The Enzyme Database

Displaying entries 51-100 of 142.

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EC 4.2.3.105     Relevance: 100%
Accepted name: tricyclene synthase
Reaction: geranyl diphosphate = tricyclene + diphosphate
For diagram of bornane and related monoterpenoids, click here
Other name(s): TPS3
Systematic name: geranyl-diphosphate diphosphate-lyase (cyclizing; tricyclene-forming)
Comments: The enzyme from Solanum lycopersicum (tomato) gives a mixture of tricyclene, camphene, β-myrcene, limonene, and traces of several other monoterpenoids. See EC 4.2.3.117. (-)-camphene synthase, EC 4.2.3.15, myrcene synthase and EC 4.2.3.16, (4S)-limonene synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Falara, V., Akhtar, T.A., Nguyen, T.T., Spyropoulou, E.A., Bleeker, P.M., Schauvinhold, I., Matsuba, Y., Bonini, M.E., Schilmiller, A.L., Last, R.L., Schuurink, R.C. and Pichersky, E. The tomato terpene synthase gene family. Plant Physiol. 157 (2011) 770–789. [DOI] [PMID: 21813655]
[EC 4.2.3.105 created 2012]
 
 
EC 1.14.11.81     Relevance: 99.8%
Accepted name: (–)-cyclopenine synthase
Reaction: (1) cyclopeptine + 2-oxoglutarate + O2 = dehydrocyclopeptine + succinate + CO2 + H2O
(2) dehydrocyclopeptine + 2-oxoglutarate + O2 = (–)-cyclopenine + succinate + CO2
For diagram of cyclopeptine, cyclopenine and viridicatin biosynthesis, click here
Glossary: cyclopeptine = (3S)-3-benzyl-4-methyl-3,4-dihydro-1H-1,4-benzodiazepine-2,5-dione
(–)-cyclopenine = (3S,3′R)-4-methyl-3′-phenyl-1H-spiro[1,4-benzodiazepine-3,2′-oxirane]-2,5-dione
Other name(s): asqJ (gene name)
Systematic name: cyclopeptine,2-oxoglutarate:oxygen oxidoreductase ((–)-cyclopenine-forming)
Comments: This fungal enzyme is involved in the biosynthesis of quinolone compounds. it catalyses two oxidation reactions: the first reaction results in a desaturation; the second reaction is a monooxygenation of the double bond, forming an epoxide. The enzyme is also active with 4′-methoxycyclopeptine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nover, L. and Luckner, M. Mixed functional oxygenations during the biosynthesis of cyclopenin and cyclopenol, benzodiazepine alkaloids of Penicillium cyclopium westling. Incorporation of molecular oxygen and NIH-shift. FEBS Lett. 3 (1969) 292–296. [DOI] [PMID: 11947032]
2.  Ishikawa, N., Tanaka, H., Koyama, F., Noguchi, H., Wang, C.C., Hotta, K. and Watanabe, K. Non-heme dioxygenase catalyzes atypical oxidations of 6,7-bicyclic systems to form the 6,6-quinolone core of viridicatin-type fungal alkaloids. Angew. Chem. Int. Ed. Engl. 53 (2014) 12880–12884. [DOI] [PMID: 25251934]
3.  Brauer, A., Beck, P., Hintermann, L. and Groll, M. Structure of the dioxygenase AsqJ: Mechanistic insights into a one-pot multistep quinolone antibiotic biosynthesis. Angew. Chem. Int. Ed. Engl. 55 (2016) 422–426. [DOI] [PMID: 26553478]
4.  Chang, W.C., Li, J., Lee, J.L., Cronican, A.A. and Guo, Y. Mechanistic investigation of a non-heme iron enzyme catalyzed epoxidation in (–)-4′-methoxycyclopenin biosynthesis. J. Am. Chem. Soc. 138 (2016) 10390–10393. [DOI] [PMID: 27442345]
5.  Song, X., Lu, J. and Lai, W. Mechanistic insights into dioxygen activation, oxygen atom exchange and substrate epoxidation by AsqJ dioxygenase from quantum mechanical/molecular mechanical calculations. Phys Chem Chem Phys 19 (2017) 20188–20197. [DOI] [PMID: 28726913]
6.  Liao, H.J., Li, J., Huang, J.L., Davidson, M., Kurnikov, I., Lin, T.S., Lee, J.L., Kurnikova, M., Guo, Y., Chan, N.L. and Chang, W.C. Insights into the desaturation of cyclopeptin and its C3 epimer catalyzed by a non-heme iron enzyme: structural characterization and mechanism elucidation. Angew. Chem. Int. Ed. Engl. 57 (2018) 1831–1835. [DOI] [PMID: 29314482]
7.  Mader, S.L., Brauer, A., Groll, M. and Kaila, V.RI. Catalytic mechanism and molecular engineering of quinolone biosynthesis in dioxygenase AsqJ. Nat. Commun. 9:1168 (2018). [DOI] [PMID: 29563492]
8.  Wojdyla, Z. and Borowski, T. On how the binding cavity of AsqJ dioxygenase controls the desaturation reaction regioselectivity: a QM/MM study. J. Biol. Inorg. Chem. 23 (2018) 795–808. [DOI] [PMID: 29876666]
9.  Li, J., Liao, H.J., Tang, Y., Huang, J.L., Cha, L., Lin, T.S., Lee, J.L., Kurnikov, I.V., Kurnikova, M.G., Chang, W.C., Chan, N.L. and Guo, Y. Epoxidation catalyzed by the nonheme iron(II)- and 2-oxoglutarate-dependent oxygenase, AsqJ: mechanistic elucidation of oxygen atom transfer by a ferryl intermediate. J. Am. Chem. Soc. 142 (2020) 6268–6284. [DOI] [PMID: 32131594]
10.  Tang, H., Tang, Y., Kurnikov, I.V., Liao, H.J., Chan, N.L., Kurnikova, M.G., Guo, Y. and Chang, W.C. Harnessing the substrate promiscuity of dioxygenase AsqJ and developing efficient chemoenzymatic synthesis for quinolones. ACS Catal. 11 (2021) 7186–7192. [DOI] [PMID: 35721870]
[EC 1.14.11.81 created 2022]
 
 
EC 2.5.1.106     Relevance: 99.4%
Accepted name: tryprostatin B synthase
Reaction: prenyl diphosphate + brevianamide F = diphosphate + tryprostatin B
For diagram of fumitremorgin alkaloid biosynthesis (part 1), click here
Glossary: brevianamide F = (3S,8aS)-3-(1H-indol-3-ylmethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
tryprostatin B = (3S,8aS)-3-{[2-(3-methylbut-2-en-1-yl)-1H-indol-3-yl]methyl}hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
Other name(s): ftmPT1 (gene name); brevianamide F prenyltransferase (ambiguous); dimethylallyl-diphosphate:brevianamide-F dimethylallyl-C-2-transferase
Systematic name: prenyl-diphosphate:brevianamide-F prenyl-C-2-transferase
Comments: The enzyme from the fungus Aspergillus fumigatus can also prenylate other tryptophan-containing cyclic dipeptides. Prenylation occurs mainly at C-2 [1], but also at C-3 [2]. Involved in the biosynthetic pathways of several indole alkaloids such as tryprostatins, cyclotryprostatins, spirotryprostatins, fumitremorgins and verruculogen.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Grundmann, A. and Li, S.M. Overproduction, purification and characterization of FtmPT1, a brevianamide F prenyltransferase from Aspergillus fumigatus. Microbiology 151 (2005) 2199–2207. [DOI] [PMID: 16000710]
2.  Wollinsky, B., Ludwig, L., Xie, X. and Li, S.M. Breaking the regioselectivity of indole prenyltransferases: identification of regular C3-prenylated hexahydropyrrolo[2,3-b]indoles as side products of the regular C2-prenyltransferase FtmPT1. Org. Biomol. Chem. 10 (2012) 9262–9270. [DOI] [PMID: 23090579]
[EC 2.5.1.106 created 2013]
 
 
EC 1.14.19.71     Relevance: 97.9%
Accepted name: fumitremorgin C synthase
Reaction: tryprostatin A + [reduced NADPH—hemoprotein reductase] + O2 = fumitremorgin C + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of fumitremorgin alkaloid biosynthesis (part 1), click here
Glossary: tryprostatin A = (3S,8aS)-3-{[6-methoxy-2-(3-methylbut-2-en-1-yl)-1H-indol-3-yl]methyl}hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
fumitremorgin C = (5aS,12S,14aS)-9-methoxy-12-(2-methylprop-1-en-1-yl)-1,2,3,5a,6,11,12,14a-octahydro-5H,14H-pyrrolo[1′′,2′′:4′,5′]pyrazino[1′,2′:1,6]pyrido[3,4-b]indole-5,14-dione
Other name(s): ftmE (gene name)
Systematic name: tryprostatin A,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein. The protein from the fungus Aspergillus fumigatus also has activity with tryprostatin B forming demethoxyfumitremorgin C. Involved in the biosynthetic pathways of several indole alkaloids such as fumitremorgins and verruculogen.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kato, N., Suzuki, H., Takagi, H., Asami, Y., Kakeya, H., Uramoto, M., Usui, T., Takahashi, S., Sugimoto, Y. and Osada, H. Identification of cytochrome P450s required for fumitremorgin biosynthesis in Aspergillus fumigatus. ChemBioChem 10 (2009) 920–928. [DOI] [PMID: 19226505]
[EC 1.14.19.71 created 2013 as EC 1.14.21.10, transferred 2018 to EC 1.14.19.71]
 
