Continued from EC 1.14.13.1 to EC 1.14.13.50
EC 1.14.13.51 to EC 1.14.13.100
See also EC 1.14.13.151 to EC 1.14.13.171
EC 1.14.13.151 to EC 1.14.13.171
Accepted name: senecionine N-oxygenase
Reaction: senecionine + NADPH + H+ + O2 = senecionine N-oxide + NADP+ + H2O
Other name(s): senecionine monooxygenase (N-oxide-forming); SNO
Systematic name: senecionine,NADPH:oxygen oxidoreductase (N-oxide-forming)
Comments: A flavoprotein. NADH cannot replace NADPH. While pyrrolizidine alkaloids of the senecionine and monocrotaline types are generally good substrates (e.g. senecionine, retrorsine and monocrotaline), the enzyme does not use ester alkaloids lacking an hydroxy group at C-7 (e.g. supinine and phalaenopsine), 1,2-dihydro-alkaloids (e.g. sarracine) or unesterified necine bases (e.g. senkirkine) as substrates [1]. Senecionine N-oxide is used by insects as a chemical defense: senecionine N-oxide is non-toxic, but it is bioactivated to a toxic form by the action of cytochrome P-450 oxidase when absorbed by insectivores.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 220581-68-0
References:
1. Lindigkeit, R., Biller, A., Buch, M., Schiebel, H.M., Boppre, M. and Hartmann, T. The two facies of pyrrolizidine alkaloids: the role of the tertiary amine and its N-oxide in chemical defense of insects with acquired plant alkaloids. Eur. J. Biochem. 245 (1997) 626-636. [PMID: 9182998]
2. Naumann, C., Hartmann, T. and Ober, D. Evolutionary recruitment of a flavin-dependent monooxygenase for the detoxification of host plant-acquired pyrrolizidine alkaloids in the alkaloid-defended arctiid moth Tyria jacobaeae. Proc. Natl. Acad. Sci. USA 99 (2002) 6085-6090. [PMID: 11972041]
Accepted name: psoralen synthase
Reaction: (+)-marmesin + NADPH + H+ + O2 = psoralen + NADP+ + acetone + 2 H2O
For diagram of reaction, click here
Glossary: (+)-marmesin = (S)-2-(2-hydroxypropan-2-yl)-2,3-dihydro-7H-furo[3,2-g]chromen-7-one
psoralen = 7H-furo[3,2-g]chromen-7-one
Other name(s): CYP71AJ1
Systematic name: (+)-marmesin,NADPH:oxygen oxidoreductase
Comments: This microsomal cytochrome P450-dependent enzyme is specific for (+)-marmesin, and to a much lesser extent 5-hydroxymarmesin, as substrate. Furanocoumarins protect plants from fungal invasion and herbivore attack. (+)-Columbianetin, the angular furanocoumarin analogue of the linear furanocoumarin (+)-marmesin, is not a substrate for the enzyme but it is a competitive inhibitor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Larbat, R., Kellner, S., Specker, S., Hehn, A., Gontier, E., Hans, J., Bourgaud, F. and Matern, U. Molecular cloning and functional characterization of psoralen synthase, the first committed monooxygenase of furanocoumarin biosynthesis. J. Biol. Chem. 282 (2007) 542-554. [PMID: 17068340]
Accepted name: 8-dimethylallylnaringenin 2'-hydroxylase
Reaction: sophoraflavanone B + NADPH + H+ + O2 = leachianone G + NADP+ + H2O
For diagram of reaction, click here
Glossary: sophoraflavanone B = (–)-(2S)-8-dimethylallylnaringenin = (–)-(2S)-5,7-dihydroxy-2-(4-hydroxyphenyl)-8-(3-methylbut-2-en-1-yl)chroman-4-one
leachianone G = (–-)-(2S)-2′-hydroxy-8-dimethylallylnaringenin = (–)-(2S)-2-(2,4-dihydroxyphenyl)-5,7-dihydroxy-8-(3-methylbut-2-en-1-yl)chroman-4-one
Other name(s): 8-DMAN 2'-hydroxylase
Systematic name: sophoraflavanone-B,NADPH:oxygen oxidoreductase (2'-hydroxylating)
Comments: A membrane-bound heme-thiolate protein that is associated with the endoplasmic reticulum [1,2]. This enzyme is specific for sophoraflavanone B as substrate. NADPH cannot be replaced by NADH, FAD or FMN. Along with EC 2.5.1.70 (naringenin 8-dimethylallyltransferase) and EC 2.5.1.71 (leachianone G 2"-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway. A member of the cytochrome-P450 monooxygenase family.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yamamoto, H., Yatou, A. and Inoue, K. 8-Dimethylallylnaringenin 2′-hydroxylase, the crucial cytochrome P450 mono-oxygenase for lavandulylated flavanone formation in Sophora flavescens cultured cells. Phytochemistry 58 (2001) 671-676. [PMID: 11672730]
2. Zhao, P., Inoue, K., Kouno, I. and Yamamoto, H. Characterization of leachianone G 2"-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures. Plant Physiol. 133 (2003) 1306-1313. [PMID: 14551337]
Accepted name: (+)-menthofuran synthase
Reaction: (+)-pulegone + NADPH + H+ + O2 = (+)-menthofuran + NADP+ + H2O
Other name(s): menthofuran synthase; (+)-pulegone 9-hydroxylase; (+)-MFS; cytochrome P450 menthofuran synthase
Systematic name: (+)-pulegone,NADPH:oxygen oxidoreductase (9-hydroxylating)
Comments: A heme-thiolate protein (P-450). 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 1.14.13.47, (S)-limonene 3-monooxygenase [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Bertea, C.M., Schalk, M., Karp, F., Maffei, M. and Croteau, R. Demonstration that menthofuran synthase of mint (Mentha) is a cytochrome P450 monooxygenase: cloning, functional expression, and characterization of the responsible gene. Arch. Biochem. Biophys. 390 (2001) 279-286. [PMID: 11396930]
2. Mahmoud, S.S. and Croteau, R.B. Menthofuran regulates essential oil biosynthesis in peppermint by controlling a downstream monoterpene reductase. Proc. Natl. Acad. Sci. USA 100 (2003) 14481-14486. [PMID: 14623962]
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 click here or click here or 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, CAS registry number:
References:
1. van der Werf, M.J., Swarts, H.J. and de Bont, J.A. Rhodococcus erythropolis DCL14 contains a novel degradation pathway for limonene. Appl. Environ. Microbiol. 65 (1999) 2092-2102. [PMID: 10224006]
2. Van Der Werf, M.J. Purification and characterization of a Baeyer-Villiger mono-oxygenase from Rhodococcus erythropolis DCL14 involved in three different monocyclic monoterpene degradation pathways. Biochem. J. 347 (2000) 693-701. [PMID: 10769172]
3. van der Werf, M.J. and Boot, A.M. Metabolism of carveol and dihydrocarveol in Rhodococcus erythropolis DCL14. Microbiology 146 (2000) 1129-1141. [PMID: 10832640]
Accepted name: epi-isozizaene 5-monooxygenase
Reaction: (+)-epi-isozizaene + 2 NADPH + 2 H+ + 2 O2 = albaflavenone + 2 NADP+ + 3 H2O (overall reaction)
(1a) (+)-epi-isozizaene + NADPH + H+ + O2 = (5S)-albaflavenol + NADP+ + H2O
(1b) (5S)-albaflavenol + NADPH + H+ + O2 = albaflavenone + NADP+ + 2 H2O
(2a) (+)-epi-isozizaene + NADPH + H+ + O2 = (5R)-albaflavenol + NADP+ + H2O
(2b) (5R)-albaflavenol + NADPH + H+ + O2 = albaflavenone + NADP+ + 2 H2O
For diagram of reaction, click here
Glossary: for epi-isozizaene click here.
