Enzyme Nomenclature

Continued from EC 1.14.13.151 to EC 1.14.13.242

EC 1.14.14 to EC 1.14.21

Sections

EC 1.14 Acting on paired donors with incorporation of molecular oxygen


EC 1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [continued]

Continued from:

EC 1.14.14.1 to EC 1.1.1.50
See separate file for EC 1.14.14.101 to EC 1.14.14.171

Contents

EC 1.14.14.51 (S)-limonene 6-monooxygenase
EC 1.14.14.52 (S)-limonene 7-monooxygenase
EC 1.14.14.53 (R)-limonene 6-monooxygenase
EC 1.14.14.54 phenylacetate 2-hydroxylase
EC 1.14.14.55 quinine 3-monooxygenase
EC 1.14.14.56 1,8-cineole 2-exo-monooxygenase
EC 1.14.14.57 taurochenodeoxycholate 6α-hydroxylase
EC 1.14.14.58 trimethyltridecatetraene synthase
EC 1.14.14.59 dimethylnonatriene synthase
EC 1.14.14.60 ferruginol monooxygenase
EC 1.14.14.61 carnosic acid synthase
EC 1.14.14.62 salviol synthase
EC 1.14.14.63 β-amyrin 16β-monooxygenase
EC 1.14.14.64 β-amyrin 6β-monooxygenase
EC 1.14.14.65 sugiol synthase
EC 1.14.14.66 marmesin synthase
EC 1.14.14.67 11-hydroxysugiol 20-monooxygenase
EC 1.14.14.68 syn-pimaradiene 3-monooxygenase
EC 1.14.14.69 ent-cassadiene hydroxylase
EC 1.14.14.70 ent-sandaracopimaradiene 3-hydroxylase
EC 1.14.14.71 cucurbitadienol 11-hydroxylase
EC 1.14.14.72 drimenol monooxygenase
EC 1.14.14.73 albendazole monooxygenase (sulfoxide-forming)
EC 1.14.14.74 albendazole monooxygenase (hydroxylating)
EC 1.14.14.75 fenbendazole monooxygenase (4'-hydroxylating)
EC 1.14.14.76 ent-isokaurene C2/C3-hydroxylase
EC 1.14.14.77 phenylacetonitrile α-monooxygenase
EC 1.14.14.78 phylloquinone ω-hydroxylase
EC 1.14.14.79 docosahexaenoic acid ω-hydroxylase
EC 1.14.14.80 long-chain fatty acid ω-monooxygenase
EC 1.14.14.81 flavanoid 3',5'-hydroxylase
EC 1.14.14.82 flavonoid 3'-monooxygenase
EC 1.14.14.83 geraniol 8-hydroxylase
EC 1.14.14.84 linalool 8-monooxygenase
EC 1.14.14.85 7-deoxyloganin 7-hydroxylase
EC 1.14.14.86 ent-kaurene monooxygenase
EC 1.14.14.87 2-hydroxyisoflavanone synthase
EC 1.14.14.88 isoflavone 3'-hydroxylase
EC 1.14.14.89 4'-methoxyisoflavone 2'-hydroxylase
EC 1.14.14.90 isoflavone 2'-hydroxylase
EC 1.14.14.91 trans-cinnamate 4-monooxygenase
EC 1.14.14.92 benzoate 4-monooxygenase
EC 1.14.14.93 3,9-dihydroxypterocarpan 6a-monooxygenase
EC 1.14.14.94 leukotriene-B4 20-monooxygenase
EC 1.14.14.95 germacrene A hydroxylase
EC 1.14.14.96 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase
EC 1.14.14.97 methyltetrahydroprotoberberine 14-monooxygenase
EC 1.14.14.98 protopine 6-monooxygenase
EC 1.14.14.99 (S)-limonene 3-monooxygenase
EC 1.14.14.100 dihydrosanguinarine 10-monooxygenase
See the following files for:
EC 1.14.14.101 to EC 1.14.14.171