 
EC 3.1.1.94     Relevance: 97.7%
Accepted name: versiconal hemiacetal acetate esterase
Reaction: (1) versiconal hemiacetal acetate + H2O = versiconal + acetate
(2) versiconol acetate + H2O = versiconol + acetate
For diagram of aflatoxin biosynthesis (part 2), click here
Glossary: versiconal = (2S,3S)-2,4,6,8-tetrahydroxy-3-(2-hydroxyethyl)anthra[2,3-b]furan-5,10-dione
versiconal hemiacetal acetate = 2-[(2S,3S)-2,4,6,8-tetrahydroxy-5,10-dioxo-5,10-dihydroanthra[2,3-b]furan-3-yl]ethyl acetate
versiconol = 1,3,6,8-tetrahydroxy-3-[(2S)-1,4-dihydroxybutan-2-yl]anthracene-5,10-dione
versiconol acetate = (3S)-4-hydroxy-3-[1,3,6,8-tetrahydroxy-9,10-dioxo-9,10-dihydroanthracen-2-yl]butyl acetate
Other name(s): VHA esterase
Systematic name: versiconal-hemiacetal-acetate O-acetylhydrolase
Comments: Isolated from the mold Aspergillus parasiticus. Involved in a metabolic grid that leads to aflatoxin biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kusumoto, K. and Hsieh, D.P. Purification and characterization of the esterases involved in aflatoxin biosynthesis in Aspergillus parasiticus. Can. J. Microbiol. 42 (1996) 804–810. [PMID: 8776851]
2.  Chang, P.K., Yabe, K. and Yu, J. The Aspergillus parasiticus estA-encoded esterase converts versiconal hemiacetal acetate to versiconal and versiconol acetate to versiconol in aflatoxin biosynthesis. Appl. Environ. Microbiol. 70 (2004) 3593–3599. [DOI] [PMID: 15184162]
[EC 3.1.1.94 created 2013]
 
 
EC 1.14.11.38     Relevance: 97.5%
Accepted name: verruculogen synthase
Reaction: fumitremorgin B + 2-oxoglutarate + 2 O2 + reduced acceptor = verruculogen + succinate + CO2 + H2O + acceptor
For diagram of fumitremorgin alkaloid biosynthesis (part 2), click here
Glossary: fumitremorgin B = (5aR,6S,12S,14aS)-5a,6-dihydroxy-9-methoxy-11-(3-methylbut-2-en-1-yl)-12-(2-methylprop-1-en-1-yl)-1,2,3,5a,6,11,12,14a-octahydro-5H,14H-pyrrolo[1′′,2′′:4′,5′]pyrazino[1′,2′:1,6]pyrido[3,4-b]indole-5,14-dione
verruculogen = (5R,10S,10aR,14aS,15bS)-10,10a-dihydroxy-6-methoxy-2,2-dimethyl-5-(2-methylprop-1-en-1-yl)-1,10,10a,14,14a,15b-hexahydro-12H-3,4-dioxa-5a,11a,15a-triazacycloocta[1,2,3-lm]indeno[5,6-b]fluorene-11,15(2H,13H)-dione
Other name(s): fmtF (gene name); FmtOx1
Systematic name: fumitremorgin B,2-oxoglutarate:oxygen oxidoreductase (verruculogen-forming)
Comments: Requires Fe2+ and ascorbate. Found in the fungus Aspergillus fumigatus. Both atoms of a dioxygen molecule are incorporated into verruculogen [1,2]. Involved in the biosynthetic pathways of several indole alkaloids such as fumitremorgin A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Steffan, N., Grundmann, A., Afiyatullov, S., Ruan, H. and Li, S.M. FtmOx1, a non-heme Fe(II) and α-ketoglutarate-dependent dioxygenase, catalyses the endoperoxide formation of verruculogen in Aspergillus fumigatus. Org. Biomol. Chem. 7 (2009) 4082–4087. [DOI] [PMID: 19763315]
2.  Kato, N., Suzuki, H., Takagi, H., Uramoto, M., Takahashi, S. and Osada, H. Gene disruption and biochemical characterization of verruculogen synthase of Aspergillus fumigatus. ChemBioChem 12 (2011) 711–714. [DOI] [PMID: 21404415]
[EC 1.14.11.38 created 2013]
 
 
EC 2.5.1.109     Relevance: 97.2%
Accepted name: brevianamide F prenyltransferase (deoxybrevianamide E-forming)
Reaction: prenyl diphosphate + brevianamide F = diphosphate + deoxybrevianamide E
For diagram of fumitremorgin alkaloid biosynthesis (part 1), click here
Glossary: brevianamide F = (3S,8aS)-3-(1H-indol-3-ylmethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
deoxybrevianamide E = (3S,8aS)-3-{[2-(2-methylbut-3-en-2-yl)-1H-indol-3-yl]methyl}-octahydropyrrolo[1,2-a]piperazine-1,4-dione
Other name(s): NotF; BrePT; brevianamide F reverse prenyltransferase; dimethylallyl-diphosphate:brevianamide-F tert-dimethylallyl-C-2-transferase
Systematic name: prenyl-diphosphate:brevianamide-F 2-methylbut-3-en-2-yl-C-2-transferase
Comments: The enzyme from the fungus Aspergilus sp. MF297-2 is specific for brevianamide F [1], while the enzyme from Aspergillus versicolor accepts a broad range of trytophan-containing cyclic dipeptides [2]. Involved in the biosynthetic pathways of several indole alkaloids such as paraherquamides and malbrancheamides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Ding, Y., de Wet, J.R., Cavalcoli, J., Li, S., Greshock, T.J., Miller, K.A., Finefield, J.M., Sunderhaus, J.D., McAfoos, T.J., Tsukamoto, S., Williams, R.M. and Sherman, D.H. Genome-based characterization of two prenylation steps in the assembly of the stephacidin and notoamide anticancer agents in a marine-derived Aspergillus sp. J. Am. Chem. Soc. 132 (2010) 12733–12740. [DOI] [PMID: 20722388]
2.  Yin, S., Yu, X., Wang, Q., Liu, X.Q. and Li, S.M. Identification of a brevianamide F reverse prenyltransferase BrePT from Aspergillus versicolor with a broad substrate specificity towards tryptophan-containing cyclic dipeptides. Appl. Microbiol. Biotechnol. 97 (2013) 1649–1660. [DOI] [PMID: 22660767]
[EC 2.5.1.109 created 2013]
 
 
EC 4.2.3.6     Relevance: 97.1%
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 1.14.13.104      
Transferred entry: (+)-menthofuran synthase. Now EC 1.14.14.143, (+)-menthofuran synthase
[EC 1.14.13.104 created 2008, deleted 2018]
 
 
EC 1.3.99.25     Relevance: 96%
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 6.3.2.40     Relevance: 96%
Accepted name: cyclopeptine synthase
Reaction: 2 ATP + S-adenosyl-L-methionine + anthranilate + L-phenylalanine = cyclopeptine + 2 AMP + 2 diphosphate + S-adenosyl-L-homocysteine
For diagram of cyclopeptine, cyclopenine and viridicatin biosynthesis, click here
Glossary: cyclopeptine = (3S)-3-benzyl-4-methyl-3,4-dihydro-1H-1,4-benzodiazepine-2,5-dione
4′-methoxycyclopeptine = (3S)-3-(4-methoxybenzyl)-4-methyl-3,4-dihydro-1H-1,4-benzodiazepine-2,5-dione
Systematic name: S-adenosyl-L-methionine:anthranilate:L-phenylalanine ligase (cyclopeptine-forming)
Comments: Cyclopeptine synthase is the key enzyme of benzodiazepine alkaloid biosynthesis in several fungi species. The enzyme is a non-ribosomal peptide synthase. It is also active with O-methyl-L-tyrosine forming 4′-methoxycyclopeptine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lerbs, W. and Luckner, M. Cyclopeptine synthetase activity in surface cultures of Penicillium cyclopium. J. Basic Microbiol. 25 (1985) 387–391. [DOI] [PMID: 2995633]
2.  Gerlach, M, Schwelle, N., Lerbs, W. and Luckner, M. Enzymatic synthesis of cyclopeptine intermediates in Penicillium cyclopium. Phytochemistry 24 (1985) 1935–1939.
3.  Ishikawa, N., Tanaka, H., Koyama, F., Noguchi, H., Wang, C.C., Hotta, K. and Watanabe, K. Non-heme dioxygenase catalyzes atypical oxidations of 6,7-bicyclic systems to form the 6,6-quinolone core of viridicatin-type fungal alkaloids. Angew. Chem. Int. Ed. Engl. 53 (2014) 12880–12884. [DOI] [PMID: 25251934]
[EC 6.3.2.40 created 2013]
 