Other name(s): CYP170A1
Systematic name: (+)-epi-isozizaene,NADPH:oxygen oxidoreductase (5-hydroxylating)
Comments: This cytochrome-P450 enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyses two sequential allylic oxidation reactions. The substrate epi-isozizaene, which is formed by the action of EC 4.2.3.37, epi-isozizaene synthase, is first oxidized to yield the epimeric intermediates (5R)-albaflavenol and (5S)-albaflavenol, which can be further oxidized to yield the sesquiterpenoid antibiotic albaflavenone.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 1207718-51-1
References:
1. Zhao, B., Lin, X., Lei, L., Lamb, D.C., Kelly, S.L., Waterman, M.R. and Cane, D.E. Biosynthesis of the sesquiterpene antibiotic albaflavenone in Streptomyces coelicolor A3(2). J. Biol. Chem. 283 (2008) 8183-8189. [PMID: 18234666]
Accepted name: limonene 1,2-monooxygenase
Reaction: (1) (S)-limonene + NAD(P)H + H+ + O2 = 1,2-epoxymenth-8-ene + NAD(P)+ + H2O
(2) (R)-limonene + NAD(P)H + H+ + O2 = 1,2-epoxymenth-8-ene + NAD(P)+ + H2O
For diagram of reaction, click here
Glossary: limonene = mentha-1,8-diene
(S)-limonene = (–)-limonene
(R)-limonene = (+)-limonene
limonene-1,2-epoxide = 1,2-epoxymenth-8-ene = 1-methyl-4-(prop-1-en-2-yl)-7-oxabicyclo[4.1.0]heptane
Systematic name: limonene,NAD(P)H:oxygen oxidoreductase
Comments: A flavoprotein (FAD). Limonene is the most widespread terpene and is formed by more than 300 plants. Rhodococcus erythropolis DCL14, a Gram-positive bacterium, is able to grow on both (S)-limonene and (R)-limonene as the sole source of carbon and energy. NADPH can act instead of NADH, although more slowly. It has not been established if the product formed is optically pure or a mixture of two enantiomers.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
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]
Accepted name: abieta-7,13-diene hydroxylase
Reaction: abieta-7,13-diene + NADPH + H+ + O2 = abieta-7,13-dien-18-ol + NADP+ + H2O
For diagram of reaction click here
Glossary: abieta-7,13-diene = (4aS,4bR,10aS)-7-isopropyl-1,1,4a-trimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthrene
abieta-7,13-dien-18-ol = ((1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthren-1-yl)methanol
Other name(s): abietadiene hydroxylase (ambiguous)
Systematic name: abieta-7,13-diene,NADPH:oxygen oxidoreductase (18-hydroxylating)
Comments: A heme-thiolate protein (P-450). This enzyme catalyses a step in the pathway of abietic acid biosynthesis. The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine). The enzyme is localized in the microsomal fraction and requires both oxygen and NADPH. Inhibition by carbon monoxide and several substituted N-heterocyclic inhibitors suggests that the enzyme is a cytochrome P-450-dependent monooxygenase [1]. Activity is induced by wounding of the plant tissue [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Funk, C. and Croteau, R. Diterpenoid resin acid biosynthesis in conifers: characterization of two cytochrome P450-dependent monooxygenases and an aldehyde dehydrogenase involved in abietic acid biosynthesis. Arch. Biochem. Biophys. 308 (1994) 258-266. [PMID: 8311462]
2. Funk, C., Lewinsohn, E., Vogel, B.S., Steele, C.L. and Croteau, R. Regulation of oleoresinosis in grand fir (Abies grandis) (coordinate induction of monoterpene and diterpene cyclases and two cytochrome P450-dependent diterpenoid hydroxylases by stem wounding). Plant Physiol. 106 (1994) 999-1005. [PMID: 12232380]
Accepted name: abieta-7,13-dien-18-ol hydroxylase
Reaction: abieta-7,13-dien-18-ol + NADPH + H+ + O2 = abieta-7,13-dien-18-al + NADP+ + 2 H2O (overall reaction)
(1a) abieta-7,13-dien-18-ol + NADPH + H+ + O2 = abieta-7,13-dien-18,18-diol + + NADP+ + H2O
(1b) abieta-7,13-dien-18,18-diol = abieta-7,13-dien-18-al + H2O (spontaneous)
For diagram of reaction click here
Glossary: abieta-7,13-dien-18-ol = ((1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthren-1-yl)methanol
abieta-7,13-dien-18-al = (1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthrene-1-carbaldehyde
Other name(s): CYP720B1; PtAO; abietadienol hydroxylase (ambiguous)
Systematic name: abieta-7,13-dien-18-ol,NADPH:oxygen oxidoreductase (18-hydroxylating)
Comments: A heme-thiolate protein (P-450). This enzyme catalyses a step in the pathway of abietic acid biosynthesis. The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine) [1], and the gene encoding the enzyme has been identified in Pinus taeda (loblolly pine) [3]. The recombinant enzyme catalyses the oxidation of multiple diterpene alcohol and aldehydes, including levopimaradienol, isopimara-7,15-dienol, isopimara-7,15-dienal, dehydroabietadienol and dehydroabietadienal. It is not able to oxidize abietadiene.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Funk, C. and Croteau, R. Diterpenoid resin acid biosynthesis in conifers: characterization of two cytochrome P450-dependent monooxygenases and an aldehyde dehydrogenase involved in abietic acid biosynthesis. Arch. Biochem. Biophys. 308 (1994) 258-266. [PMID: 8311462]
2. Funk, C., Lewinsohn, E., Vogel, B.S., Steele, C.L. and Croteau, R. Regulation of oleoresinosis in grand fir (Abies grandis) (coordinate induction of monoterpene and diterpene cyclases and two cytochrome P450-dependent diterpenoid hydroxylases by stem wounding). Plant Physiol. 106 (1994) 999-1005. [PMID: 12232380]
3. Ro, D.K., Arimura, G., Lau, S.Y., Piers, E. and Bohlmann, J. Loblolly pine abietadienol/abietadienal oxidase PtAO (CYP720B1) is a multifunctional, multisubstrate cytochrome P450 monooxygenase. Proc. Natl. Acad. Sci. USA 102 (2005) 8060-8065. [PMID: 15911762]
Accepted name: geranylgeraniol 18-hydroxylase
Reaction: geranylgeraniol + NADPH + H+ + O2 = 18-hydroxygeranylgeraniol + NADP+ + H2O
For diagram click here.
glossary: plaunotol = 18-hydroxygeranylgeraniol
Other name(s): GGOH-18-hydroxylase
Systematic name: geranylgeraniol,NADPH:oxygen oxidoreductase (18-hydroxylating)
Comments: A heme-thiolate protein (P-450).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Tansakul, P. and De-Eknamkul, W. Geranylgeraniol-18-hydroxylase: the last enzyme in the plaunotol biosynthetic pathway in Croton sublyratus. Phytochemistry 47 (1998) 1241-1246.
Accepted name: methanesulfonate monooxygenase
Reaction: methanesulfonate + NADH + H+ + O2 = formaldehyde + NAD+ + sulfite + H2O
Glossary: methanesulfonate = CH3-SO3-
formaldehyde = H-CHO
Other name(s): mesylate monooxygenase; mesylate,reduced-FMN:oxygen oxidoreductase; MsmABC; methanesulfonic acid monooxygenase; MSA monooxygenase; MSAMO; methanesulfonate,FMNH2:oxygen oxidoreductase
Systematic name: methanesulfonate,NADH:oxygen oxidoreductase
Comments: A flavoprotein. Methanesulfonate is the simplest of the sulfonates and is a substrate for the growth of certain methylotrophic microorganisms. Compared with EC 1.14.14.5, alkanesulfonate monooxygenase, this enzyme has a restricted substrate range that includes only the short-chain aliphatic sulfonates (methanesulfonate to butanesulfonate) and excludes all larger molecules, such as arylsulfonates [1]. The enzyme from the bacterium Methylosulfonomonas methylovora is a multicomponent system comprising a hydroxylase, a reductase (MsmD; EC 1.5.1.29, FMN reductase) and a ferredoxin (MsmC). The hydroxylase has both large (MsmA) and small (MsmB) subunits, with each large subunit containing a Rieske-type [2Fe-2S] centre.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. de Marco, P., Moradas-Ferreira, P., Higgins, T.P., McDonald, I., Kenna, E.M. and Murrell, J.C. Molecular analysis of a novel methanesulfonic acid monooxygenase from the methylotroph Methylosulfonomonas methylovora. J. Bacteriol. 181 (1999) 2244-2251. [PMID: 10094704]
2. Higgins, T.P., Davey, M., Trickett, J., Kelly, D.P. and Murrell, J.C. Metabolism of methanesulfonic acid involves a multicomponent monooxygenase enzyme. Microbiology 142 (1996) 251-260. [PMID: 8932698]
Accepted name: 3-epi-6-deoxocathasterone 23-monooxygenase
Reaction: (1) 3-epi-6-deoxocathasterone + NADPH + H+ + O2 = 6-deoxotyphasterol + NADP+ + H2O
(2) (22S,24R)-22-hydroxy-5α-ergostan-3-one + NADPH + H+ + O2 = 3-dehydro-6-deoxoteasterone + NADP+ + H2O
Other name(s): cytochrome P450 90C1; CYP90D1; CYP90C1
Systematic name: 3-epi-6-deoxocathasterone,NADPH:oxygen oxidoreductase (C-23-hydroxylating)
Comments: This enzyme is involved in brassinosteroid biosynthesis. C-23 hydroxylation shortcuts bypass campestanol, 6-deoxocathasterone, and 6-deoxoteasterone and lead directly from (22S,24R)-22-hydroxy-5α-ergostan-3-one and 3-epi-6-deoxocathasterone to 3-dehydro-6-deoxoteasterone and 6-deoxotyphasterol [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Ohnishi, T., Szatmari, A.M., Watanabe, B., Fujita, S., Bancos, S., Koncz, C., Lafos, M., Shibata, K., Yokota, T., Sakata, K., Szekeres, M. and Mizutani, M. C-23 hydroxylation by Arabidopsis CYP90C1 and CYP90D1 reveals a novel shortcut in brassinosteroid biosynthesis. Plant Cell 18 (2006) 3275-3288. [PMID: 17138693]