EC 1.14.14.51

Accepted name: (S)-limonene 6-monooxygenase

Reaction: (S)-limonene + [reduced NADPH —hemoprotein reductase] + O2 = (–)-trans-carveol + [oxidized NADPH —hemoprotein reductase] + H2O

For diagram of reaction click here

Glossary: limonene = a monoterpenoid
(S)-limonene = (–)-limonene

Other name(s): (–)-limonene 6-hydroxylase; (–)-limonene 6-monooxygenase; (–)-limonene,NADPH:oxygen oxidoreductase (6-hydroxylating)

Systematic name: (S)-limonene,[reduced NADPH —hemoprotein reductase]:oxygen oxidoreductase (6-hydroxylating)

Comments: A cytochrome P-450 (heme thiolate) enzyme. The enzyme participates in the biosynthesis of (–)-carvone, which is responsible for the aroma of spearmint.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Karp, F., Mihaliak, C.A., Harris, J.L. and Croteau, R. Monoterpene biosynthesis: specificity of the hydroxylations of (–)-limonene by enzyme preparations from peppermint (Mentha piperita), spearmint (Mentha spicata), and perilla (Perilla frutescens) leaves. Arch. Biochem. Biophys. 276 (1990) 219-226. [PMID: 2297225]

[EC 1.14.14.51 created 1992 as EC 1.14.13.48, modified 2003, transferred 2017 to EC 1.14.14.51]

EC 1.14.14.52

Accepted name: (S)-limonene 7-monooxygenase

Reaction: (S)-limonene + [reduced NADPH —hemoprotein reductase] + O2 = (–)-perillyl alcohol + [oxidized NADPH —hemoprotein reductase] + H2O

For diagram of reaction click here

Glossary: limonene = a monoterpenoid
(S)-limonene = (–)-limonene

Other name(s): (–)-limonene 7-monooxygenase; (–)-limonene hydroxylase; (–)-limonene monooxygenase; (–)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating)

Systematic name: (S)-limonene,[reduced NADPH —hemoprotein reductase]:oxygen oxidoreductase (7-hydroxylating)

Comments: A cytochrome P-450 (heme thiolate) enzyme. The enzyme, characterized from the plant Perilla frutescens, participates in the biosynthesis of perillyl aldehyde, the major constituent of the essential oil that accumulates in the glandular trichomes of this plant. Some forms of the enzyme also catalyse the oxidation of (–)-perillyl alcohol to (–)-perillyl aldehyde.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Karp, F., Mihaliak, C.A., Harris, J.L. and Croteau, R. Monoterpene biosynthesis: specificity of the hydroxylations of (–)-limonene by enzyme preparations from peppermint (Mentha piperita), spearmint (Mentha spicata), and perilla (Perilla frutescens) leaves. Arch. Biochem. Biophys. 276 (1990) 219-226. [PMID: 2297225]

2. Mau, C.J., Karp, F., Ito, M., Honda, G. and Croteau, R.B. A candidate cDNA clone for (–)-limonene-7-hydroxylase from Perilla frutescens. Phytochemistry 71 (2010) 373-379. [PMID: 20079506]

3. Fujiwara, Y. and Ito, M. Molecular cloning and characterization of a Perilla frutescens cytochrome P450 enzyme that catalyzes the later steps of perillaldehyde biosynthesis. Phytochemistry 134 (2017) 26-37. [PMID: 27890582]

[EC 1.14.14.52 created 1992 as EC 1.14.13.49, modified 2003, transferred 2017 to EC 1.14.14.52]

EC 1.14.14.53

Accepted name: (R)-limonene 6-monooxygenase

Reaction: (R)-limonene + [reduced NADPH —hemoprotein reductase] + O2 = (+)-trans-carveol + [oxidized NADPH —hemoprotein reductase] + H2O

For diagram of reaction click here

Glossary: limonene = a monoterpenoid
(R)-limonene = (+)-limonene

Other name(s): (+)-limonene-6-hydroxylase; (+)-limonene 6-monooxygenase

Systematic name: (R)-limonene,[reduced NADPH —hemoprotein reductase]:oxygen oxidoreductase (6-hydroxylating)