 
EC 4.1.2.30      
Transferred entry: 17α-hydroxyprogesterone aldolase. Now EC 1.14.14.32, 17α-hydroxyprogesterone deacetylase
[EC 4.1.2.30 created 1976, deleted 2016]
 
 
EC 1.14.13.177      
Transferred entry: fumitremorgin C monooxygenase. Now EC 1.14.14.119, fumitremorgin C monooxygenase
[EC 1.14.13.177 created 2013, deleted 2018]
 
 
EC 1.14.13.175      
Transferred entry: aflatoxin B synthase. Now EC 1.14.14.117, aflatoxin B synthase
[EC 1.14.13.175 created 2013, deleted 2018]
 
 
EC 1.1.1.296     Relevance: 95.2%
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 1.14.99.58     Relevance: 93.5%
Accepted name: heme oxygenase (biliverdin-IX-β and δ-forming)
Reaction: (1) protoheme + 3 reduced acceptor + 3 O2 = biliverdin-IX-δ + CO + Fe2+ + 3 acceptor + 3 H2O
(2) protoheme + 3 reduced acceptor + 3 O2 = biliverdin-IX-β + CO + Fe2+ + 3 acceptor + 3 H2O
For diagram of biliverdin biosynthesis, click here
Glossary: biliverdin-IX-β = 3,7-bis(2-carboxyethyl)-2,8,12,17-tetramethyl-13,18-divinylbilin-1,19(21H,24H)-dione
biliverdin-IX-δ = 3,7-bis(2-carboxyethyl)-2,8,13,18-tetramethyl-12,17-divinylbilin-1,19(21H,24H)-dione
Other name(s): pigA (gene name)
Systematic name: protoheme,donor:oxygen oxidoreductase (biliverdin-IX-β and δ-forming)
Comments: The enzyme, characterized from the bacterium Pseudomonas aeruginosa, differs from EC 1.14.15.20, heme oxygenase (biliverdin-producing, ferredoxin), in that the heme substrate is rotated by approximately 110 degrees within the active site, resulting in cleavage at a different part of the ring. It forms a mixture of about 70% biliverdin-IX-δ and 30% biliverdin-IX-β.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ratliff, M., Zhu, W., Deshmukh, R., Wilks, A. and Stojiljkovic, I. Homologues of neisserial heme oxygenase in gram-negative bacteria: degradation of heme by the product of the pigA gene of Pseudomonas aeruginosa. J. Bacteriol. 183 (2001) 6394–6403. [DOI] [PMID: 11591684]
2.  Caignan, G.A., Deshmukh, R., Wilks, A., Zeng, Y., Huang, H.W., Moenne-Loccoz, P., Bunce, R.A., Eastman, M.A. and Rivera, M. Oxidation of heme to β- and δ-biliverdin by Pseudomonas aeruginosa heme oxygenase as a consequence of an unusual seating of the heme. J. Am. Chem. Soc. 124 (2002) 14879–14892. [DOI] [PMID: 12475329]
3.  Friedman, J., Lad, L., Li, H., Wilks, A. and Poulos, T.L. Structural basis for novel δ-regioselective heme oxygenation in the opportunistic pathogen Pseudomonas aeruginosa. Biochemistry 43 (2004) 5239–5245. [DOI] [PMID: 15122889]
[EC 1.14.99.58 created 2017]
 
 
EC 1.23.1.3     Relevance: 92.1%
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, PDB
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 1.1.1.328     Relevance: 91.4%
Accepted name: nicotine blue oxidoreductase
Reaction: 3,3′-bipyridine-2,2′,5,5′,6,6′-hexol + NAD(P)+ = (E)-2,2′,5,5′-tetrahydroxy-6H,6′H-[3,3′-bipyridinylidene]-6,6′-dione + NAD(P)H + H+
For diagram of nicotine catabolism by arthrobacter, click here
Glossary: 3,3′-bipyridine-2,2′,5,5′,6,6′-hexol = nicotine blue leuco form
(E)-2,2′,5,5′-tetrahydroxy-6H,6′H-[3,3′-bipyridinylidene]-6,6′-dione = nicotine blue
Other name(s): nboR (gene name)
Systematic name: 3,3′-bipyridine-2,2′,5,5′,6,6′-hexol:NADP+ 11-oxidoreductase
Comments: The enzyme, characterized from the nicotine degrading bacterium Arthrobacter nicotinovorans, catalyses the reduction of "nicotine blue" to its hydroquinone form (the opposite direction from that shown). Nicotine blue is the name given to the compound formed by the autocatalytic condensation of two molecules of 2,3,6-trihydroxypyridine, an intermediate in the nicotine degradation pathway. The main role of the enzyme may be to prevent the intracellular formation of nicotine blue semiquinone radicals, which by redox cycling would lead to the formation of toxic reactive oxygen species. The enzyme possesses a slight preference for NADH over NADPH.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Mihasan, M., Chiribau, C.B., Friedrich, T., Artenie, V. and Brandsch, R. An NAD(P)H-nicotine blue oxidoreductase is part of the nicotine regulon and may protect Arthrobacter nicotinovorans from oxidative stress during nicotine catabolism. Appl. Environ. Microbiol. 73 (2007) 2479–2485. [DOI] [PMID: 17293530]
[EC 1.1.1.328 created 2012]
 
 
EC 1.14.13.54     Relevance: 90.9%
Accepted name: ketosteroid monooxygenase
Reaction: a ketosteroid + NADPH + H+ + O2 = a steroid ester/lactone + NADP+ + H2O (general reaction)
(1) progesterone + NADPH + H+ + O2 = testosterone acetate + NADP+ + H2O
(2) androstenedione + NADPH + H+ + O2 = testololactone + NADP+ + H2O
(3) 17α-hydroxyprogesterone + NADPH + H+ + O2 = androstenedione + acetate + NADP+ + H2O
Glossary: progesterone = pregn-4-ene-3,20-dione
testosterone acetate = 3-oxoandrost-4-en-17β-yl acetate
androstenedione = androst-4-ene-3,17-dione
testololactone = 3-oxo-13,17-secoandrost-4-eno-17,13α-lactone
17α-hydroxyprogesterone = 17α-hydroxypregn-4-ene-3,20-dione
Other name(s): steroid-ketone monooxygenase; progesterone, NADPH2:oxygen oxidoreductase (20-hydroxylating, ester-producing); 17α-hydroxyprogesterone, NADPH2:oxygen oxidoreductase (20-hydroxylating, side-chain cleaving); androstenedione, NADPH2:oxygen oxidoreductase (17-hydroxylating, lactonizing)
Systematic name: ketosteroid,NADPH:oxygen oxidoreductase (20-hydroxylating, ester-producing/20-hydroxylating, side-chain cleaving/17-hydroxylating, lactonizing)
Comments: A single FAD-containing enzyme catalyses three types of monooxygenase (Baeyer-Villiger oxidation) reaction. The oxidative esterification of a number of derivatives of progesterone to produce the corresponding 17α-hydroxysteroid 17-acetate ester, such as testosterone acetate, is shown in Reaction (1). The oxidative lactonization of a number of derivatives of androstenedione to produce the 13,17-secoandrosteno-17,13α-lactone, such as testololactone, is shown in Reaction (2). The oxidative cleavage of the 17β-side-chain of 17α-hydroxyprogesterone to produce androstenedione and acetate is shown in Reaction (3). Reaction (1) is also catalysed by EC 1.14.99.4 (progesterone monooxygenase), and Reactions (2) and (3) correspond to that catalysed by EC 1.14.99.12 (androst-4-ene-3,17-dione monooxygenase). The possibility that a single enzyme is responsible for the reactions ascribed to EC 1.14.99.4 and EC 1.14.99.12 in other tissues cannot be excluded.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9044-53-5
References:
1.  Katagiri, M. and Itagaki, E. A steroid ketone monooxygenase from Cylindrocarpon radicicola. In: Müller, F. (Ed.), Chemistry and Biochemistry of Flavoenzymes, CRC Press, Florida, 1991, pp. 102–108.
2.  Itagaki, E. Studies on a steroid monooxygenase from Cylindrocarpon radicicola ATCC 11011. Purification and characterization. J. Biochem. (Tokyo) 99 (1986) 815–824. [PMID: 3486863]
3.  Itagaki, E. Studies on a steroid monooxygenase from Cylindrocarpon radicicola ATCC11011. Oxygenative lactonization of androstenedione to testololactone. J. Biochem. (Tokyo) 99 (1986) 825–832. [PMID: 3486864]
[EC 1.14.13.54 created 1999]
 
