The Enzyme Database

Displaying entries 51-100 of 147.

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EC 1.1.1.184     Relevance: 100%
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+)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 89700-36-7
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. [DOI] [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. [DOI] [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: 99.4%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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: 99.4%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 102484-73-1
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: 95.9%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 97955-12-9
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: 92.9%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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: 83.4%
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).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 75496-55-8
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: 82.7%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [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. [DOI] [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. [DOI] [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). [DOI] [PMID: 22848751]
[EC 3.6.1.53 created 2008]
 
 
EC 2.3.1.152     Relevance: 82.3%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 203009-15-8
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: 82.3%
Accepted name: isopiperitenol dehydrogenase
Reaction: (-)-trans-isopiperitenol + NAD+ = (-)-isopiperitenone + NADH + H+
For diagram of (-)-carvone, perillyl aldehyde and pulegone biosynthesis, click here
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 96595-05-0
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. [DOI] [PMID: 3885858]
[EC 1.1.1.223 created 1989]
 
 
EC 2.8.2.15     Relevance: 80.2%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9032-76-2
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. [DOI] [PMID: 6932974]
[EC 2.8.2.15 created 1984]
 
 
EC 1.17.9.1     Relevance: 79.6%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 66772-07-4
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. [DOI] [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: 78.9%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [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. [DOI] [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: 78.4%
Accepted name: ent-13-epi-manoyl oxide synthase
Reaction: ent-8α-hydroxylabd-13-en-15-yl diphosphate = ent-13-epi-manoyl oxide + diphosphate
For diagram of (–)-kolavenyl diphosphate derived diterpenoids, click here
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).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [PMID: 26077765]
[EC 4.2.3.186 created 2017]
 
 
EC 5.5.1.28     Relevance: 78.2%
Accepted name: (–)-kolavenyl diphosphate synthase
Reaction: geranylgeranyl diphosphate = (–)-kolavenyl diphosphate
For diagram of (–)-kolavenyl diphosphate derived diterpenoids, click here
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).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [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. [DOI] [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: 77.8%
Accepted name: (-)-α-cuprenene synthase
Reaction: (2E,6E)-farnesyl diphosphate = (-)-α-cuprenene + diphosphate
For diagram of biosynthesis of bicyclic sesquiterpenoids derived from bisabolyl cation, click here and for diagram of trichodiene and (–)-α-cuprenene biosynthesis, click here
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [PMID: 20419721]
[EC 4.2.3.95 created 2012]
 
 
EC 4.2.3.6     Relevance: 75.3%
Accepted name: trichodiene synthase
Reaction: (2E,6E)-farnesyl diphosphate = trichodiene + diphosphate
For diagram of biosynthesis of bicyclic sesquiterpenoids derived from bisabolyl cation, click here and for diagram of trichodiene and (–)-α-cuprenene biosynthesis, click here
Other name(s): trichodiene synthetase; sesquiterpene cyclase; trans,trans-farnesyl-diphosphate sesquiterpenoid-lyase
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, trichodiene-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 101915-76-8
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. [DOI] [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. [DOI] [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. [DOI] [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: 74.2%
Accepted name: carvone reductase
Reaction: (1) (+)-dihydrocarvone + acceptor = (–)-carvone + reduced acceptor
(2) (–)-isodihydrocarvone + acceptor = (+)-carvone + reduced acceptor
For diagram of (–)-carvone catabolism, click here
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [PMID: 10832640]
[EC 1.3.99.25 created 2008]
 
 
EC 1.1.1.296     Relevance: 73.7%
Accepted name: dihydrocarveol dehydrogenase
Reaction: menth-8-en-2-ol + NAD+ = menth-8-en-2-one + NADH + H+
For diagram of (–)-carvone catabolism, click here
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [PMID: 10832640]
[EC 1.1.1.296 created 2008]
 
 
EC 1.23.1.3     Relevance: 71.2%
Accepted name: (–)-pinoresinol reductase
Reaction: (–)-lariciresinol + NADP+ = (–)-pinoresinol + NADPH + H+
For diagram of (–)-lariciresinol biosynthesis, click here
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].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [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. [DOI] [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. [DOI] [PMID: 18347017]
[EC 1.23.1.3 created 2013]
 
 
EC 1.1.1.284     Relevance: 70.7%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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: 70.6%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [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. [DOI] [PMID: 13679086]
[EC 1.3.1.82 created 2008]
 
 
EC 2.3.1.232     Relevance: 69.9%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [PMID: 16262710]
[EC 2.3.1.232 created 2014]
 
 
EC 2.7.8.34     Relevance: 69.8%
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
For diagram of bis(1L-myo-inositol) 1,3′-phosphate biosynthesis, click here
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [PMID: 17526717]
[EC 2.7.8.34 created 2011]
 