Comments: The reaction is stereospecific with over 95% yield of (+)-trans-carveol from (R)-limonene. (S)-Limonene, the substrate for EC 1.14.14.51, (S)-limonene 6-monooxygenase, is not a substrate. Forms part of the carvone biosynthesis pathway in Carum carvi (caraway) seeds.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Bouwmeester, H.J., Gershenzon, J., Konings, M.C.J.M. and Croteau, R. Biosynthesis of the monoterpenes limonene and carvone in the fruit of caraway. I. Demonstration of enzyme activities and their changes with development. Plant Physiol. 117 (1998) 901-912. [PMID: 9662532]

2. Bouwmeester, H.J., Konings, M.C.J.M., Gershenzon, J., Karp, F. and Croteau, R. Cytochrome P-450 dependent (+)-limonene-6-hydroxylation in fruits of caraway (Carum carvi). Phytochemistry 50 (1999) 243-248.

[EC 1.14.14.53 created 2003 as EC 1.14.13.80, transferred 2017 to EC 1.14.14.53]

EC 1.14.14.54

Accepted name: phenylacetate 2-hydroxylase

Reaction: phenylacetate + [reduced NADPH —hemoprotein reductase] + O2 = (2-hydroxyphenyl)acetate + [oxidized NADPH —hemoprotein reductase] + H2O

Other name(s): CYP504; phaA (gene name)

Systematic name: phenylacetate,[reduced NADPH —hemoprotein reductase]:oxygen oxidoreductase (2-hydroxylating)

Comments: This cytochrome P-450 (heme-thiolate) enzyme, found in Aspergillus nidulans, is involved in the degradation of phenylacetate.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Mingot, J.M., Penalva, M.A. and Fernandez-Canon, J.M. Disruption of phacA, an Aspergillus nidulans gene encoding a novel cytochrome P450 monooxygenase catalyzing phenylacetate 2-hydroxylation, results in penicillin overproduction. J. Biol. Chem. 274 (1999) 14545-14550. [PMID: 10329644]

2. Rodriguez-Saiz, M., Barredo, J.L., Moreno, M.A., Fernandez-Canon, J.M., Penalva, M.A. and Diez, B. Reduced function of a phenylacetate-oxidizing cytochrome P450 caused strong genetic improvement in early phylogeny of penicillin-producing strains. J. Bacteriol. 183 (2001) 5465-5471. [PMID: 11544206]

[EC 1.14.14.54 created 2017]

EC 1.14.14.55

Accepted name: quinine 3-monooxygenase

Reaction: quinine + [reduced NADPH—hemoprotein reductase] + O2 = 3-hydroxyquinine + [oxidized NADPH—hemoprotein reductase] + H2O

Glossary: quinine = a quinoline alkaloid

Other name(s): CYP3A4 (gene name)

Systematic name: quinine,[reduced NADPH–hemoprotein reductase]:oxygen oxidoreductase

Comments: A cytochrome P-450 (heme-thiolate) protein.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Relling, M.V., Evans, R., Dass, C., Desiderio, D.M. and Nemec, J. Human cytochrome P450 metabolism of teniposide and etoposide. J. Pharmacol. Exp. Ther. 261 (1992) 491-496. [PMID: 1578365]

2. Zhang, H., Coville, P.F., Walker, R.J., Miners, J.O., Birkett, D.J. and Wanwimolruk, S. Evidence for involvement of human CYP3A in the 3-hydroxylation of quinine. Br. J. Clin. Pharmacol. 43 (1997) 245-252. [PMID: 9088578]

3. Zhao, X.-J., Kawashiro, T. and Ishizaki, T. Mutual inhibition between quinine and etoposide by human liver microsomes. Evidence for cytochrome P4503A4 involvement in their major metabolic pathways. Drug Metab. Dispos. 26 (1998) 188-191. [PMID: 9456308]