 
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 1.14.14.117     Relevance: 90.3%
Accepted name: aflatoxin B synthase
Reaction: (1) 8-O-methylsterigmatocystin + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = aflatoxin B1 + 2 [oxidized NADPH—hemoprotein reductase] + H2O + methanol + CO2
(2) 8-O-methyldihydrosterigmatocystin + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = aflatoxin B2 + 2 [oxidized NADPH—hemoprotein reductase] + H2O + methanol + CO2
For diagram of aflatoxin biosynthesis (part 4), click here
Glossary: aflatoxin B1 = (6aR,9aS)-4-methoxy-2,3,6a,9a-tetrahydrocyclopenta[c]furo[3′,2′:4,5]furo[2,3-h][1]benzopyran-1,11-dione
aflatoxin B2 = (6aR,9aS)-4-methoxy-2,3,6a,8,9,9a-hexahydrocyclopenta[c]furo[3′,2′:4,5]furo[2,3-h][1]benzopyran-1,11-dione
8-O-methylsterigmatocystin = 6,8-dimethoxy-3a,12c-dihydrofuro[3′,2′:4,5]furo[2,3-c]xanthen-7-one
8-O-methyldihydrosterigmatocystin = 6,8-dimethoxy-1,2,3a,12c-tetrahydrofuro[3′,2′:4,5]furo[2,3-c]xanthen-7-one
Other name(s): ordA (gene name)
Systematic name: 8-O-methylsterigmatocystin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (aflatoxin-B-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. Isolated from the mold Aspergillus parasiticus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bhatnagar, D., Cleveland, T.E. and Kingston, D.G. Enzymological evidence for separate pathways for aflatoxin B1 and B2 biosynthesis. Biochemistry 30 (1991) 4343–4350. [PMID: 1902378]
2.  Yu, J., Chang, P.K., Ehrlich, K.C., Cary, J.W., Montalbano, B., Dyer, J.M., Bhatnagar, D. and Cleveland, T.E. Characterization of the critical amino acids of an Aspergillus parasiticus cytochrome P-450 monooxygenase encoded by ordA that is involved in the biosynthesis of aflatoxins B1, G1, B2, and G2. Appl. Environ. Microbiol. 64 (1998) 4834–4841. [PMID: 9835571]
3.  Udwary, D.W., Casillas, L. K. and Townsend, C.A. Synthesis of 11-hydroxyl O-methylsterigmatocystin and the role of a cytochrome P-450 in the final step of aflatoxin biosynthesis. J. Am. Chem. Soc. 124 (2002) 5294–5303. [DOI] [PMID: 11996570]
[EC 1.14.14.117 created 2013 as EC 1.14.13.175, transferred 2018 to EC 1.14.14.117]
 
 
EC 3.1.1.83     Relevance: 90.1%
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 2.3.1.230     Relevance: 89.8%
Accepted name: 2-heptyl-4(1H)-quinolone synthase
Reaction: octanoyl-CoA + (2-aminobenzoyl)acetate = 2-heptyl-4-quinolone + CoA + CO2 + H2O (overall reaction)
(1a) octanoyl-CoA + L-cysteinyl-[PqsC protein] = S-octanoyl-L-cysteinyl-[PqsC protein] + CoA
(1b) S-octanoyl-L-cysteinyl-[PqsC protein] + (2-aminobenzoyl)acetate = 1-(2-aminophenyl)decane-1,3-dione + CO2 + L-cysteinyl-[PqsC protein]
(1c) 1-(2-aminophenyl)decane-1,3-dione = 2-heptyl-4-quinolone + H2O
Glossary: 2-heptyl-4-quinolone = 2-heptylquinolin-4(1H)-one
Other name(s): pqsBC (gene names); malonyl-CoA:anthraniloyl-CoA C-acetyltransferase (decarboxylating)
Systematic name: octanoyl-CoA:(2-aminobenzoyl)acetate octanoyltransferase
Comments: The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is a heterodimeric complex. The PqsC subunit acquires an octanoyl group from octanoyl-CoA and attaches it to an internal cysteine residue. Together with the PqsB subunit, the proteins catalyse the coupling of the octanoyl group with (2-aminobenzoyl)acetate, leading to decarboxylation and dehydration events that result in closure of the quinoline ring.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Dulcey, C.E., Dekimpe, V., Fauvelle, D.A., Milot, S., Groleau, M.C., Doucet, N., Rahme, L.G., Lepine, F. and Deziel, E. The end of an old hypothesis: the pseudomonas signaling molecules 4-hydroxy-2-alkylquinolines derive from fatty acids, not 3-ketofatty acids. Chem. Biol. 20 (2013) 1481–1491. [DOI] [PMID: 24239007]
2.  Drees, S.L., Li, C., Prasetya, F., Saleem, M., Dreveny, I., Williams, P., Hennecke, U., Emsley, J. and Fetzner, S. PqsBC, a condensing enzyme in the biosynthesis of the Pseudomonas aeruginosa quinolone signal: crystal structure, inhibition, and reaction mechanism. J. Biol. Chem. 291 (2016) 6610–6624. [DOI] [PMID: 26811339]
[EC 2.3.1.230 created 2013, modified 2017]
 
 
EC 1.14.14.119     Relevance: 89.8%
Accepted name: fumitremorgin C monooxygenase
Reaction: fumitremorgin C + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = 12α,13α-dihydroxyfumitremorgin C + 2 [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of fumitremorgin alkaloid biosynthesis (part 2), click here
Glossary: fumitremorgin C = (5aS,12S,14aS)-9-methoxy-12-(2-methylprop-1-en-1-yl)-1,2,3,5a,6,11,12,14a-octahydro-5H,14H-pyrrolo[1′′,2′′:4′,5′]pyrazino[1′,2′:1,6]pyrido[3,4-b]indole-5,14-dione
12α,13α-dihydroxyfumitremorgin = (5aR,6S,12S,14aS)-5a,6-dihydroxy-9-methoxy-12-(2-methylprop-1-en-1-yl)-1,2,3,5a,6,11,12,14a-octahydro-5H,14H-pyrrolo[1′′,2′′:4′,5′]pyrazino[1′,2′:1,6]pyrido[3,4-b]indole-5,14-dione
Other name(s): ftmG (gene name)
Systematic name: fumitremorgin C,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12α,13α-dihydroxyfumitremorgin C-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. Involved in the biosynthetic pathway of the indole alkaloid verruculogen.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kato, N., Suzuki, H., Takagi, H., Asami, Y., Kakeya, H., Uramoto, M., Usui, T., Takahashi, S., Sugimoto, Y. and Osada, H. Identification of cytochrome P450s required for fumitremorgin biosynthesis in Aspergillus fumigatus. ChemBioChem 10 (2009) 920–928. [DOI] [PMID: 19226505]
[EC 1.14.14.119 created 2013 as EC 1.14.13.177, transferred 2018 to EC 1.14.14.119]
 
 
EC 1.14.99.57     Relevance: 89.6%
Accepted name: heme oxygenase (mycobilin-producing)
Reaction: (1) protoheme + 3 reduced acceptor + 3 O2 = mycobilin a + Fe2+ + 3 acceptor + 3 H2O
(2) protoheme + 3 reduced acceptor + 3 O2 = mycobilin b + Fe2+ + 3 acceptor + 3 H2O
For diagram of mycobilin biosynthesis, click here
Glossary: mycobilin a = 8,12-bis(2-carboxyethyl)-19-formyl-3,7,13,18-tetramethyl-3,17-divinylbiladiene-ab-1,15(21H)-dione
mycobilin b = 8,12-bis(2-carboxyethyl)-19-formyl-2,7,13,17-tetramethyl-3,18-divinylbiladiene-ab-1,15(21H)-dione
Other name(s): mhuD (gene name)
Systematic name: protoheme,donor:oxygen oxidoreductase (mycobilin-producing)
Comments: The enzyme, characterized from the bacterium Mycobacterium tuberculosis, is involved in heme degradation and iron utilization. The enzyme binds two stacked protoheme molecules per monomer. Unlike the canonical heme oxygenases, the enzyme does not release carbon monoxide or formaldehyde. Instead, it forms unique products, named mycobilins, that retain the α-meso-carbon at the ring cleavage site as an aldehyde group. EC 1.6.2.4, NADPH-hemoprotein reductase, can act as electron donor in vitro.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Chim, N., Iniguez, A., Nguyen, T.Q. and Goulding, C.W. Unusual diheme conformation of the heme-degrading protein from Mycobacterium tuberculosis. J. Mol. Biol. 395 (2010) 595–608. [DOI] [PMID: 19917297]
2.  Nambu, S., Matsui, T., Goulding, C.W., Takahashi, S. and Ikeda-Saito, M. A new way to degrade heme: the Mycobacterium tuberculosis enzyme MhuD catalyzes heme degradation without generating CO. J. Biol. Chem. 288 (2013) 10101–10109. [DOI] [PMID: 23420845]
3.  Graves, A.B., Morse, R.P., Chao, A., Iniguez, A., Goulding, C.W. and Liptak, M.D. Crystallographic and spectroscopic insights into heme degradation by Mycobacterium tuberculosis MhuD. Inorg. Chem. 53 (2014) 5931–5940. [DOI] [PMID: 24901029]
[EC 1.14.99.57 created 2017]
 