 
EC 3.1.1.83     Relevance: 69.6%
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
For diagram of (–)-carvone catabolism, click here and for diagram of menthol biosynthesis, click here
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [PMID: 11157238]
[EC 3.1.1.83 created 2008]
 
 
EC 1.14.14.114     Relevance: 68.2%
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
For diagram of artemisinin biosynthesis, click here
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [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: 66.9%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [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. [DOI] [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. [DOI] [PMID: 24802551]
[EC 1.1.3.47 created 2014]
 
 
EC 1.14.14.143     Relevance: 66.4%
Accepted name: (+)-menthofuran synthase
Reaction: (+)-pulegone + [reduced NADPH—hemoprotein reductase] + O2 = (+)-menthofuran + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of (–)-carvone, perillyl aldehyde and pulegone biosynthesis, click here and for mechanism of reaction, click here
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].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [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. [DOI] [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: 65.4%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 93792-13-3
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 9790672]
10.  Pollegioni, L., Tonin, F. and Rosini, E. Lignin-degrading enzymes. FEBS J. 282 (2015) 1190–1213. [DOI] [PMID: 25649492]
[EC 1.11.1.14 created 1992, modified 2006, modified 2011, modified 2016]
 
 
EC 1.14.14.161     Relevance: 64.6%
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
For diagram of gibberellin A12 biosynthesis, click here
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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: 63.2%
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).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI]
[EC 3.1.6.19 created 2013, modified 2021]
 
 
EC 3.2.1.139     Relevance: 61.4%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37259-81-7
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: 59.3%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 95990-29-7
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. [DOI] [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. [DOI] [PMID: 3624201]
[EC 3.8.1.5 created 1989]
 
 
EC 1.14.13.105     Relevance: 59%
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)
For diagram of (–)-carvone catabolism, click here, for diagram of limonene catabolism, click here and for diagram of menthol biosynthesis, click here
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].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [PMID: 10832640]
[EC 1.14.13.105 created 2008]
 
 
EC 3.2.1.51     Relevance: 58.9%
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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9037-65-4
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. [DOI] [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. [DOI] [PMID: 5672520]
[EC 3.2.1.51 created 1972]
 
 
EC 3.1.1.50     Relevance: 58.2%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 66625-78-3
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: 57.6%
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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-45-0
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: 57.5%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 86280-59-3
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: 55.9%
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).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [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. [DOI] [PMID: 12142403]
[EC 1.1.5.11 created 2016]
 
 
EC 1.1.2.9     Relevance: 55.4%
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).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [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. [DOI] [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. [DOI] [PMID: 12142403]
[EC 1.1.2.9 created 2016]
 
 
EC 3.1.1.70     Relevance: 55.4%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 125858-78-8
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: 55.4%
Accepted name: acetylesterase
Reaction: an acetic ester + H2O = an alcohol + acetate
For diagram of peraksine biosynthesis, click here
Other name(s): C-esterase (in animal tissues); acetic ester hydrolase; chloroesterase; p-nitrophenyl acetate esterase; Citrus acetylesterase
Systematic name: acetic-ester acetylhydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 9000-82-2
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: 55.2%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83869-30-1
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. [DOI] [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. [DOI] [PMID: 27355]
[EC 3.2.1.126 created 1989]
 
 
EC 4.2.3.157     Relevance: 55.2%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [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. [DOI] [PMID: 28247907]
[EC 4.2.3.157 created 2017]
 
 
EC 1.1.1.16     Relevance: 55%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-23-3
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. [DOI] [PMID: 26472925]
[EC 1.1.1.16 created 1961]
 
 
EC 4.1.99.11     Relevance: 54.5%
Accepted name: benzylsuccinate synthase
Reaction: benzylsuccinate = toluene + fumarate
For diagram of anaerobic toluene catabolism, click here
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 209264-18-6
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. [DOI] [PMID: 9632263]
[EC 4.1.99.11 created 2000]
 
 
EC 3.2.1.112     Relevance: 54%
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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 92480-05-2
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. [DOI] [PMID: 6468386]
[EC 3.2.1.112 created 1986]
 
 
EC 1.3.1.92     Relevance: 53.2%
Accepted name: artemisinic aldehyde Δ11(13)-reductase
Reaction: (11R)-dihydroartemisinic aldehyde + NADP+ = artemisinic aldehyde + NADPH + H+
For diagram of artemisinin biosynthesis, click here
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. [DOI] [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. [DOI] [PMID: 18495659]
[EC 1.3.1.92 created 2012]
 
 
EC 1.1.1.33     Relevance: 53.1%
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+)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-34-6
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]
 
 


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