Accepted name: FAD-dependent urate hydroxylase
Reaction: urate + NADH + H+ + O2 = 5-hydroxyisourate + NAD+ + H2O
Other name(s): HpxO enzyme; FAD-dependent urate oxidase; urate hydroxylase
Systematic name: urate,NADH:oxygen oxidoreductase (5-hydroxyisourate forming)
Comments: A flavoprotein. The reaction is part of the purine catabolic pathway in the bacterium Klebsiella pneumoniae. The enzyme is different from EC 1.7.3.3, factor-independent urate hydroxylase, found in most plants, which produces hydrogen peroxide. The product of the enzyme is a substrate for EC 3.5.2.17, hydroxyisourate hydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. O'Leary, S.E., Hicks, K.A., Ealick, S.E. and Begley, T.P. Biochemical characterization of the HpxO enzyme from Klebsiella pneumoniae, a novel FAD-dependent urate oxidase. Biochemistry 48 (2009) 3033-3035. [PMID: 19260710]
Accepted name: 6-hydroxynicotinate 3-monooxygenase
Reaction: 6-hydroxynicotinate + NADH + H+ + O2 = 2,5-dihydroxypyridine + NAD+ + H2O + CO2
Other name(s): NicC; 6HNA monooxygenase; HNA-3-monooxygenase
Systematic name: 6-hydroxynicotinate,NADH:oxygen oxidoreductase (3-hydroxylating, decarboxylating)
Comments: A flavoprotein (FAD) [1]. The reaction is involved in the aerobic catabolism of nicotinic acid.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Nakano, H., Wieser, M., Hurh, B., Kawai, T., Yoshida, T., Yamane, T. and Nagasawa, T. Purification, characterization and gene cloning of 6-hydroxynicotinate 3-monooxygenase from Pseudomonas fluorescens TN5. Eur. J. Biochem. 260 (1999) 120-126. [PMID: 10091591]
2. Jimenez, J.I., Canales, A., Jimenez-Barbero, J., Ginalski, K., Rychlewski, L., Garcia, J.L. and Diaz, E. Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440. Proc. Natl. Acad. Sci. USA 105 (2008) 11329-11334. [PMID: 18678916]
Accepted name: angelicin synthase
Reaction: (+)-columbianetin + NADPH + H+ + O2 = angelicin + NADP+ + acetone + 2 H2O
Other name(s): CYP71AJ4 (gene name)
Systematic name: (+)-columbianetin,NADPH:oxygen oxidoreductase
Comments: This P450 monooxygenase enzyme is involved in the formation of angular furanocoumarins. Attacks its substrate by syn-elimination of hydrogen from C-3'.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Larbat, R., Hehn, A., Hans, J., Schneider, S., Jugde, H., Schneider, B., Matern, U. and Bourgaud, F. Isolation and functional characterization of CYP71AJ4 encoding for the first P450 monooxygenase of angular furanocoumarin biosynthesis. J. Biol. Chem. 284 (2009) 4776-4785. [PMID: 19098286]
Accepted name: geranylhydroquinone 3"-hydroxylase
Reaction: geranylhydroquinone + NADPH + H+ + O2 = 3"-hydroxygeranylhydroquinone + NADP+ + H2O
Glossary: 3"-hydroxygeranylhydroquinone = 2-[(2Z)-3-(hydroxymethyl)-7-methylocta-2,6-dien-1-yl]benzene-1,4-diol
Other name(s): GHQ 3"-hydroxylase
Systematic name: geranylhydroquinone,NADPH:oxygen oxidoreductase (3"-hydroxylating)
Comments: Contains cytochrome P450.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yamamoto, H., Inoue, K., Li, S.M. and Heide, L. Geranylhydroquinone 3"-hydroxylase, a cytochrome P-450 monooxygenase from Lithospermum erythrorhizon cell suspension cultures. Planta 210 (2000) 312-317. [PMID: 10664138]
Accepted name: isoleucine N-monooxygenase
Reaction: L-isoleucine + 2 O2 + 2 NADPH + 2 H+ = (E)-2-methylbutanal oxime + 2 NADP+ + CO2 + 3 H2O (overall reaction)
(1a) L-isoleucine + O2 + NADPH + H+ = N-hydroxy-L-isoleucine + NADP+ + H2O
(1b) N-hydroxy-L-isoleucine + O2 + NADPH + H+ = N,N-dihydroxy-L-isoleucine + NADP+ + H2O
(1c) N,N-dihydroxy-L-isoleucine = (E)-2-methylbutanal oxime + CO2 + H2O (spontaneous)
Other name(s): CYP79D3; CYP79D4
Systematic name: L-isoleucine,NADPH:oxygen oxidoreductase (N-hydroxylating)
Comments: A heme-thiolate protein (P-450). This enzyme catalyses two successive N-hydroxylations of L-isoleucine, the first committed steps in the biosynthesis of the cyanogenic glucoside lotaustralin in the plant Lotus japonicus. The product of the two hydroxylations, N,N-dihydroxy-L-isoleucine, is extremely labile and dehydrates spontaneously. The dehydrated product is then subject to a decarboxylation that produces the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The product, (E)-2-methylbutanal oxime, undergoes a spontaneous isomerization to the (Z) form. The enzyme can also accept L-valine as substrate, with a lower activity. It is different from EC 1.14.13.118 (valine N-monooxygenase), which prefers L-valine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Andersen, M.D., Busk, P.K., Svendsen, I. and Moller, B.L. Cytochromes P-450 from cassava (Manihot esculenta Crantz) catalyzing the first steps in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin. Cloning, functional expression in Pichia pastoris, and substrate specificity of the isolated recombinant enzymes. J. Biol. Chem. 275 (2000) 1966-1975. [PMID: 10636899]
2. Forslund, K., Morant, M., Jorgensen, B., Olsen, C.E., Asamizu, E., Sato, S., Tabata, S. and Bak, S. Biosynthesis of the nitrile glucosides rhodiocyanoside A and D and the cyanogenic glucosides lotaustralin and linamarin in Lotus japonicus. Plant Physiol. 135 (2004) 71-84. [PMID: 15122013]
Accepted name: valine N-monooxygenase
Reaction: L-valine + 2 O2 + 2 NADPH + 2 H+ = (E)-2-methylpropanal oxime + 2 NADP+ + CO2 + 3 H2O (overall reaction)
(1a) L-valine + O2 + NADPH + H+ = N-hydroxy-L-valine + NADP+ + H2O
(1b) N-hydroxy-L-valine + O2 + NADPH + H+ = N,N-dihydroxy-L-valine + NADP+ + H2O
(1c) N,N-dihydroxy-L-valine = (E)-2-methylpropanal oxime + CO2 + H2O (spontaneous)
Other name(s): CYP79D1; CYP79D2
Systematic name: L-valine,NADPH:oxygen oxidoreductase (N-hydroxylating)
Comments: A heme-thiolate protein (P-450). This enzyme catalyses two successive N-hydroxylations of L-valine, the first committed steps in the biosynthesis of the cyanogenic glucoside linamarin in Manihot esculenta (cassava). The product of the two hydroxylations, N,N-dihydroxy-L-valine, is extremely labile and dehydrates spontaneously. The dehydrated product is then subject to a decarboxylation that produces the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The product, (E)-2-methylpropanal-oxime, undergoes a spontaneous isomerization to the (Z) form. The enzyme can also accept L-isoleucine as substrate, with a lower activity. It is different from EC 1.14.13.117 (isoleucine N-monooxygenase), which prefers L-isoleucine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Andersen, M.D., Busk, P.K., Svendsen, I. and Moller, B.L. Cytochromes P-450 from cassava (Manihot esculenta Crantz) catalyzing the first steps in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin. Cloning, functional expression in Pichia pastoris, and substrate specificity of the isolated recombinant enzymes. J. Biol. Chem. 275 (2000) 1966-1975. [PMID: 10636899]
2. Forslund, K., Morant, M., Jorgensen, B., Olsen, C.E., Asamizu, E., Sato, S., Tabata, S. and Bak, S. Biosynthesis of the nitrile glucosides rhodiocyanoside A and D and the cyanogenic glucosides lotaustralin and linamarin in Lotus japonicus. Plant Physiol. 135 (2004) 71-84. [PMID: 15122013]
Accepted name: 5-epiaristolochene 1,3-dihydroxylase
Reaction: 5-epiaristolochene + 2 NADPH + 2 H+ + 2 O2 = capsidiol + 2 NADP+ + 2 H2O
For diagram of reaction click here.
Other name(s): 5-epi-aristolochene 1,3-dihydroxylase; EAH
Systematic name: 5-epiaristolochene,NADPH:oxygen oxidoreductase (1- and 3-hydroxylating)
Comments: A heme-thiolate protein (P-450). Kinetic studies suggest that 1β-hydroxyepiaristolochene is mainly formed first followed by hydroxylation at C-3. However the reverse order via 3α-hydroxyepiaristolochene does occur.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Ralston, L., Kwon, S.T., Schoenbeck, M., Ralston, J., Schenk, D.J., Coates, R.M. and Chappell, J. Cloning, heterologous expression, and functional characterization of 5-epi-aristolochene-1,3-dihydroxylase from tobacco (Nicotiana tabacum). Arch. Biochem. Biophys. 393 (2001) 222-235. [PMID: 11556809]
2. Takahashi, S., Zhao, Y., O'Maille, P.E., Greenhagen, B.T., Noel, J.P., Coates, R.M. and Chappell, J. Kinetic and molecular analysis of 5-epiaristolochene 1,3-dihydroxylase, a cytochrome P450 enzyme catalyzing successive hydroxylations of sesquiterpenes. J. Biol. Chem. 280 (2005) 3686-3696. [PMID: 15522862]
Accepted name: costunolide synthase
Reaction: germacra-1(10),4,11(13)-trien-12-oate + NADPH + H+ + O2 = (+)-costunolide + NADP+ + 2 H2O
For diagram of reaction click here.