 
EC 2.5.1.77      
Transferred entry: 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase. Now EC 2.5.1.147, 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-methylphenol transferase and EC 4.3.1.32, 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase.
[EC 2.5.1.77 created 2010, 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 1.14.99.63     Relevance: 88.5%
Accepted name: β-carotene 4-ketolase
Reaction: (1) β-carotene + 2 reduced acceptor + 2 O2 = echinenone + 2 acceptor + 3 H2O
(2) echinenone + 2 reduced acceptor + 2 O2 = canthaxanthin + 2 acceptor + 3 H2O
For diagram of canthaxanthin biosynthesis, click here
Glossary: echinenone = β,β-caroten-4-one
canthaxanthin = β,β-carotene-4,4′-dione
zeaxanthin = β,β-carotene-3,3′-diol
astaxanthin = 3,3′-dihydroxy-β,β-carotene-4,4′-dione
Other name(s): BKT (ambiguous); β-C-4 oxygenase; β-carotene ketolase; crtS (gene name); crtW (gene name)
Systematic name: β-carotene,donor:oxygen oxidoreductase (echinenone-forming)
Comments: The enzyme, studied from algae, plants, fungi, and bacteria, adds an oxo group at position 4 of a carotenoid β ring. It is involved in the biosynthesis of carotenoids such as astaxanthin and flexixanthin. The enzyme does not act on β rings that are hydroxylated at position 3, such as in zeaxanthin (cf. EC 1.14.99.64, zeaxanthin 4-ketolase). The enzyme from the yeast Xanthophyllomyces dendrorhous is bifuntional and also catalyses the activity of EC 1.14.15.24, β-carotene 3-hydroxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lotan, T. and Hirschberg, J. Cloning and expression in Escherichia coli of the gene encoding β-C-4-oxygenase, that converts β-carotene to the ketocarotenoid canthaxanthin in Haematococcus pluvialis. FEBS Lett. 364 (1995) 125–128. [PMID: 7750556]
2.  Breitenbach, J., Misawa, N., Kajiwara, S. and Sandmann, G. Expression in Escherichia coli and properties of the carotene ketolase from Haematococcus pluvialis. FEMS Microbiol. Lett. 140 (1996) 241–246. [PMID: 8764486]
3.  Steiger, S. and Sandmann, G. Cloning of two carotenoid ketolase genes from Nostoc punctiforme for the heterologous production of canthaxanthin and astaxanthin. Biotechnol. Lett. 26 (2004) 813–817. [PMID: 15269553]
4.  Ojima, K., Breitenbach, J., Visser, H., Setoguchi, Y., Tabata, K., Hoshino, T., van den Berg, J. and Sandmann, G. Cloning of the astaxanthin synthase gene from Xanthophyllomyces dendrorhous (Phaffia rhodozyma) and its assignment as a β-carotene 3-hydroxylase/4-ketolase. Mol. Genet. Genomics 275 (2006) 148–158. [PMID: 16416328]
5.  Tao, L., Yao, H., Kasai, H., Misawa, N. and Cheng, Q. A carotenoid synthesis gene cluster from Algoriphagus sp. KK10202C with a novel fusion-type lycopene β-cyclase gene. Mol. Genet. Genomics 276 (2006) 79–86. [PMID: 16625353]
6.  Kathiresan, S., Chandrashekar, A., Ravishankar, G.A. and Sarada, R. Regulation of astaxanthin and its intermediates through cloning and genetic transformation of β-carotene ketolase in Haematococcus pluvialis. J. Biotechnol. 196-197 (2015) 33–41. [PMID: 25612872]
[EC 1.14.99.63 created 2018]
 
 
EC 5.5.1.8     Relevance: 88.4%
Accepted name: (+)-bornyl diphosphate synthase
Reaction: geranyl diphosphate = (+)-bornyl diphosphate
For diagram of bornane and related monoterpenoids, click here
Glossary: (+)-bornyl diphosphate = (1R,2S,4R)-1,7,7-trimethylbicyclo[2.2.1]heptan-2-yl diphosphate
Other name(s): bornyl pyrophosphate synthase (ambiguous); bornyl pyrophosphate synthetase (ambiguous); (+)-bornylpyrophosphate cyclase; geranyl-diphosphate cyclase (ambiguous); (+)-bornyl-diphosphate lyase (decyclizing)
Systematic name: (+)-bornyl-diphosphate lyase (ring-opening)
Comments: Requires Mg2+. The enzyme from Salvia officinalis (sage) can also use (3R)-linalyl diphosphate or more slowly neryl diphosphate in vitro [3]. The reaction proceeds via isomeration of geranyl diphosphate to (3R)-linalyl diphosphate. The oxygen and phosphorus originally linked to C-1 of geranyl diphosphate end up linked to C-2 of (+)-bornyl diphosphate [3]. cf. EC 5.5.1.22 [(–)-bornyl diphosphate synthase].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 72668-91-8
References:
1.  Croteau, R. and Karp, F. Biosynthesis of monoterpenes: preliminary characterization of bornyl pyrophosphate synthetase from sage (Salvia officinalis) and demonstration that geranyl pyrophosphate is the preferred substrate for cyclization. Arch. Biochem. Biophys. 198 (1979) 512–522. [DOI] [PMID: 42356]
2.  Croteau, R., Gershenzon, J., Wheeler, C.J. and Satterwhite, D.M. Biosynthesis of monoterpenes: stereochemistry of the coupled isomerization and cyclization of geranyl pyrophosphate to camphane and isocamphane monoterpenes. Arch. Biochem. Biophys. 277 (1990) 374–381. [DOI] [PMID: 2178556]
3.  Croteau, R., Satterwhite, D.M., Cane, D.E. and Chang, C.C. Biosynthesis of monoterpenes. Enantioselectivity in the enzymatic cyclization of (+)- and (-)-linalyl pyrophosphate to (+)- and (-)-bornyl pyrophosphate. J. Biol. Chem. 261 (1986) 13438–13445. [PMID: 3759972]
4.  Croteau, R., Felton, N.M. and Wheeler, C.J. Stereochemistry at C-1 of geranyl pyrophosphate and neryl pyrophosphate in the cyclization to (+)- and (-)-bornyl pyrophosphate. J. Biol. Chem. 260 (1985) 5956–5962. [PMID: 3997807]
5.  Croteau, R.B., Shaskus, J.J., Renstrom, B., Felton, N.M., Cane, D.E., Saito, A. and Chang, C. Mechanism of the pyrophosphate migration in the enzymatic cyclization of geranyl and linalyl pyrophosphates to (+)- and (-)-bornyl pyrophosphates. Biochemistry 24 (1985) 7077–7085. [PMID: 4084562]
6.  McGeady, P. and Croteau, R. Isolation and characterization of an active-site peptide from a monoterpene cyclase labeled with a mechanism-based inhibitor. Arch. Biochem. Biophys. 317 (1995) 149–155. [DOI] [PMID: 7872777]
7.  Wise, M.L., Savage, T.J., Katahira, E. and Croteau, R. Monoterpene synthases from common sage (Salvia officinalis). cDNA isolation, characterization, and functional expression of (+)-sabinene synthase, 1,8-cineole synthase, and (+)-bornyl diphosphate synthase. J. Biol. Chem. 273 (1998) 14891–14899. [DOI] [PMID: 9614092]
8.  Whittington, D.A., Wise, M.L., Urbansky, M., Coates, R.M., Croteau, R.B. and Christianson, D.W. Bornyl diphosphate synthase: structure and strategy for carbocation manipulation by a terpenoid cyclase. Proc. Natl. Acad. Sci. USA 99 (2002) 15375–15380. [DOI] [PMID: 12432096]
9.  Peters, R.J. and Croteau, R.B. Alternative termination chemistries utilized by monoterpene cyclases: chimeric analysis of bornyl diphosphate, 1,8-cineole, and sabinene synthases. Arch. Biochem. Biophys. 417 (2003) 203–211. [DOI] [PMID: 12941302]
[EC 5.5.1.8 created 1984, modified 2012]
 
