1884. [PMID: 5231417]
3.  Struve, W.G., Sinha, R.K. and Neuhaus, F.C. On the initial stage in peptidoglycan synthesis. Phospho-N-acetylmuramyl-pentapeptide translocase (uridine monophosphate). Biochemistry 5 (1966) 82–93. [PMID: 5938956]
4.  van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503–519. [PMID: 11699883]
[EC 2.7.8.13 created 1972, modified 2002]
 
 
EC 2.8.2.14     Relevance: 10.5%
Accepted name: bile-salt sulfotransferase
Reaction: (1) 3′-phosphoadenylyl sulfate + glycolithocholate = adenosine 3′,5′-bisphosphate + glycolithocholate 3-sulfate
(2) 3′-phosphoadenylyl sulfate + taurolithocholate = adenosine 3′,5′-bisphosphate + taurolithocholate sulfate
Glossary: glycolithocholate 3-sulfate = N-(3α-sulfooxy-5β-cholan-24-oyl)glycine
Other name(s): BAST I; bile acid:3′-phosphoadenosine-5′-phosphosulfate sulfotransferase; bile salt:3′phosphoadenosine-5′-phosphosulfate:sulfotransferase; bile acid sulfotransferase I; glycolithocholate sulfotransferase; 3′-phosphoadenylyl-sulfate:glycolithocholate sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:glycolithocholate sulfonotransferase
Comments: The formation of sulfate esters of bile acids is an essential step in the prevention of toxicity by monohydroxy bile acids in many species [3]. This enzyme is both a bile salt and a 3-hydroxysteroid sulfotransferase. In addition to the 5β-bile acid glycolithocholate, deoxycholate, 3β-hydroxy-5-cholenoate and dehydroepiandrosterone (3β-hydroxyandrost-5-en-17-one) also act as substrates [see also EC 2.8.2.2 (alcohol sulfotransferase) and EC 2.8.2.34 (glycochenodeoxycholate sulfotransferase)]. May be identical to EC 2.8.2.2 [3].
References:
1.  Chen, L.-J., Bolt, R.J. and Admirand, W.H. Enzymatic sulfation of bile salts. Partial purification and characterization of an enzyme from rat liver that catalyzes the sulfation of bile salts. Biochim. Biophys. Acta 480 (1977) 219–227. [PMID: 831833]
2.  Barnes, S., Waldrop, R., Crenshaw, J., King, R.J. and Taylor, K.B. Evidence for an ordered reaction mechanism for bile salt: 3′phosphoadenosine-5′-phosphosulfate: sulfotransferase from rhesus monkey liver that catalyzes the sulfation of the hepatotoxin glycolithocholate. J. Lipid Res. 27 (1986) 1111–1123. [PMID: 3470420]
3.  Barnes, S., Buchina, E.S., King, R.J., McBurnett, T. and Taylor, K.B. Bile acid sulfotransferase I from rat liver sulfates bile acids and 3-hydroxy steroids: purification, N-terminal amino acid sequence, and kinetic properties. J. Lipid Res. 30 (1989) 529–540. [PMID: 2754334]
4.  Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137–174. [PMID: 12543708]
[EC 2.8.2.14 created 1978, modified 2005]
 
 
EC 1.14.14.160     Relevance: 10.4%
Accepted name: zealexin A1 synthase
Reaction: (S)-β-macrocarpene + 3 O2 + 3 [reduced NADPH—hemoprotein reductase] = zealexin A1 + 4 H2O + 3 [oxidized NADPH—hemoprotein reductase] (overall reaction)
(1a) (S)-β-macrocarpene + O2 + [reduced NADPH—hemoprotein reductase] = [(4S)-4-(5,5-dimethylcyclohex-1-en-1-yl)-cyclohex-1-en-1-yl]methanol + H2O + [oxidized NADPH—hemoprotein reductase]
(1b) [(4S)-4-(5,5-dimethylcyclohex-1-en-1-yl)-cyclohex-1-en-1-yl] methanol + O2 + [reduced NADPH—hemoprotein reductase] = (4S)-4-(5,5-dimethylcyclohex-1-en-1-yl)cyclohex-1-ene-1-carbaldehyde + 2 H2O + [oxidized NADPH—hemoprotein reductase]
(1c) (4S)-4-(5,5-dimethylcyclohex-1-en-1-yl)cyclohex-1-ene-1-carbaldehyde + O2 + [reduced NADPH—hemoprotein reductase] = zealexin A1 + H2O + [oxidized NADPH—hemoprotein reductase]
Glossary: (S)-β-macrocarpene = (1′S)-4′,5,5-trimethyl-1,1′-bi(cyclohexane)-1,3′-diene
zealexin A1 = (4S)-4-(5,5-dimethylcyclohex-1-en-1-yl)cyclohex-1-ene-1-carboxylate
Other name(s): CYP71Z18 (gene name)
Systematic name: (S)-β-macrocarpene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (zealexin A1-forming)
Comments: A cytochrome P-450 (heme thiolate) enzyme characterized from maize. The enzyme sequentially oxidizes(S)-β-macrocarpene via alcohol and aldehyde intermediates to form zealexin A1, a maize phytoalexin that provides biochemical protection against fungal infection.
References:
1.  Mao, H., Liu, J., Ren, F., Peters, R.J. and Wang, Q. Characterization of CYP71Z18 indicates a role in maize zealexin biosynthesis. Phytochemistry 121 (2016) 4–10. [PMID: 26471326]
[EC 1.14.14.160 created 2018]
 