Systematic name: germacra-1(10),4,11(13)-trien-12-oate,NADPH:oxygen oxidoreductase (6α-hydroxylating)
Comments: A heme-thiolate protein (P-450). The enzyme hydroxylates carbon C-6 of germacra-1(10),4,11(13)-trien-12-oate to give 6α-hydroxygermacra-1(10),4,11(13)-trien-12-oate, which probably spontaneously cyclises to form the lactone ring.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. de Kraker, J.W., Franssen, M.C., Joerink, M., de Groot, A. and Bouwmeester, H.J. Biosynthesis of costunolide, dihydrocostunolide, and leucodin. Demonstration of cytochrome p450-catalyzed formation of the lactone ring present in sesquiterpene lactones of chicory. Plant Physiol. 129 (2002) 257-268. [PMID: 12011356]
Accepted name: premnaspirodiene oxygenase
Reaction: (–)-vetispiradiene + 2 NADPH + 2 H+ + 2 O2 = solavetivone + 2 NADP+ + 3 H2O (overall reaction)
(1a) (–)-vetispiradiene + NADPH + H+ + O2 = solavetivol + NADP+ + H2O
(1b) solavetivol + NADPH + H+ + O2 = solavetivone + NADP+ + 2 H2O
For diagram of reaction click here.
Glossary: (–)-premnaspirodiene = (–)-vetispiradiene
Other name(s): HPO; Hyoscymus muticus premnaspirodiene oxygenase
Systematic name: (–)-vetispiradiene,NADPH:oxygen 2α-oxidoreductase
Comments: A heme-thiolate protein (P-450). The enzyme from the plant Hyoscymus muticus also hydroxylates valencene at C-2 to give the α-hydroxy compound, nootkatol, and this is converted into nootkatone. 5-Epiaristolochene and epieremophilene are hydroxylated at C-2 to give a 2β-hydroxy derivative which is not further oxidized.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Takahashi, S., Yeo, Y.S., Zhao, Y., O'Maille, P.E., Greenhagen, B.T., Noel, J.P., Coates, R.M. and Chappell, J. Functional characterization of premnaspirodiene oxygenase, a cytochrome P450 catalyzing regio- and stereo-specific hydroxylations of diverse sesquiterpene substrates. J. Biol. Chem. 282 (2007) 31744-31754. [PMID: 17715131]
Accepted name: chlorophyllide-a oxygenase
Reaction: chlorophyllide a + 2 O2 + 2 NADPH + 2 H+ = chlorophyllide b + 3 H2O + 2
NADP+ (overall reaction)
(1a) chlorophyllide a + O2 + NADPH + H+ = 71-hydroxychlorophyllide a + H2O + NADP+
(1b) 71-hydroxychlorophyllide a + O2 + NADPH + H+ = chlorophyllide b + 2 H2O + NADP+
For diagram of reaction click here.
Other name(s): chlorophyllide a oxygenase; chlorophyll-b synthase; CAO
Systematic name: chlorophyllide-a:oxygen 71-oxidoreductase
Comments: Chlorophyll b is required for the assembly of stable light-harvesting complexes (LHCs) in the chloroplast of green algae, cyanobacteria and plants [2,3]. Contains a mononuclear iron centre [3]. The enzyme catalyses two successive hydroxylations at the 7-methyl group of chlorophyllide a. The second step yields the aldehyde hydrate, which loses H2O spontaneously to form chlorophyllide b [2]. Chlorophyll a and protochlorophyllide a are not substrates [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Espineda, C.E., Linford, A.S., Devine, D. and Brusslan, J.A. The AtCAO gene, encoding chlorophyll a oxygenase, is required for chlorophyll b synthesis in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 96 (1999) 10507-10511. [PMID: 10468639]
2. Oster, U., Tanaka, R., Tanaka, A. and Rüdiger, W. Cloning and functional expression of the gene encoding the key enzyme for chlorophyll b biosynthesis (CAO) from Arabidopsis thaliana. Plant J. 21 (2000) 305-310. [PMID: 10758481]
3. Eggink, L.L., LoBrutto, R., Brune, D.C., Brusslan, J., Yamasato, A., Tanaka, A. and Hoober, J.K. Synthesis of chlorophyll b: localization of chlorophyllide a oxygenase and discovery of a stable radical in the catalytic subunit. BMC Plant Biol. 4 (2004) 5. [PMID: 15086960]
4. Porra, R.J., Schafer, W., Cmiel, E., Katheder, I. and Scheer, H. The derivation of the formyl-group oxygen of chlorophyll b in higher plants from molecular oxygen. Achievement of high enrichment of the 7-formyl-group oxygen from 18O2 in greening maize leaves. Eur. J. Biochem. 219 (1994) 671-679. [PMID: 8307032]
Accepted name: germacrene A hydroxylase
Reaction: (+)-germacrene A + NADPH + H+ + O2 = germacra-1(10),4,11(13)-trien-12-ol + NADP+ + H2O
For diagram of reaction click here.
Systematic name: (+)-germacrene-A,NADPH:oxygen oxidoreductase (12-hydroxylating)
Comments: A heme-thiolate protein (P-450). This is probably part of the biosynthesis of many sesquiterpenoid lactones. In Lactuca sativa EC 1.14.13.213 is a mutifunctional enzyme with EC 1.1.1.314, germacrene A alcohol dehydrogenase [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. de Kraker, J.W., Franssen, M.C., Dalm, M.C., de Groot, A. and Bouwmeester, H.J. Biosynthesis of germacrene A carboxylic acid in chicory roots. Demonstration of a cytochrome P450 (+)-germacrene A hydroxylase and NADP+-dependent sesquiterpenoid dehydrogenase(s) involved in sesquiterpene lactone biosynthesis. Plant Physiol. 125 (2001) 1930-1940. [PMID: 11299372]
2. Nguyen, D.T., Gopfert, J.C., Ikezawa, N., Macnevin, G., Kathiresan, M., Conrad, J., Spring, O. and Ro, D.K. Biochemical conservation and evolution of germacrene A oxidase in asteraceae. J. Biol. Chem. 285 (2010) 16588-16598. [PMID: 20351109]
Accepted name: phenylalanine N-monooxygenase
Reaction: L-phenylalanine + 2 O2 + 2 NADPH + 2 H+ = (E)-phenylacetaldoxime + 2 NADP+ + CO2 + 3 H2O (overall reaction)
(1a) L-phenylalanine + O2 + NADPH + H+ = N-hydroxy-L-phenylalanine + NADP+ + H2O
(1b) N-hydroxy-L-phenylalanine + O2 + NADPH + H+ = N,N-dihydroxy-L-phenylalanine + NADP+ + H2O
(1c) N,N-dihydroxy-L-phenylalanine = (E)-phenylacetaldoxime + CO2 + H2O
Other name(s): phenylalanine N-hydroxylase; CYP79A2
Systematic name: L-phenylalanine,NADPH:oxygen oxidoreductase (N-hydroxylating)
Comments: A heme-thiolate protein (P-450). This enzyme catalyses two successive N-hydroxylations of L-phenylalanine, the first committed steps in the biosynthesis of benzylglucosinolate. The product of the two hydroxylations, N,N-dihydroxy-L-phenylalanine, is extremely labile and dehydrates spontaneously.The dehydrated product is then subject to a decarboxylation that produces the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The product, (E)-phenylacetaldoxime, undergoes a spontaneous isomerization to the (Z) form.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Wittstock, U. and Halkier, B.A. Cytochrome P450 CYP79A2 from Arabidopsis thaliana L. Catalyzes the conversion of L-phenylalanine to phenylacetaldoxime in the biosynthesis of benzylglucosinolate. J. Biol. Chem. 275 (2000) 14659-14666. [PMID: 10799553]
Accepted name: tryptophan N-monooxygenase
Reaction: L-tryptophan + 2 O2 + 2 NADPH + 2 H+ = (E)-indol-3-ylacetaldoxime + 2 NADP+ + CO2 + 3 H2O (overall reaction)
(1a) L-tryptophan + O2 + NADPH + H+ = N-hydroxy-L-tryptophan + NADP+ + H2O
(1b) N-hydroxy-L-tryptophan + O2 + NADPH + H+ = N,N-dihydroxy-L-tryptophan + NADP+ + H2O
(1c) N,N-dihydroxy-L-tryptophan = (E)-indol-3-ylacetaldoxime + CO2 + H2O
Other name(s): tryptophan N-hydroxylase; CYP79B1; CYP79B2; CYP79B3
Systematic name: L-tryptophan,NADPH:oxygen oxidoreductase (N-hydroxylating)
Comments: A heme-thiolate protein (P-450). This enzyme catalyses two successive N-hydroxylations of L-tryptophan, the first steps in the biosynthesis of the both auxin and the indole alkaloid phytoalexin camalexin. The product of the two hydroxylations, N,N-dihydroxy-L-tryptophan, is extremely labile and dehydrates spontaneously.The dehydrated product is then subject to a decarboxylation that produces the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The product, (E)-indol-3-ylacetaldoxime, undergoes a spontaneous isomerization to the (Z) form.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Mikkelsen, M.D., Hansen, C.H., Wittstock, U. and Halkier, B.A. Cytochrome P450 CYP79B2 from Arabidopsis catalyzes the conversion of tryptophan to indole-3-acetaldoxime, a precursor of indole glucosinolates and indole-3-acetic acid. J. Biol. Chem. 275 (2000) 33712-33717. [PMID: 10922360]
2. Hull, A.K., Vij, R. and Celenza, J.L. Arabidopsis cytochrome P450s that catalyze the first step of tryptophan-dependent indole-3-acetic acid biosynthesis. Proc. Natl. Acad. Sci. USA 97 (2000) 2379-2384. [PMID: 10681464]
3. Zhao, Y., Hull, A.K., Gupta, N.R., Goss, K.A., Alonso, J., Ecker, J.R., Normanly, J., Chory, J. and Celenza, J.L. Trp-dependent auxin biosynthesis in Arabidopsis: involvement of cytochrome P450s CYP79B2 and CYP79B3. Genes Dev. 16 (2002) 3100-3112. [PMID: 12464638]
4. Naur, P., Hansen, C.H., Bak, S., Hansen, B.G., Jensen, N.B., Nielsen, H.L. and Halkier, B.A. CYP79B1 from Sinapis alba converts tryptophan to indole-3-acetaldoxime. Arch. Biochem. Biophys. 409 (2003) 235-241. [PMID: 12464264]
Accepted name: vitamin D3 24-hydroxylase
Reaction: (1) calcitriol + NADPH + H+ + O2 = calcitetrol + NADP+ + H2O
(2) calcidiol + NADPH + H+ + O2 = secalciferol + NADP+ + H2O
For diagram of reaction click here.