 
EC 2.5.1.107     Relevance: 87.7%
Accepted name: verruculogen prenyltransferase
Reaction: prenyl diphosphate + verruculogen = diphosphate + fumitremorgin A
For diagram of fumitremorgin alkaloid biosynthesis (part 2), click here
Glossary: prenyl diphosphate = dimethylallyl diphosphate
verruculogen = (5R,10S,10aR,14aS,15bS)-10,10a-dihydroxy-6-methoxy-2,2-dimethyl-5-(2-methylprop-1-en-1-yl)-1,10,10a,14,14a,15b-hexahydro-12H-3,4-dioxa-5a,11a,15a-triazacycloocta[1,2,3-lm]indeno[5,6-b]fluorene-11,15(2H,13H)-dione
fumitremorgin A = (5R,10S,10aR,14aS,15bS)-10a-hydroxy-7-methoxy-2,2-dimethyl-10-[(3-methylbut-2-en-1-yl)oxy]-5-(2-methylprop-1-en-1-yl)-1,10,10a,14,14a,15b-hexahydro-12H-3,4-dioxa-5a,11a,15a-triazacycloocta[1,2,3-lm]indeno[5,6-b]fluorene-11,15(H,13H)-dione
Other name(s): FtmPT3; dimethylallyl-diphosphate:verruculogen dimethylallyl-O-transferase
Systematic name: prenyl-diphosphate:verruculogen dimethylallyl-O-transferase
Comments: Found in a number of fungi. Catalyses the last step in the biosynthetic pathway of the indole alkaloid fumitremorgin A. The enzyme from the fungus Neosartorya fischeri is also active with fumitremorgin B and 12α,13α-dihydroxyfumitremorgin C.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Mundt, K., Wollinsky, B., Ruan, H.L., Zhu, T. and Li, S.M. Identification of the verruculogen prenyltransferase FtmPT3 by a combination of chemical, bioinformatic and biochemical approaches. ChemBioChem 13 (2012) 2583–2592. [DOI] [PMID: 23109474]
[EC 2.5.1.107 created 2013]
 
 
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 2.5.1.110     Relevance: 87.5%
Accepted name: 12α,13α-dihydroxyfumitremorgin C prenyltransferase
Reaction: prenyl diphosphate + 12α,13α-dihydroxyfumitremorgin C = diphosphate + fumitremorgin B
For diagram of fumitremorgin alkaloid biosynthesis (part 2), click here
Glossary: 12α,13α-dihydroxyfumitremorgin = (5aR,6S,12S,14aS)-5a,6-dihydroxy-9-methoxy-12-(2-methylprop-1-en-1-yl)-1,2,3,5a,6,11,12,14a-octahydro-5H,14H-pyrrolo[1′′,2′′:4′,5′]pyrazino[1′,2′:1,6]pyrido[3,4-b]indole-5,14-dione
fumitremorgin B = (5aR,6S,12S,14aS)-5a,6-dihydroxy-9-methoxy-11-(3-methylbut-2-en-1-yl)-12-(2-methylprop-1-en-1-yl)-1,2,3,5a,6,11,12,14a-octahydro-5H,14H-pyrrolo[1′′,2′′:4′,5′]pyrazino[1′,2′:1,6]pyrido[3,4-b]indole-5,14-dione
Other name(s): ftmH (gene name); FtmPT2; dimethylallyl-diphosphate:12α,13α-dihydroxyfumitremorgin C dimethylallyl-N-1-transferase
Systematic name: prenyl-diphosphate:12α,13α-dihydroxyfumitremorgin C prenyl-N-1-transferase
Comments: The enzyme from the fungus Aspergillus fumigatus also shows some activity with fumitremorgin C. Involved in the biosynthetic pathways of several indole alkaloids such as fumitremorgins and verruculogen.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Grundmann, A., Kuznetsova, T., Afiyatullov, S.Sh and Li, S.M. FtmPT2, an N-prenyltransferase from Aspergillus fumigatus, catalyses the last step in the biosynthesis of fumitremorgin B. ChemBioChem 9 (2008) 2059–2063. [DOI] [PMID: 18683158]
[EC 2.5.1.110 created 2013]
 
 
EC 5.5.1.22     Relevance: 87%
Accepted name: (–)-bornyl diphosphate synthase
Reaction: geranyl diphosphate = (–)-bornyl diphosphate
For diagram of bornane and related monoterpenoids, click here
Glossary: (–)-bornyl diphosphate = (2R,4S)-1,7,7-trimethylbicyclo[2.2.1]hept-2-yl diphosphate
Other name(s): bornyl pyrophosphate synthase (ambiguous); bornyl pyrophosphate synthetase (ambiguous); (–)-bornyl pyrophosphate cyclase; bornyl diphosphate synthase; geranyl-diphosphate cyclase (ambiguous); (–)-bornyl-diphosphate lyase (decyclizing)
Systematic name: (–)-bornyl-diphosphate lyase (ring-opening)
Comments: Requires Mg2+. The enzyme from Tanacetum vulgare (tansy) can also use (3S)-linalyl diphosphate or more slowly neryl diphosphate in vitro. The reaction proceeds via isomeration of geranyl diphosphate to (3S)-linalyl diphosphate [3]. The oxygen and phosphorus originally linked to C-1 of geranyl diphosphate end up linked to C-2 of (–)-bornyl diphosphate [4]. cf. EC 5.5.1.8 (+)-bornyl diphosphate synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 110639-17-3
References:
1.  Croteau, R., Gershenzon, J., Wheeler, C.J. and Satterwhite, D.M. Biosynthesis of monoterpenes: stereochemistry of the coupled isomerization and cyclization of geranyl pyrophosphate to camphane and isocamphane monoterpenes. Arch. Biochem. Biophys. 277 (1990) 374–381. [DOI] [PMID: 2178556]
2.  Croteau, R. and Shaskus, J. Biosynthesis of monoterpenes: demonstration of a geranyl pyrophosphate:(-)-bornyl pyrophosphate cyclase in soluble enzyme preparations from tansy (Tanacetum vulgare). Arch. Biochem. Biophys. 236 (1985) 535–543. [DOI] [PMID: 3970524]
3.  Croteau, R., Felton, N.M. and Wheeler, C.J. Stereochemistry at C-1 of geranyl pyrophosphate and neryl pyrophosphate in the cyclization to (+)- and (-)-bornyl pyrophosphate. J. Biol. Chem. 260 (1985) 5956–5962. [PMID: 3997807]
4.  Croteau, R.B., Shaskus, J.J., Renstrom, B., Felton, N.M., Cane, D.E., Saito, A. and Chang, C. Mechanism of the pyrophosphate migration in the enzymatic cyclization of geranyl and linalyl pyrophosphates to (+)- and (-)-bornyl pyrophosphates. Biochemistry 24 (1985) 7077–7085. [PMID: 4084562]
5.  Adam, K.P. and Croteau, R. Monoterpene biosynthesis in the liverwort Conocephalum conicum: demonstration of sabinene synthase and bornyl diphosphate synthase. Phytochemistry 49 (1998) 475–480. [DOI] [PMID: 9747540]
[EC 5.5.1.22 created 2012]
 
 
EC 2.1.1.225     Relevance: 86.2%
Accepted name: tRNA:m4X modification enzyme
Reaction: (1) S-adenosyl-L-methionine + cytidine4 in tRNAPro = S-adenosyl-L-homocysteine + 2′-O-methylcytidine4 in tRNAPro
(2) S-adenosyl-L-methionine + cytidine4 in tRNAGly(GCC) = S-adenosyl-L-homocysteine + 2′-O-methylcytidine4 in tRNAGly(GCC)
(3) S-adenosyl-L-methionine + adenosine4 in tRNAHis = S-adenosyl-L-homocysteine + 2′-O-methyladenosine4 in tRNAHis
For diagram of bornane and related monoterpenoids, click here
Other name(s): TRM13; Trm13p; tRNA:Xm4 modification enzyme
Systematic name: S-adenosyl-L-methionine:tRNAPro/His/Gly(GCC) (cytidine/adenosine4-2′-O)-methyltransferase
Comments: The enzyme from Saccharomyces cerevisiae 2′-O-methylates cytidine4 in tRNAPro and tRNAGly(GCC), and adenosine4 in tRNAHis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wilkinson, M.L., Crary, S.M., Jackman, J.E., Grayhack, E.J. and Phizicky, E.M. The 2′-O-methyltransferase responsible for modification of yeast tRNA at position 4. RNA 13 (2007) 404–413. [DOI] [PMID: 17242307]
[EC 2.1.1.225 created 2011]
 