 
EC 2.3.1.298     Relevance: 10%
Accepted name: ultra-long-chain ceramide synthase
Reaction: an ultra-long-chain fatty acyl-CoA + a sphingoid base = an ultra-long-chain ceramide + CoA
Glossary: a sphingoid base = an amino alcohol, composed predominantly of 18 carbon atoms, characterized by the presence of a hydroxyl group at C-1 (and often also at C-3), and an amine group at C-2.
an ultra-long-chain fatty acyl-CoA = an acyl-CoA with a chain length of 28 or longer.
Other name(s): mammalian ceramide synthase 3; sphingoid base N-ultra-long-chain fatty acyl-CoA transferase; CERS3 (gene name)
Systematic name: ultra-long-chain fatty acyl-CoA:sphingoid base N-acyltransferase
Comments: Mammals have six ceramide synthases that exhibit relatively strict specificity regarding the chain-length of their acyl-CoA substrates. Ceramide synthase 3 (CERS3) is the only enzyme that is active with ultra-long-chain acyl-CoA donors (C28 or longer). It is active in the epidermis, where its products are incorporated into acylceramides. CERS3 also accepts (2R)-2-hydroxy fatty acids and ω-hydroxy fatty acids, and can accept very-long-chain acyl-CoA substrates (see EC 2.3.1.297, very-long-chain ceramide synthase). It can use multiple sphingoid bases including sphinganine, sphingosine, phytosphingosine, and (6R)-6-hydroxysphingosine.
References:
1.  Mizutani, Y., Kihara, A. and Igarashi, Y. LASS3 (longevity assurance homologue 3) is a mainly testis-specific (dihydro)ceramide synthase with relatively broad substrate specificity. Biochem. J. 398 (2006) 531–538. [PMID: 16753040]
2.  Mizutani, Y., Kihara, A., Chiba, H., Tojo, H. and Igarashi, Y. 2-Hydroxy-ceramide synthesis by ceramide synthase family: enzymatic basis for the preference of FA chain length. J. Lipid Res. 49 (2008) 2356–2364. [PMID: 18541923]
3.  Jennemann, R., Rabionet, M., Gorgas, K., Epstein, S., Dalpke, A., Rothermel, U., Bayerle, A., van der Hoeven, F., Imgrund, S., Kirsch, J., Nickel, W., Willecke, K., Riezman, H., Grone, H.J. and Sandhoff, R. Loss of ceramide synthase 3 causes lethal skin barrier disruption. Hum. Mol. Genet. 21 (2012) 586–608. [PMID: 22038835]
4.  Mizutani, Y., Sun, H., Ohno, Y., Sassa, T., Wakashima, T., Obara, M., Yuyama, K., Kihara, A. and Igarashi, Y. Cooperative synthesis of ultra long-chain fatty acid and ceramide during keratinocyte differentiation. PLoS One 8:e67317 (2013). [PMID: 23826266]
[EC 2.3.1.298 created 2019]
 
 
EC 1.14.13.109      
Transferred entry: abieta-7,13-dien-18-ol hydroxylase. Now EC 1.14.14.145, abieta-7,13-dien-18-ol hydroxylase
[EC 1.14.13.109 created 2009, modified 2012, deleted 2018]
 