Glossary: calcidiol = 25-hydroxyvitamin D3
calcitriol = 1α,25-dihydroxyvitamin D3
calcitetrol = 1α,24R,25-trihydroxyvitamin D3
secalciferol = (24R)-24,25-dihydroxycalciol = 24R,25-dihydroxyvitamin D3
Other name(s): CYP24A1
Systematic name: calcitriol,NADPH:oxygen oxidoreductase (24-hydroxylating)
Comments: A heme-thiolate enzyme (P-450). The second donor, NADPH, donates electrons through EC 1.18.1.2, ferredoxinÑNADP+ reductase and a [2Fe-2S] ferredoxin. The enzyme can perform up to 6 rounds of hydroxylation of the substrate calcitriol leading to calcitroic acid. The human enzyme also shows 23-hydroxylating activity leading to 1,25 dihydroxyvitamin D3-26,23-lactone as end product while the mouse and rat enzymes do not.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Masuda, S., Strugnell, S.A., Knutson, J.C., St-Arnaud, R. and Jones, G. Evidence for the activation of 1α-hydroxyvitamin D2 by 25-hydroxyvitamin D-24-hydroxylase: delineation of pathways involving 1α,24-dihydroxyvitamin D2 and 1α,25-dihydroxyvitamin D2. Biochim. Biophys. Acta 1761 (2006) 221-234. [PMID: 16516540]
2. Hamamoto, H., Kusudo, T., Urushino, N., Masuno, H., Yamamoto, K., Yamada, S., Kamakura, M., Ohta, M., Inouye, K. and Sakaki, T. Structure-function analysis of vitamin D 24-hydroxylase (CYP24A1) by site-directed mutagenesis: amino acid residues responsible for species-based difference of CYP24A1 between humans and rats. Mol. Pharmacol. 70 (2006) 120-128. [PMID: 16617161]
3. Sakaki, T., Kagawa, N., Yamamoto, K. and Inouye, K. Metabolism of vitamin D3 by cytochromes P450. Front. Biosci. 10 (2005) 119-134. [PMID: 15574355]
4. Prosser, D.E., Kaufmann, M., O'Leary, B., Byford, V. and Jones, G. Single A326G mutation converts human CYP24A1 from 25-OH-D3-24-hydroxylase into -23-hydroxylase, generating 1α,25-(OH)2D3-26,23-lactone. Proc. Natl. Acad. Sci. USA 104 (2007) 12673-12678. [PMID: 17646648]
5. Kusudo, T., Sakaki, T., Abe, D., Fujishima, T., Kittaka, A., Takayama, H., Hatakeyama, S., Ohta, M. and Inouye, K. Metabolism of A-ring diastereomers of 1α,25-dihydroxyvitamin D3 by CYP24A1. Biochem. Biophys. Res. Commun. 321 (2004) 774-782. [PMID: 15358094]
6. Sawada, N., Kusudo, T., Sakaki, T., Hatakeyama, S., Hanada, M., Abe, D., Kamao, M., Okano, T., Ohta, M. and Inouye, K. Novel metabolism of 1 α,25-dihydroxyvitamin D3 with C24-C25 bond cleavage catalyzed by human CYP24A1. Biochemistry 43 (2004) 4530-4537. [PMID: 15078099]
7. Prosser, D.E. and Jones, G. Enzymes involved in the activation and inactivation of vitamin D. Trends Biochem. Sci. 29 (2004) 664-673. [PMID: 15544953]
Accepted name: 3-(3-hydroxyphenyl)propanoate hydroxylase
Reaction: (1) 3-(3-hydroxyphenyl)propanoate + NADH + H+ + O2 = 3-(2,3-dihydroxyphenyl)propanoate + H2O + NAD+
(2) (2E)-3-(3-hydroxyphenyl)prop-2-enoate + NADH + H+ + O2 = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + H2O + NAD+
Glossary: 3-hydroxycinnamate = 3-coumarate = 3-(3-hydroxyphenyl)prop-2-enoate
Other name(s): mhpA (gene name)
Systematic name: 3-(3-hydroxyphenyl)propanoate,NADH:oxygen oxidoreductase (2-hydroxylating)
Comments: A flavoprotein (FAD). This enzyme participates in a meta-cleavage pathway employed by the bacterium Escherichia coli for the degradation of various phenylpropanoid compounds.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Burlingame, R. and Chapman, P.J. Catabolism of phenylpropionic acid and its 3-hydroxy derivative by Escherichia coli. J. Bacteriol. 155 (1983) 113-121. [PMID: 6345502]
2. Burlingame, R.P., Wyman, L. and Chapman, P.J. Isolation and characterization of Escherichia coli mutants defective for phenylpropionate degradation. J. Bacteriol. 168 (1986) 55-64. [PMID: 3531186]
3. Ferrández, A., García, J.L. and Díaz, E. Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12. J. Bacteriol. 179 (1997) 2573-2581. [PMID: 9098055]
4. Díaz, E., Ferrández, A. and García, J.L. Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12. J. Bacteriol. 180 (1998) 2915-2923. [PMID: 9603882]
Accepted name: 7-methylxanthine demethylase
Reaction: 7-methylxanthine + O2 + NAD(P)H + H+ = xanthine + NAD(P)+ + H2O + formaldehyde
Other name(s): ndmC (gene name)
Systematic name: 7-methylxanthine:oxygen oxidoreductase (demethylating)
Comments: A non-heme iron oxygenase. The enzyme from the bacterium Pseudomonas putida prefers NADH over NADPH. The enzyme is specific for 7-methylxanthine [2]. Forms part of the caffeine degradation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:
References:
1. Summers, R.M., Louie, T.M., Yu, C.L. and Subramanian, M. Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source. Microbiology 157 (2011) 583-592. [PMID: 20966097]
2. Summers, R.M., Louie, T.M., Yu, C.L., Gakhar, L., Louie, K.C. and Subramanian, M. Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids. J. Bacteriol. 194 (2012) 2041Ð2049. [PMID: 22328667]
Accepted name: β-carotene 3-hydroxylase
Reaction: β-carotene + 2 NADH + 2 H+ + 2 O2 = zeaxanthin + 2 NAD+ + 2 H2O
(overall reaction)
(1a) β-carotene + NADH + H+ + O2 = β-cryptoxanthin + NAD+ + H2O
(1b) β-cryptoxanthin + NADH + H+ + O2 = zeaxanthin + NAD+ + H2O
For diagram of reaction click here and another example.