 
EC 1.1.3.14     Relevance: 83.3%
Accepted name: catechol oxidase (dimerizing)
Reaction: 4 catechol + 3 O2 = 2 dibenzo[1,4]dioxin-2,3-dione + 6 H2O
For diagram of reaction, click here
Systematic name: catechol:oxygen oxidoreductase (dimerizing)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-83-2
References:
1.  Nair, P.M. and Vining, L.C. Enzymic oxidation of catechol to diphenylenedioxide-2,3-quinone. Arch. Biochem. Biophys. 106 (1964) 422–427. [PMID: 14217190]
[EC 1.1.3.14 created 1972]
 
 
EC 2.4.1.278     Relevance: 83.1%
Accepted name: 3-α-mycarosylerythronolide B desosaminyl transferase
Reaction: dTDP-D-desosamine + 3-α-L-mycarosylerythronolide B = dTDP + erythromycin D
For diagram of erythromycin biosynthesis, click here
Glossary: dTDP-D-desosamine = dTDP-3,4,6-trideoxy-3-(dimethylamino)-α-D-xylo-hexopyranose
erythromycin D = (3R,4S,5S,6R,7R,9R,11R,12S,13R,14R)-4-(2,6-dideoxy-3-C-methyl-α-L-ribo-hexopyranosyloxy)-14-ethyl-7,12-dihydroxy-6-[3,4,6-trideoxy-3-(dimethylamino)-β-D-xylo-hexopyranosyloxy]-3,5,7,9,11,13-hexamethyloxacyclotetradecane-2,10-dione
3-O-α-mycarosylerythronolide B = (3R,4S,5R,6R,7R,9R,11R,12S,13R,14R)-4-(2,6-dideoxy-3-C-methyl-α-L-ribo-hexopyranosyloxy)-14-ethyl-6,7,12-trihydroxy-3,5,7,9,11,13-hexamethyloxacyclotetradecane-2,10-dione
Other name(s): EryCIII; dTDP-3-dimethylamino-4,6-dideoxy-α-D-glucopyranose:3-α-mycarosylerythronolide B 3-dimethylamino-4,6-dideoxy-α-D-glucosyltransferase
Systematic name: dTDP-3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose:3-α-mycarosylerythronolide B 3-dimethylamino-3,4,6-trideoxy-β-D-glucosyltransferase
Comments: The enzyme is involved in erythromycin biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Yuan, Y., Chung, H.S., Leimkuhler, C., Walsh, C.T., Kahne, D. and Walker, S. In vitro reconstitution of EryCIII activity for the preparation of unnatural macrolides. J. Am. Chem. Soc. 127 (2005) 14128–14129. [DOI] [PMID: 16218575]
2.  Lee, H.Y., Chung, H.S., Hang, C., Khosla, C., Walsh, C.T., Kahne, D. and Walker, S. Reconstitution and characterization of a new desosaminyl transferase, EryCIII, from the erythromycin biosynthetic pathway. J. Am. Chem. Soc. 126 (2004) 9924–9925. [DOI] [PMID: 15303858]
3.  Moncrieffe, M.C., Fernandez, M.J., Spiteller, D., Matsumura, H., Gay, N.J., Luisi, B.F. and Leadlay, P.F. Structure of the glycosyltransferase EryCIII in complex with its activating P450 homologue EryCII. J. Mol. Biol. 415 (2012) 92–101. [DOI] [PMID: 22056329]
[EC 2.4.1.278 created 2012, modified 2014]
 
 
EC 2.1.1.292     Relevance: 82.9%
Accepted name: carminomycin 4-O-methyltransferase
Reaction: S-adenosyl-L-methionine + carminomycin = S-adenosyl-L-homocysteine + daunorubicin
For diagram of daunorubicin biosynthesis, click here
Glossary: daunorubicin = (+)-daunomycin = (8S,10S)-8-acetyl-10-[(2S,4S,5S,6S)-4-amino-5-hydroxy-6-methyloxan-2-yl]oxy-6,8,11-trihydroxy-1-methoxy-9,10-dihydro-7H-tetracene-5,12-dione
carminomycin = (1S,3S)-3-acetyl-3,5,10,12-tetrahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranoside = (1S,3S)-3-acetyl-3,5,10,12-tetrahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydronaphthacen-1-yl 3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranoside
carubicin = (1S,3S)-3-acetyl-3,5,12-trihydroxy-10-methoxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranoside
= (8S,10S)-8-acetyl-10-[(3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranosyl)oxy]-6,8,11-trihydroxy-1-methoxy-7,8,9,10-tetrahydronaphthacene-5,12-dione
Other name(s): DnrK; DauK
Systematic name: S-adenosyl-L-methionine:carminomycin 4-O-methyltransferase
Comments: The enzymes from the Gram-positive bacteria Streptomyces sp. C5 and Streptomyces peucetius are involved in the biosynthesis of the anthracycline daunorubicin. In vitro the enzyme from Streptomyces sp. C5 also catalyses the 4-O-methylation of 13-dihydrocarminomycin, rhodomycin D and 10-carboxy-13-deoxycarminomycin [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Connors, N.C. and Strohl, W.R. Partial purification and properties of carminomycin 4-O-methyltransferase from Streptomyces sp. strain C5. J. Gen. Microbiol. 139 Pt 6 (1993) 1353–1362. [DOI] [PMID: 8360627]
2.  Jansson, A., Koskiniemi, H., Mantsala, P., Niemi, J. and Schneider, G. Crystal structure of a ternary complex of DnrK, a methyltransferase in daunorubicin biosynthesis, with bound products. J. Biol. Chem. 279 (2004) 41149–41156. [DOI] [PMID: 15273252]
3.  Dickens, M.L., Priestley, N.D. and Strohl, W.R. In vivo and in vitro bioconversion of ε-rhodomycinone glycoside to doxorubicin: functions of DauP, DauK, and DoxA. J. Bacteriol. 179 (1997) 2641–2650. [DOI] [PMID: 9098063]
[EC 2.1.1.292 created 2013]
 
 
EC 1.1.99.26     Relevance: 81.6%
Accepted name: 3-hydroxycyclohexanone dehydrogenase
Reaction: 3-hydroxycyclohexanone + acceptor = cyclohexane-1,3-dione + reduced acceptor
Systematic name: 3-hydroxycyclohexanone:acceptor 1-oxidoreductase
Comments: 2,6-Dichloroindophenol and methylene blue can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 123516-44-9
References:
1.  Dangel, W., Tschech, A. and Fuchs, G. Enzyme-reactions involved in anaerobic cyclohexanol metabolism by a denitrifying Pseudomonas species. Arch. Microbiol. 152 (1989) 273–279. [PMID: 2505723]
[EC 1.1.99.26 created 1992]
 
 
EC 1.1.1.63      
Transferred entry: testosterone 17β-dehydrogenase. Now EC 1.1.1.239, 3α(17β)-hydroxysteroid dehydrogenase (NAD+)
[EC 1.1.1.63 created 1965, deleted 2012]
 
 
EC 1.3.1.80      
Transferred entry: red chlorophyll catabolite reductase. Now classified as EC 1.3.7.12, red chlorophyll catabolite reductase
[EC 1.3.1.80 created 2007, deleted 2016]
 
 
EC 3.5.4.32     Relevance: 78.5%
Accepted name: 8-oxoguanine deaminase
Reaction: 8-oxoguanine + H2O = urate + NH3
Glossary: 8-oxoguanine = 2-amino-7,9-dihydro-1H-purine-6,8-dione
Other name(s): 8-OGD
Systematic name: 8-oxoguanine aminohydrolase
Comments: Zn2+ is bound in the active site. 8-Oxoguanine is formed via the oxidation of guanine within DNA by reactive oxygen species. If uncorrected, this modification leads to the incorporation of 8-oxoG:A mismatches and eventually to G:C to T:A transversions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Hall, R.S., Fedorov, A.A., Marti-Arbona, R., Fedorov, E.V., Kolb, P., Sauder, J.M., Burley, S.K., Shoichet, B.K., Almo, S.C. and Raushel, F.M. The hunt for 8-oxoguanine deaminase. J. Am. Chem. Soc. 132 (2010) 1762–1763. [DOI] [PMID: 20088583]
[EC 3.5.4.32 created 2012]
 
 
EC 3.5.2.20     Relevance: 78.3%
Accepted name: isatin hydrolase
Reaction: isatin + H2O = isatinate
Glossary: isatin = 1H-indole-2,3-dione
isatinate = 2-(2-aminophenyl)-2-oxoacetate
Systematic name: isatin amidohydrolase
Comments: Requires Mn2+. This enzyme, found in several bacterial species, is involved in the degradation of indole-3-acetic acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Sommer, M.R. and Jochimsen, B. Identification of enzymes involved in indole-3-acetic acid degradation. Plant Soil 186 (1996) 143–149.
2.  Bjerregaard-Andersen, K., Sommer, T., Jensen, J.K., Jochimsen, B., Etzerodt, M. and Morth, J.P. A proton wire and water channel revealed in the crystal structure of isatin hydrolase. J. Biol. Chem. 289 (2014) 21351–21359. [DOI] [PMID: 24917679]
[EC 3.5.2.20 created 2014]
 