 
EC 1.14.15.29     Relevance: 9.7%
Accepted name: cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]
Reaction: cholest-4-en-3-one + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2 = (25S)-3-oxocholest-4-en-26-oate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O (overall reaction)
(1a) cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = (25S)-26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1b) (25S)-26-hydroxycholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = (25S)-26-oxocholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
(1c) (25S)-26-oxocholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = (25S)-3-oxocholest-4-en-26-oate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Other name(s): CYP125; CYP125A1; cholest-4-en-3-one 27-monooxygenase (misleading); cholest-4-en-3-one,NADH:oxygen oxidoreductase (26-hydroxylating); cholest-4-en-3-one 26-monooxygenase (ambiguous)
Systematic name: cholest-4-en-3-one,[reduced ferredoxin]:oxygen oxidoreductase [(25S)-3-oxocholest-4-en-26-oate-forming]
Comments: A cytochrome P-450 (heme-thiolate) protein found in several bacterial pathogens. The enzyme is involved in degradation of the host's cholesterol. It catalyses the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol [4]. The products are exclusively in the (25S) configuration. The enzyme is part of a two-component system that also includes a ferredoxin reductase (most likely KshB, which also interacts with EC 1.14.15.30, 3-ketosteroid 9α-monooxygenase). The enzyme also accepts cholesterol as a substrate. cf. EC 1.14.15.28, cholest-4-en-3-one 27-monooxygenase.
References:
1.  Rosloniec, K.Z., Wilbrink, M.H., Capyk, J.K., Mohn, W.W., Ostendorf, M., van der Geize, R., Dijkhuizen, L. and Eltis, L.D. Cytochrome P450 125 (CYP125) catalyses C26-hydroxylation to initiate sterol side-chain degradation in Rhodococcus jostii RHA1. Mol. Microbiol. 74 (2009) 1031–1043. [PMID: 19843222]
2.  McLean, K.J., Lafite, P., Levy, C., Cheesman, M.R., Mast, N., Pikuleva, I.A., Leys, D. and Munro, A.W. The Structure of Mycobacterium tuberculosis CYP125: molecular basis for cholesterol binding in a P450 needed for host infection. J. Biol. Chem. 284 (2009) 35524–35533. [PMID: 19846552]
3.  Capyk, J.K., Kalscheuer, R., Stewart, G.R., Liu, J., Kwon, H., Zhao, R., Okamoto, S., Jacobs, W.R., Jr., Eltis, L.D. and Mohn, W.W. Mycobacterial cytochrome P450 125 (Cyp125) catalyzes the terminal hydroxylation of C27 steroids. J. Biol. Chem. 284 (2009) 35534–35542. [PMID: 19846551]
4.  Ouellet, H., Guan, S., Johnston, J.B., Chow, E.D., Kells, P.M., Burlingame, A.L., Cox, J.S., Podust, L.M. and de Montellano, P.R. Mycobacterium tuberculosis CYP125A1, a steroid C27 monooxygenase that detoxifies intracellularly generated cholest-4-en-3-one. Mol. Microbiol. 77 (2010) 730–742. [PMID: 20545858]
[EC 1.14.15.29 created 2012 as EC 1.14.13.141, modified 2016, transferred 2018 to EC 1.14.15.29]
 