Other name(s): β-carotene 3,3'-monooxygenase; CrtZ
Systematic name: β-carotene,NADH:oxygen 3-oxidoreductase
Comments: Requires ferredoxin and Fe(II). Also acts on other carotenoids with a β-end group. In some species canthaxanthin is the preferred substrate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Sun, Z., Gantt, E. and Cunningham, F.X., Jr. Cloning and functional analysis of the β-carotene hydroxylase of Arabidopsis thaliana. J. Biol. Chem. 271 (1996) 24349-24352. [PMID: 8798688]
2. Fraser, P.D., Miura, Y. and Misawa, N. In vitro characterization of astaxanthin biosynthetic enzymes. J. Biol. Chem. 272 (1997) 6128-6135. [PMID: 9045623]
3. Fraser, P.D., Shimada, H. and Misawa, N. Enzymic confirmation of reactions involved in routes to astaxanthin formation, elucidated using a direct substrate in vitro assay. Eur. J. Biochem. 252 (1998) 229-236. [PMID: 9523693]
4. Bouvier, F., Keller, Y., d'Harlingue, A. and Camara, B. Xanthophyll biosynthesis: molecular and functional characterization of carotenoid hydroxylases from pepper fruits (Capsicum annuum L.). Biochim. Biophys. Acta 1391 (1998) 320-328. [PMID: 9555077]
5. Linden, H. Carotenoid hydroxylase from Haematococcus pluvialis: cDNA sequence, regulation and functional complementation. Biochim. Biophys. Acta 1446 (1999) 203-212. [PMID: 10524195]
6. Zhu, C., Yamamura, S., Nishihara, M., Koiwa, H. and Sandmann, G. cDNAs for the synthesis of cyclic carotenoids in petals of Gentiana lutea and their regulation during flower development. Biochim. Biophys. Acta 1625 (2003) 305-308. [PMID: 12591618]
7. Choi, S.K., Matsuda, S., Hoshino, T., Peng, X. and Misawa, N. Characterization of bacterial β-carotene 3,3'-hydroxylases, CrtZ, and P450 in astaxanthin biosynthetic pathway and adonirubin production by gene combination in Escherichia coli. Appl. Microbiol. Biotechnol. 72 (2006) 1238-1246. [PMID: 16614859]
Accepted name: pyrrole-2-carboxylate monooxygenase
Reaction: pyrrole-2-carboxylate + NADH + H+ + O2 = 5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
Other name(s): pyrrole-2-carboxylate oxygenase
Systematic name: pyrrole-2-carboxylate,NADH:oxygen oxidoreductase (5-hydroxylating)
Comments: A flavoprotein (FAD). The enzyme initiates the degradation of pyrrole-2-carboxylate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hormann, K. and Andreesen, J.R. Purification and characterization of a pyrrole-2-carboxylate oxygenase from Arthrobacter strain Py1. Biol. Chem. Hoppe-Seyler 375 (1994) 211-218. [PMID: 8011178]
2. Becker, D., Schrader, T. and Andreesen, J.R. Two-component flavin-dependent pyrrole-2-carboxylate monooxygenase from Rhodococcus sp. Eur. J. Biochem. 249 (1997) 739-747. [PMID: 9395321]
Accepted name: dimethyl-sulfide monooxygenase
Reaction: dimethyl sulfide + O2 + NADH + H+ = methanethiol + formaldehyde + NAD+ + H2O
Other name(s): dimethylsulfide monooxygenase
Systematic name: dimethyl sulfide,NADH:oxygen oxidoreductase
Comments: The enzyme has lower activity with diethyl sulfide and other short-chain alkyl methyl sulfides. Its activity is stimulated by combined addition of FMN, and, after depletion of cations, of Mg2+ and Fe2+. The enzyme from Hyphomicrobium is a two component system that includes an FMN-dependent reductase subunit and a monooxygenase subunit.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. De Bont, J.A.M., Van Dijken, J.P. and Harder, W. Dimethyl sulphoxide and dimethyl sulphide as a carbon, sulphur and energy source for growth of Hyphomicrobium S. J. Gen. Microbiol. 127 (1981) 315-323.
2. Boden, R., Borodina, E., Wood, A.P., Kelly, D.P., Murrell, J.C. and Schafer, H. Purification and characterization of dimethylsulfide monooxygenase from Hyphomicrobium sulfonivorans. J. Bacteriol. 193 (2011) 1250-1258. [PMID: 21216999]
Accepted name: squalene monooxygenase
Reaction: squalene + NADPH + H+ + O2 = (3S)-2,3-epoxy-2,3-dihydrosqualene + NADP+ + H2O
For diagram of reaction click here
Other name(s): squalene epoxidase; squalene-2,3-epoxide cyclase; squalene 2,3-oxidocyclase; squalene hydroxylase; squalene oxydocyclase; squalene-2,3-epoxidase
Systematic name: squalene,NADPH:oxygen oxidoreductase (2,3-epoxidizing)
Comments: A flavoprotein (FAD). This enzyme, together with EC 5.4.99.7 lanosterol synthase, was formerly known as squalene oxidocyclase. The electron donor, NADPH, is coupled via EC 1.6.2.4, NADPH—hemoprotein reductase [5,7].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Corey, E.J., Russey, W.E. and Ortiz de Montellano, P.R. 2,3-Oxidosqualene, an intermediate in the biological synthesis of sterols from squalene. J. Am. Chem. Soc. 88 (1966) 4750-4751. [PMID: 5918046]
2. Tchen, T.T. and Bloch, K. On the conversion of squalene to lanosterol in vitro. J. Biol. Chem. 226 (1957) 921-930. [PMID: 13438881]
3. van Tamelen, E.E., Willett, J.D., Clayton, R.B. and Lord, K.E. Enzymic conversion of squalene 2,3-oxide to lanosterol and cholesterol. J. Am. Chem. Soc. 88 (1966) 4752-4754. [PMID: 5918048]
4. Yamamoto, S. and Bloch, K. Studies on squalene epoxidase of rat liver. J. Biol. Chem. 245 (1970) 1670-1674. [PMID: 5438357]
5. Ono, T. and Bloch, K. Solubilization and partial characterization of rat liver squalene epoxidase. J. Biol. Chem. 250 (1975) 1571-1579. [PMID: 234459]
6. Satoh, T., Horie, M., Watanabe, H., Tsuchiya, Y. and Kamei, T. Enzymatic properties of squalene epoxidase from Saccharomyces cerevisiae. Biol. Pharm. Bull. 16 (1993) 349-352. [PMID: 8358382]
7. Chugh, A., Ray, A. and Gupta, J.B. Squalene epoxidase as hypocholesterolemic drug target revisited. Prog. Lipid Res. 42 (2003) 37-50. [PMID: 12467639]
8. He, F., Zhu, Y., He, M. and Zhang, Y. Molecular cloning and characterization of the gene encoding squalene epoxidase in Panax notoginseng. DNA Seq 19 (2008) 270-273. [PMID: 17852349]
Accepted name: pentalenene oxygenase
Reaction: pentalenene + 2 NADPH + 2 H+ + 2 O2 = pentalen-13-al + 2 NADP+ + 3 H2O (overall reaction)
(1a) pentalenene + NADPH + H+ + O2 = pentalen-13-ol + NADP+ + H2O
(1b) pentalen-13-ol + NADPH + H+ + O2 = pentalen-13-al + NADP+ + 2 H2O
For diagram of reaction click here.
Other name(s): PtlI
Systematic name: pentalenene,NADPH:oxygen 13-oxidoreductase
Comments: A heme-thiolate protein (P-450). The enzyme is involved in the biosynthesis of pentalenolactone and related antibiotics.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Quaderer, R., Omura, S., Ikeda, H. and Cane, D.E. Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlI, a cytochrome P450 of Streptomyces avermitilis. J. Am. Chem. Soc. 128 (2006) 13036-13037. [PMID: 17017767]
Accepted name: β-amyrin 11-oxidase
Reaction: β-amyrin + 2 O2 + 2 NADPH + 2 H+ = 11-oxo-β-amyrin + 3 H2O + 2 NADP+ (overall reaction)
(1a) β-amyrin + O2 + NADPH + H+ = 11α-hydroxy-β-amyrin + H2O + NADP+
(1b) 11α-hydroxy-β-amyrin + O2 + NADPH + H+ = 11-oxo-β-amyrin + 2 H2O + NADP+
For diagram of reaction click here.
Other name(s): CYP88D6
Systematic name: β-amyrin,NADPH:oxygen oxidoreductase (hydroxylating)
Comments: Requires cytochrome P450. Part of the glycyrrhizin biosynthesis pathway. The enzyme is also able to oxidize 30-hydroxy-β-amyrin to 11α,30-dihydroxy-β-amyrin but this is not thought to be part of glycyrrhizin biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Seki, H., Ohyama, K., Sawai, S., Mizutani, M., Ohnishi, T., Sudo, H., Akashi, T., Aoki, T., Saito, K. and Muranaka, T. Licorice β-amyrin 11-oxidase, a cytochrome P450 with a key role in the biosynthesis of the triterpene sweetener glycyrrhizin. Proc. Natl. Acad. Sci. USA 105 (2008) 14204-14209. [PMID: 18779566]
Accepted name: 1-hydroxy-2-naphthoate hydroxylase
Reaction: 1-hydroxy-2-naphthoate + NAD(P)H + H+ + O2 = 1,2-dihydroxynaphthalene + NAD(P)+ + H2O + CO2
Other name(s): 1-hydroxy-2-naphthoic acid hydroxylase
Systematic name: 1-hydroxy-2-naphthoate,NAD(P)H:oxygen oxidoreductase (2-hydroxylating, decarboxylating)
Comments: The enzyme is involved in the catabolic pathway for the degradation of chrysene in some bacteria [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Deveryshetty, J. and Phale, P.S. Biodegradation of phenanthrene by Alcaligenes sp. strain PPH: partial purification and characterization of 1-hydroxy-2-naphthoic acid hydroxylase. FEMS Microbiol. Lett. 311 (2010) 93-101. [PMID: 20727010]
2. Nayak, A.S., Sanjeev Kumar, S., Santosh Kumar, M., Anjaneya, O. and Karegoudar, T.B. A catabolic pathway for the degradation of chrysene by Pseudoxanthomonas sp. PNK-04. FEMS Microbiol. Lett. 320 (2011) 128-134. [PMID: 21545490]
Accepted name: isoflavonoid synthase
Reaction: liquiritigenin + O2 + NADPH + H+ = 2,7,4'-trihydroxyisoflavanone + H2O + NADP+
For diagram of reaction click here.