 
EC 3.5.4.21     Relevance: 78.1%
Accepted name: creatinine deaminase
Reaction: creatinine + H2O = N-methylhydantoin + NH3
For diagram of creatine biosynthesis, click here
Glossary: N-methylhydantoin = N-methylimidazolidine-2,4-dione
Other name(s): creatinine hydrolase; creatinine desiminase
Systematic name: creatinine iminohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-15-9
References:
1.  Szulmajster, J. Bacterial degradation of creatinine. II. Creatinine desimidase. Biochim. Biophys. Acta 30 (1958) 154–163. [DOI] [PMID: 13584408]
[EC 3.5.4.21 created 1972]
 
 
EC 1.14.13.105     Relevance: 76.2%
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 1.3.7.12     Relevance: 75.5%
Accepted name: red chlorophyll catabolite reductase
Reaction: primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
For diagram of chlorophyll catabolism, click here
Glossary: red chlorophyll catabolite = RCC = (7S,8S,101R)-8-(2-carboxyethyl)-17-ethyl-19-formyl-101-(methoxycarbonyl)-3,7,13,18-tetramethyl-2-vinyl-8,23-dihydro-7H-10,12-ethanobiladiene-ab-1,102(21H)-dione
primary fluorescent chlorophyll catabolite = pFCC = (82R,12S,13S)-12-(2-carboxyethyl)-3-ethyl-1-formyl-82-(methoxycarbonyl)-2,7,13,17-tetramethyl-18-vinyl-12,13-dihydro-8,10-ethanobilene-b-81,19(16H)-dione
Other name(s): RCCR; RCC reductase; red Chl catabolite reductase
Systematic name: primary fluorescent chlorophyll catabolite:ferredoxin oxidoreductase
Comments: The enzyme participates in chlorophyll degradation, which occurs during leaf senescence and fruit ripening in higher plants. The reaction requires reduced ferredoxin, which is generated from NADPH produced either through the pentose-phosphate pathway or by the action of photosystem I [1,2]. This reaction takes place while red chlorophyll catabolite is still bound to EC 1.14.15.17, pheophorbide a oxygenase [3]. Depending on the plant species used as the source of enzyme, one of two possible C-1 epimers of primary fluorescent chlorophyll catabolite (pFCC), pFCC-1 or pFCC-2, is normally formed, with all genera or species within a family producing the same isomer [3,4]. After modification and export, pFCCs are eventually imported into the vacuole, where the acidic environment causes their non-enzymic conversion into colourless breakdown products called non-fluorescent chlorophyll catabolites (NCCs) [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Rodoni, S., Mühlecker, W., Anderl, M., Kräutler, B., Moser, D., Thomas, H., Matile, P. and Hörtensteiner, S. Chlorophyll breakdown in senescent chloroplasts. Cleavage of pheophorbide a in two enzymic steps. Plant Physiol. 115 (1997) 669–676. [PMID: 12223835]
2.  Wüthrich, K.L., Bovet, L., Hunziker, P.E., Donnison, I.S. and Hörtensteiner, S. Molecular cloning, functional expression and characterisation of RCC reductase involved in chlorophyll catabolism. Plant J. 21 (2000) 189–198. [DOI] [PMID: 10743659]
3.  Pružinská, A., Anders, I., Aubry, S., Schenk, N., Tapernoux-Lüthi, E., Müller, T., Kräutler, B. and Hörtensteiner, S. In vivo participation of red chlorophyll catabolite reductase in chlorophyll breakdown. Plant Cell 19 (2007) 369–387. [DOI] [PMID: 17237353]
4.  Hörtensteiner, S. Chlorophyll degradation during senescence. Annu. Rev. Plant Biol. 57 (2006) 55–77. [DOI] [PMID: 16669755]
5.  Rodoni, S., Vicentini, F., Schellenberg, M., Matile, P. and Hörtensteiner, S. Partial purification and characterization of red chlorophyll catabolite reductase, a stroma protein involved in chlorophyll breakdown. Plant Physiol. 115 (1997) 677–682. [PMID: 12223836]
[EC 1.3.7.12 created 2007 as EC 1.3.1.80, transferred 2016 to EC 1.3.7.12]
 
 
EC 1.1.1.321     Relevance: 74.3%
Accepted name: benzil reductase [(R)-benzoin forming]
Reaction: (R)-benzoin + NADP+ = benzil + NADPH + H+
Glossary: (R)-benzoin = (2R)-2-hydroxy-1,2-diphenylethanone
benzil = 1,2-diphenylethane-1,2-dione
Systematic name: (R)-benzoin:NADP+ oxidoreductase
Comments: The enzyme from the bacterium Xanthomonas oryzae is able to reduce enantioselectively only one of the two carbonyl groups of benzil to give optically active (R)-benzoin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Konishi, J., Ohta, H. and Tuchihashi, G. Asymmetric reduction of benzil to benzoin catalyzed by the enzyme system of a microorganism. Chem. Lett. 14 (1985) 1111–1112.
[EC 1.1.1.321 created 2012]
 
 
EC 1.14.99.4     Relevance: 74.2%
Accepted name: progesterone monooxygenase
Reaction: progesterone + reduced acceptor + O2 = testosterone acetate + acceptor + H2O
Other name(s): progesterone hydroxylase
Systematic name: progesterone,hydrogen-donor:oxygen oxidoreductase (hydroxylating)
Comments: Has a wide specificity. A single enzyme from ascomycete the Neonectria radicicola (EC 1.14.13.54 ketosteroid monooxygenase) catalyses both this reaction and that catalysed by EC 1.14.99.12 androst-4-ene-3,17-dione monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-85-2
References:
1.  Rahim, M.A. and Sih, C.J. Mechanisms of steroid oxidation by microorganisms. XI. Enzymatic cleavage of the pregnane side chain. J. Biol. Chem. 241 (1966) 3615–3623. [PMID: 5950688]
[EC 1.14.99.4 created 1972, modified 1999]
 
 
EC 1.13.11.81     Relevance: 72.2%
Accepted name: 7,8-dihydroneopterin oxygenase
Reaction: 7,8-dihydroneopterin + O2 = 7,8-dihydroxanthopterin + formate + glycolaldehyde
For diagram of methanopterin biosynthesis (part 1), click here
Glossary: 7,8-dihydroneopterin = 2-amino-6-[(1S,2R)-1,2,3-trihydroxypropyl]-7,8-dihydropteridin-4(3H)-one
7,8-dihydroxanthopterin = 2-amino-3,5,7,8-tetrahydropteridin-4,6-dione
Systematic name: 7,8-dihydroneopterin:oxygen oxidoreductase
Comments: The enzyme from the bacterium Mycobacterium tuberculosis is multifunctional and also catalyses the epimerisation of the 2′-hydroxy group of 7,8-dihydroneopterin (EC 5.1.99.8, 7,8-dihydroneopterin epimerase) and the reaction of EC 4.1.2.25 (dihydroneopterin aldolase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Czekster, C.M. and Blanchard, J.S. One substrate, five products: reactions catalyzed by the dihydroneopterin aldolase from Mycobacterium tuberculosis. J. Am. Chem. Soc. 134 (2012) 19758–19771. [DOI] [PMID: 23150985]
[EC 1.13.11.81 created 2015]
 
 
EC 1.14.13.87      
Transferred entry: licodione synthase. Now EC 1.14.14.140, licodione synthase
[EC 1.14.13.87 created 2004, deleted 2018]
 
 
EC 1.1.1.278     Relevance: 71.4%
Accepted name: 3β-hydroxy-5α-steroid dehydrogenase
Reaction: 3β-hydroxy-5α-pregnane-20-one + NADP+ = 5α-pregnan-3,20-dione + NADPH + H+
For diagram of reaction, click here
Systematic name: 3β-hydroxy-5α-steroid:NADP+ 3-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 58875-02-8
References:
1.  Lindemann, P. and Luckner, M. Biosynthesis of pregnane derivatives in somatic embryos of Digitalis lanata. Phytochemistry 46 (1997) 507–513.
2.  Warneck, H.M. and Seitz, H.U. 3β-Hydroxysteroid oxidoreductase in suspension cultures of Digitalis lanata EHRH. Z. Naturforsch. C: Biosci. 45 (1990) 963–972. [PMID: 2291772]
[EC 1.1.1.278 created 2003]
 
 


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