 
EC 2.3.1.297     Relevance: 9.7%
Accepted name: very-long-chain ceramide synthase
Reaction: a very-long-chain fatty acyl-CoA + a sphingoid base = a very-long-chain ceramide + CoA
Glossary: a sphingoid base = an amino alcohol, composed predominantly of 18 carbon atoms, characterised by the presence of a hydroxyl group at C-1 (and often also at C-3), and an amine group at C-2
Other name(s): sphingoid base N-very-long-chain fatty acyl-CoA transferase; mammalian ceramide synthase 2; CERS3 (gene name); LASS3 (gene name); LAG1 (gene name); LAC1 (gene name); LOH1 (gene name); LOH3 (gene name)
Systematic name: very-long-chain fatty acyl-CoA:sphingoid base N-acyltransferase
Comments: This entry describes ceramide synthase enzymes that are specific for very-long-chain fatty acyl-CoA substrates. The two isoforms from yeast and the plant LOH1 and LOH3 isoforms transfer 24:0 and 26:0 acyl chains preferentially and use phytosphingosine as the preferred sphingoid base. The mammalian CERS2 isoform is specific for acyl donors of 20-26 carbons, which can be saturated or unsaturated. The mammalian CERS3 isoform catalyses this activity, but has a broader substrate range and also catalyses the activity of EC 2.3.1.298, ultra-long-chain ceramide synthase. Both mammalian enzymes can use multiple sphingoid bases, including sphinganine, sphingosine, and phytosphingosine.
References:
1.  Guillas, I., Kirchman, P.A., Chuard, R., Pfefferli, M., Jiang, J.C., Jazwinski, S.M. and Conzelmann, A. C26-CoA-dependent ceramide synthesis of Saccharomyces cerevisiae is operated by Lag1p and Lac1p. EMBO J. 20 (2001) 2655–2665. [PMID: 11387200]
2.  Pan, H., Qin, W.X., Huo, K.K., Wan, D.F., Yu, Y., Xu, Z.G., Hu, Q.D., Gu, K.T., Zhou, X.M., Jiang, H.Q., Zhang, P.P., Huang, Y., Li, Y.Y. and Gu, J.R. Cloning, mapping, and characterization of a human homologue of the yeast longevity assurance gene LAG1. Genomics 77 (2001) 58–64. [PMID: 11543633]
3.  Schorling, S., Vallee, B., Barz, W.P., Riezman, H. and Oesterhelt, D. Lag1p and Lac1p are essential for the Acyl-CoA-dependent ceramide synthase reaction in Saccharomyces cerevisae. Mol. Biol. Cell 12 (2001) 3417–3427. [PMID: 11694577]
4.  Mizutani, Y., Kihara, A. and Igarashi, Y. Mammalian Lass6 and its related family members regulate synthesis of specific ceramides. Biochem. J. 390 (2005) 263–271. [PMID: 15823095]
5.  Laviad, E.L., Albee, L., Pankova-Kholmyansky, I., Epstein, S., Park, H., Merrill, A.H., Jr. and Futerman, A.H. Characterization of ceramide synthase 2: tissue distribution, substrate specificity, and inhibition by sphingosine 1-phosphate. J. Biol. Chem. 283 (2008) 5677–5684. [PMID: 18165233]
6.  Imgrund, S., Hartmann, D., Farwanah, H., Eckhardt, M., Sandhoff, R., Degen, J., Gieselmann, V., Sandhoff, K. and Willecke, K. Adult ceramide synthase 2 (CERS2)-deficient mice exhibit myelin sheath defects, cerebellar degeneration, and hepatocarcinomas. J. Biol. Chem. 284 (2009) 33549–33560. [PMID: 19801672]
[EC 2.3.1.297 created 2019]
 
 
EC 1.14.14.145     Relevance: 9.4%
Accepted name: abieta-7,13-dien-18-ol hydroxylase
Reaction: abieta-7,13-dien-18-ol + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = abieta-7,13-dien-18-oate + 2 [oxidized NADPH—hemoprotein reductase] + 3 H2O (overall reaction)
(1a) abieta-7,13-dien-18-ol + [reduced NADPH—hemoprotein reductase] + O2 = abieta-7,13-dien-18,18-diol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) abieta-7,13-dien-18,18-diol = abieta-7,13-dien-18-al + H2O (spontaneous)
(1c) abieta-7,13-dien-18-al + [reduced NADPH—hemoprotein reductase] + O2 = abieta-7,13-dien-18-oate + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: abieta-7,13-dien-18-ol = ((1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthren-1-yl)methanol
abieta-7,13-dien-18-al = (1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthrene-1-carbaldehyde
Other name(s): CYP720B1; PtAO; abietadienol hydroxylase (ambiguous)
Systematic name: abieta-7,13-dien-18-ol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (18-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses a step in the pathway of abietic acid biosynthesis. The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine) [1], and the gene encoding the enzyme has been identified in Pinus taeda (loblolly pine) [3]. The recombinant enzyme catalyses the oxidation of multiple diterpene alcohol and aldehydes, including levopimaradienol, isopimara-7,15-dienol, isopimara-7,15-dienal, dehydroabietadienol and dehydroabietadienal. It is not able to oxidize abietadiene.
References:
1.  Funk, C. and Croteau, R. Diterpenoid resin acid biosynthesis in conifers: characterization of two cytochrome P450-dependent monooxygenases and an aldehyde dehydrogenase involved in abietic acid biosynthesis. Arch. Biochem. Biophys. 308 (1994) 258–266. [PMID: 8311462]
2.  Funk, C., Lewinsohn, E., Vogel, B.S., Steele, C.L. and Croteau, R. Regulation of oleoresinosis in grand fir (Abies grandis) (coordinate induction of monoterpene and diterpene cyclases and two cytochrome P450-dependent diterpenoid hydroxylases by stem wounding). Plant Physiol. 106 (1994) 999–1005. [PMID: 12232380]
3.  Ro, D.K., Arimura, G., Lau, S.Y., Piers, E. and Bohlmann, J. Loblolly pine abietadienol/abietadienal oxidase PtAO (CYP720B1) is a multifunctional, multisubstrate cytochrome P450 monooxygenase. Proc. Natl. Acad. Sci. USA 102 (2005) 8060–8065. [PMID: 15911762]
[EC 1.14.14.145 created 2009 as EC 1.14.13.109, modified 2012, transferred 2018 to EC 1.14.14.145]