Glossary: liquiritigenin = 7,4'-dihydroxyflavanone
Other name(s): CYT93C; IFS; 2-hydroxyisoflavanone synthase (ambiguous)
Systematic name: liquiritigenin,NADPH:oxygen oxidoreductase (hydroxylating, aryl migration)
Comments: Requires cytochrome P450. The reaction involves the migration of the 2-phenyl group of the flavanone liquiritigenin to the 3-position of the isoflavanone. The 2-hydroxyl group is derived from the oxygen molecule.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hashim, M.F., Hakamatsuka, T., Ebizuka, Y. and Sankawa, U. Reaction mechanism of oxidative rearrangement of flavanone in isoflavone biosynthesis. FEBS Lett. 271 (1990) 219-222. [PMID: 2226805]
2. Sawada, Y., Kinoshita, K., Akashi, T., Aoki, T. and Ayabe, S. Key amino acid residues required for aryl migration catalysed by the cytochrome P450 2-hydroxyisoflavanone synthase. Plant J. 31 (2002) 555-564. [PMID: 12207646]
3. Sawada, Y. and Ayabe, S. Multiple mutagenesis of P450 isoflavonoid synthase reveals a key active-site residue. Biochem. Biophys. Res. Commun. 330 (2005) 907-913. [PMID: 15809082]
Accepted name: indole-2-monooxygenase
Reaction: indole + NAD(P)H + H+ + O2 = indolin-2-one + NAD(P)+ + H2O
For diagram of reaction click here.
Other name(s): BX2 (gene name); CYP71C4 (gene name)
Systematic name: indole,NAD(P)H:oxygen oxidoreductase (2-hydroxylating)
Comments: The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poaceae (grasses). It is a member of the cytochrome P450 dependent monooxygenases.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Frey, M., Chomet, P., Glawischnig, E., Stettner, C., Grün, S., Winklmair, A., Eisenreich, W., Bacher, A., Meeley, R.B., Briggs, S.P., Simcox, K. and Gierl, A. Analysis of a chemical plant defense mechanism in grasses. Science 277 (1997) 696-699. [PMID: 9235894]
2. Glawischnig, E., Grun, S., Frey, M. and Gierl, A. Cytochrome P450 monooxygenases of DIBOA biosynthesis: specificity and conservation among grasses. Phytochemistry 50 (1999) 925-930. [PMID: 10385992]
Accepted name: indolin-2-one monooxygenase
Reaction: indolin-2-one + NAD(P)H + H+ + O2 = 3-hydroxyindolin-2-one + NAD(P)+ + H2O
For diagram of reaction click here.
Other name(s): BX3 (gene name); CYP71C2 (gene name)
Systematic name: indolin-2-one,NAD(P)H:oxygen oxidoreductase (3-hydroxylating)
Comments: The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poaceae (grasses). It is a member of the cytochrome P450 dependent monooxygenases.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Frey, M., Chomet, P., Glawischnig, E., Stettner, C., Grün, S., Winklmair, A., Eisenreich, W., Bacher, A., Meeley, R.B., Briggs, S.P., Simcox, K. and Gierl, A. Analysis of a chemical plant defense mechanism in grasses. Science 277 (1997) 696-699. [PMID: 9235894]
2. Glawischnig, E., Grun, S., Frey, M. and Gierl, A. Cytochrome P450 monooxygenases of DIBOA biosynthesis: specificity and conservation among grasses. Phytochemistry 50 (1999) 925-930. [PMID: 10385992]
Accepted name: 3-hydroxyindolin-2-one monooxygenase
Reaction: 3-hydroxyindolin-2-one + NAD(P)H + H+ + O2 = 2-hydroxy-2H-1,4-benzoxazin-3(4H)-one + NAD(P)+ + H2O
For diagram of reaction click here.
Glossary: 2-hydroxy-2H-1,4-benzoxazin-3(4H)-one = HBOA
Other name(s): BX4 (gene name); CYP71C1 (gene name)
Systematic name: 3-hydroxyindolin-2-one,NAD(P)H:oxygen oxidoreductase (2-hydroxy-2H-1,4-benzoxazin-3(4H)-one-forming)
Comments: The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poaceae (grasses). It is a member of the cytochrome P450 dependent monooxygenases.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Glawischnig, E., Grun, S., Frey, M. and Gierl, A. Cytochrome P450 monooxygenases of DIBOA biosynthesis: specificity and conservation among grasses. Phytochemistry 50 (1999) 925-930. [PMID: 10385992]
2. Frey, M., Chomet, P., Glawischnig, E., Stettner, C., Grün, S., Winklmair, A., Eisenreich, W., Bacher, A., Meeley, R.B., Briggs, S.P., Simcox, K. and Gierl, A. Analysis of a chemical plant defense mechanism in grasses. Science 277 (1997) 696-699. [PMID: 9235894]
3. Spiteller, P., Glawischnig, E., Gierl, A. and Steglich, W. Studies on the biosynthesis of 2-hydroxy-1,4-benzoxazin-3-one (HBOA) from 3-hydroxyindolin-2-one in Zea mays. Phytochemistry 57 (2001) 373-376. [PMID: 11393516]
Accepted name: 2-hydroxy-1,4-benzoxazin-3-one monooxygenase
Reaction: 2-hydroxy-2H-1,4-benzoxazin-3(4H)-one + NAD(P)H + H+ + O2 = 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one + NAD(P)+ + H2O
For diagram of reaction click here.
Glossary: 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one = DIBOA
2-hydroxy-2H-1,4-benzoxazin-3(4H)-one = HBOA
Other name(s): BX5 (gene name); CYP71C3 (gene name)
Systematic name: 2-hydroxy-2H-1,4-benzoxazin-3(4H)-one,NAD(P)H:oxygen oxidoreductase (N-hydroxylating)
Comments: The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poaceae (grasses). It is a member of the cytochrome P450 dependent monooxygenases.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Bailey, B.A. and Larson, R.L. Maize microsomal benzoxazinone N-monooxygenase. Plant Physiol. 95 (1991) 792-796. [PMID: 16668055]
2. Glawischnig, E., Grun, S., Frey, M. and Gierl, A. Cytochrome P450 monooxygenases of DIBOA biosynthesis: specificity and conservation among grasses. Phytochemistry 50 (1999) 925-930. [PMID: 10385992]
Accepted name: cholest-4-en-3-one 26-monooxygenase
Reaction: cholest-4-en-3-one + NADH + H+ + O2 = 26-hydroxycholest-4-en-3-one + NAD+ + H2O
Other name(s): CYP125; CYP125A1; cholest-4-en-3-one 27-monooxygenase
Systematic name: cholest-4-en-3-one,NADH:oxygen oxidoreductase (26-hydroxylating)
Comments: This heme thiolate (P450) enzyme, found in several bacterial pathogens, is involved in degradation of the host cholesterol. It catalyses the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate [4]. These activities are required to initiate the degradation of the alkyl side-chain of cholesterol. The enzyme also accepts cholesterol as a substrate, but unlike EC 1.14.13.15, cholestanetriol 26-monooxygenase, this enzyme is specific for C-26 and prefers cholest-4-en-3-one.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Rosloniec, K.Z., Wilbrink, M.H., Capyk, J.K., Mohn, W.W., Ostendorf, M., van der Geize, R., Dijkhuizen, L. and Eltis, L.D. Cytochrome P450 125 (CYP125) catalyses C26-hydroxylation to initiate sterol side-chain degradation in Rhodococcus jostii RHA1. Mol. Microbiol. 74 (2009) 1031-1043. [PMID: 19843222]
2. McLean, K.J., Lafite, P., Levy, C., Cheesman, M.R., Mast, N., Pikuleva, I.A., Leys, D. and Munro, A.W. The Structure of Mycobacterium tuberculosis CYP125: molecular basis for cholesterol binding in a P450 needed for host infection. J. Biol. Chem. 284 (2009) 35524-35533. [PMID: 19846552]
3. Capyk, J.K., Kalscheuer, R., Stewart, G.R., Liu, J., Kwon, H., Zhao, R., Okamoto, S., Jacobs, W.R., Jr., Eltis, L.D. and Mohn, W.W. Mycobacterial cytochrome P450 125 (Cyp125) catalyzes the terminal hydroxylation of C27 steroids. J. Biol. Chem. 284 (2009) 35534-35542. [PMID: 19846551]
4. Ouellet, H., Guan, S., Johnston, J.B., Chow, E.D., Kells, P.M., Burlingame, A.L., Cox, J.S., Podust, L.M. and de Montellano, P.R. Mycobacterium tuberculosis CYP125A1, a steroid C27 monooxygenase that detoxifies intracellularly generated cholest-4-en-3-one. Mol. Microbiol. 77 (2010) 730-742. [PMID: 20545858]
Accepted name: 3-ketosteroid 9α-monooxygenase
Reaction: androsta-1,4-diene-3,17-dione + NADH + H+ + O2 = 9α-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O
Other name(s): KshAB; 3-ketosteroid 9α-hydroxylase
Systematic name: androsta-1,4-diene-3,17-dione,NADH:oxygen oxidoreductase (9α-hydroxylating)
Comments: The enzyme is involved in the cholesterol degradation pathway of several bacterial pathogens, such as Mycobacterium tuberculosis. It is a two-component system consisting of a terminal oxygenase (KshA) and a ferredoxin reductase (KshB). The oxygenase contains a Rieske-type iron-sulfur center and non-heme iron. The reductase component is a flavoprotein containing an NAD-binding domain and a plant-type iron-sulfur cluster. The product of the enzyme is unstable, and spontaneously converts to 3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number:
References:
1. Petrusma, M., Dijkhuizen, L. and van der Geize, R. Rhodococcus rhodochrous DSM 43269 3-ketosteroid 9α-hydroxylase, a two-component iron-sulfur-containing monooxygenase with subtle steroid substrate specificity. Appl. Environ. Microbiol. 75 (2009) 5300-5307. [PMID: 19561185]
2. Capyk, J.K., D'Angelo, I., Strynadka, N.C. and Eltis, L.D. Characterization of 3-ketosteroid 9α-hydroxylase, a Rieske oxygenase in the cholesterol degradation pathway of Mycobacterium tuberculosis. J. Biol. Chem. 284 (2009) 9937-9946. [PMID: 19234303]
3. Capyk, J.K., Casabon, I., Gruninger, R., Strynadka, N.C. and Eltis, L.D. Activity of 3-ketosteroid 9α-hydroxylase (KshAB) indicates cholesterol side chain and ring degradation occur simultaneously in Mycobacterium tuberculosis. J. Biol. Chem. (2011) . [PMID: 21987574]
Accepted name: ent-isokaurene C2-hydroxylase
Reaction: ent-isokaurene + O2 + NADPH + H+ = ent-2α-hydroxyisokaurene + H2O + NADP+
For diagram of reaction click here.
Other name(s): CYP71Z6
Systematic name: ent-isokaurene,NADPH:oxygen oxidoreductase (hydroxylating)
Comments: This is the initial step in the conversion of ent-isokaurene to the antibacterial oryzalides in rice, Oryza sativa.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Wu, Y., Hillwig, M.L., Wang, Q. and Peters, R.J. Parsing a multifunctional biosynthetic gene cluster from rice: biochemical characterization of CYP71Z6 & 7. FEBS Lett. 585 (2011) 3446-3451. [PMID: 21985968]
Accepted name: 9β-pimara-7,15-diene oxidase
Reaction: 9β-pimara-7,15-diene + 3 O2 + 3 NADPH + 3 H+ = 9β-pimara-7,15-dien-19-oate + 3 NADP+ + 4 H2O (overall reaction)
(1a) 9β-pimara-7,15-diene + O2 + NADPH + H+ = 9β-pimara-7,15-dien-19-ol + NADP+ + H2O
(1b) 9β-pimara-7,15-dien-19-ol + O2 + NADPH + H+ = 9β-pimara-7,15-dien-19-al + NADP+ + 2 H2O
(1c) 9β-pimara-7,15-dien-19-al + O2 + NADPH + H+ = 9β-pimara-7,15-dien-19-oate + NADP+ + H2O
For diagram of reaction click here.
Glossary: syn-pimara-7,15-diene = 9β-pimara-7,15-diene
Other name(s): CYP99A3
Systematic name: 9β-pimara-7,15-diene,NADPH:oxygen 19-oxidoreductase
Comments: Requires cytochrome P450. A rice, Oryza sativa, enzyme involved in the phytoalexin momilactone biosynthesis. It also acts similarly on 9β-stemod-13(17)-ene.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Wang, Q., Hillwig, M.L. and Peters, R.J. CYP99A3: functional identification of a diterpene oxidase from the momilactone biosynthetic gene cluster in rice. Plant J. 65 (2011) 87-95. [PMID: 21175892]
Accepted name: ent-cassa-12,15-diene 11-hydroxylase
Reaction: ent-cassa-12,15-diene + O2 + NADPH + H+ = ent-11β-hydroxycassa-12,15-diene + NADP+ + H2O
For diagram of reaction click here.
Other name(s): ent-cassadiene C11α-hydroxylase; CYP76M7
Systematic name: ent-cassa-12,15-diene,NADPH:oxygen 11-oxidoreductase
Comments: Requires cytochrome P450. A rice, Oryza sativa, enzyme involved in the biosynthesis of the antifungal phytocassanes.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Swaminathan, S., Morrone, D., Wang, Q., Fulton, D.B. and Peters, R.J. CYP76M7 is an ent-cassadiene C11α-hydroxylase defining a second multifunctional diterpenoid biosynthetic gene cluster in rice. Plant Cell 21 (2009) 3315-3325. [PMID: 19825834]
Accepted name: taxoid 14β-hydroxylase
Reaction: 10β-hydroxytaxa-4(20),11-dien-5α-yl acetate + O2 + NADPH + H+ = 10β,14β-dihydroxytaxa-4(20),11-dien-5α-yl acetate + NADP+ + H2O
Systematic name: 10β-hydroxytaxa-4(20),11-dien-5α-yl-acetate,NADPH:oxygen 14-oxidoreductase
Comments: Requires cytochrome P450. From the yew Taxus cuspidata. Also acts on taxa-4(20),11-dien-5α-yl acetate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Jennewein, S., Rithner, C.D., Williams, R.M. and Croteau, R. Taxoid metabolism: taxoid 14β-hydroxylase is a cytochrome P450-dependent monooxygenase. Arch. Biochem. Biophys. 413 (2003) 262-270. [PMID: 12729625]
Accepted name: taxoid 7β-hydroxylase
Reaction: taxusin + O2 + NADPH + H+ = 7β-hydroxytaxusin + NADP+ + H2O
Glossary: taxusin = taxa-4(20),11-diene-5α,9α,10β,13α-tetrayl tetraacetate
Systematic name: taxusin,NADPH:oxygen 7-oxidoreductase
Comments: Requires cytochrome P450. From the yew tree Taxus cuspidata. Does not act on earlier intermediates in taxol biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Chau, M., Jennewein, S., Walker, K. and Croteau, R. Taxol biosynthesis: molecular cloning and characterization of a cytochrome P450 taxoid 7 β-hydroxylase. Chem. Biol. 11 (2004) 663-672. [PMID: 15157877]
Accepted name: trimethylamine monooxygenase
Reaction: N,N,N-trimethylamine + NADPH + H+ + O2 = N,N,N-trimethylamine N-oxide + NADP+ + H2O
Other name(s): flavin-containing monooxygenase 3; FMO3; tmm (gene name)
Systematic name: N,N,N-trimethylamine,NADPH:oxygen oxidoreductase (N-oxide-forming)
Comments: A flavoprotein. The bacterial enzyme enables bacteria to use trimethylamine as the sole source of carbon and energy [1,4]. The mammalian enzyme is involved in detoxification of trimethylamine. Mutations in the human enzyme cause the inheritable disease known as trimethylaminuria (fish odor syndrome) [2,3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Large, P.J., Boulton, C.A. and Crabbe, M.J. The reduced nicotinamide-adenine dinucleotide phosphate- and oxygen-dependent N-oxygenation of trimethylamine by Pseudomonas aminovorans. Biochem. J. 128 (1972) 137P-138P. [PMID: 4404764]
2. Dolphin, C.T., Riley, J.H., Smith, R.L., Shephard, E.A. and Phillips, I.R. Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA. Genomics 46 (1997) 260-267. [PMID: 9417913]
3. Treacy, E.P., Akerman, B.R., Chow, L.M., Youil, R., Bibeau, C., Lin, J., Bruce, A.G., Knight, M., Danks, D.M., Cashman, J.R. and Forrest, S.M. Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication. Hum. Mol. Genet. 7 (1998) 839-845. [PMID: 9536088]
4. Chen, Y., Patel, N.A., Crombie, A., Scrivens, J.H. and Murrell, J.C. Bacterial flavin-containing monooxygenase is trimethylamine monooxygenase. Proc. Natl. Acad. Sci. USA 108 (2011) 17791-17796. [PMID: 22006322]
Accepted name: phenylacetyl-CoA 1,2-epoxidase
Reaction: phenylacetyl-CoA + NADPH + H+ + O2 = 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + NADP+ + H2O
For diagram of reaction click here.
Glossary: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA = 2-{7-oxabicyclo[4.1.0]hepta-2,4-dien-1-yl}acetyl-CoA
Other name(s): ring 1,2-phenylacetyl-CoA epoxidase; phenylacetyl-CoA monooxygenase; PaaAC; PaaABC(D)E
Systematic name: phenylacetyl-CoA:oxygen oxidoreductase (1,2-epoxidizing)
Comments: Part of the aerobic pathway of phenylacetate catabolism in Escherichia coli and Pseudomonas putida.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number:
References:
1. Teufel, R., Mascaraque, V., Ismail, W., Voss, M., Perera, J., Eisenreich, W., Haehnel, W. and Fuchs, G. Bacterial phenylalanine and phenylacetate catabolic pathway revealed. Proc. Natl. Acad. Sci. USA 107 (2010) 14390-14395. [PMID: 20660314]
2. Grishin, A.M., Ajamian, E., Zhang, L. and Cygler, M. Crystallization and preliminary X-ray analysis of PaaAC, the main component of the hydroxylase of the Escherichia coli phenylacetyl-coenzyme A oxygenase complex. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66 (2010) 1045-1049. [PMID: 20823522]
3. Grishin, A.M., Ajamian, E., Tao, L., Zhang, L., Menard, R. and Cygler, M. Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex. J. Biol. Chem. 286 (2011) 10735-10743. [PMID: 21247899]
Accepted name: α-humulene 10-hydroxylase
Reaction: α-humulene + O2 + NADPH + H+ = 10-hydroxy-α-humulene + NADP+ + H2O
For diagram of reaction click here.
Other name(s): CYP71BA1
Systematic name: α-humulene,NADPH:oxygen 10-oxidoreductase
Comments: Requires cytochrome P450. The recommended numbering of humulene gives 10-hydroxy-α-humulene as the product rather than 8-hydroxy-α-humulene as used by the reference. See Section F: Natural Product Nomenclature.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yu, F., Okamoto, S., Harada, H., Yamasaki, K., Misawa, N. and Utsumi, R. Zingiber zerumbet CYP71BA1 catalyzes the conversion of α-humulene to 8-hydroxy-α-humulene in zerumbone biosynthesis. Cell. Mol. Life Sci. 68 (2011) 1033-1040. [PMID: 20730551]