4. Zhao, X.-J., Yokoyama, H., Chiba, K., Wanwimolruk, S. and Ishizaki, T. Identification of human cytochrome P450 isoforms involved in the 3-hydroxylation of quinine by human liver microsomes and nine recombinant human cytochromes P450. J. Pharmacol. Exp. Ther. 279 (1996) 1327-1334. [PMID: 8968357]

[EC 1.14.14.55 created 2000 as EC 1.14.13.67, transferred 2017 to EC 1.14.14.55]

EC 1.14.14.56

Accepted name: 1,8-cineole 2-exo-monooxygenase

Reaction: 1,8-cineole + [reduced NADPH—hemoprotein reductase] + O2 = 2-exo-hydroxy-1,8-cineole + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Glossary: 1,8-cineole = 1,3,3-trimethyl-2-oxabicyclo[2.2.2]octane
2-exo-hydroxy-1,8-cineole = (1R,4S,6S)-1,3,3-trimethyl-2-oxabicyclo[2.2.2]octan-6-ol

Other name(s): CYP3A4

Systematic name: 1,8-cineole,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2-exo-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein. The mammalian enzyme, expressed in liver microsomes, performs a variety of oxidation reactions of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. cf. EC 1.14.14.55, quinine 3-monooxygenase, EC 1.14.14.57, taurochenodeoxycholate 6-hydroxylase and EC 1.14.14.73, albendazole monooxygenase (sulfoxide-forming).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Miyazawa, M., Shindo, M. and Shimada, T. Oxidation of 1,8-cineole, the monoterpene cyclic ether originated from Eucalyptus polybractea, by cytochrome P450 3A enzymes in rat and human liver microsomes. Drug Metab. Dispos. 29 (2001) 200-205. [PMID: 11159812]

2. Miyazawa, M. and Shindo, M. Biotransformation of 1,8-cineole by human liver microsomes. Nat. Prod. Lett. 15 (2001) 49-53. [PMID: 11547423]

3. Miyazawa, M., Shindo, M. and Shimada, T. Roles of cytochrome P450 3A enzymes in the 2-hydroxylation of 1,4-cineole, a monoterpene cyclic ether, by rat and human liver microsomes. Xenobiotica 31 (2001) 713-723. [PMID: 11695850]

[EC 1.14.14.56 created 2012 as EC 1.14.13.157, transferred 2017 to EC 1.14.14.56, modified 2018]

EC 1.14.14.57

Accepted name: taurochenodeoxycholate 6α-hydroxylase

Reaction: (1) taurochenodeoxycholate + [reduced NADPH—hemoprotein reductase] + O2 = taurohyocholate + [oxidized NADPH—hemoprotein reductase] + H2O
(2) lithocholate + [reduced NADPH—hemoprotein reductase] + O2 = hyodeoxycholate + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Glossary: taurochenodeoxycholic acid = N-(3α,7α-dihydroxy-5β-cholan-24-oyl)taurine
taurohyocholic acid = N-(3α,6α,7α-trihydroxy-5β-cholan-24-oyl)taurine
hyodeoxycholate = 3α,6α-dihydroxy-5β-cholan-24-oate
lithocholate = 3α-hydroxy-5β-cholan-24-oate

Other name(s): CYP3A4; CYP4A21; taurochenodeoxycholate 6α-monooxygenase

Systematic name: taurochenodeoxycholate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6α-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein. Requires cytochrome b5 for maximal activity. Acts on taurochenodeoxycholate, taurodeoxycholate and less readily on lithocholate and chenodeoxycholate. In adult pig (Sus scrofa), hyocholic acid replaces cholic acid as a primary bile acid [5].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Araya, Z. and Wikvall, K. 6α-Hydroxylation of taurochenodeoxycholic acid and lithocholic acid by CYP3A4 in human liver microsomes. Biochim. Biophys. Acta 1438 (1999) 47-54. [PMID: 10216279]

2. Araya, Z., Hellman, U. and Hansson, R. Characterisation of taurochenodeoxycholic acid 6α-hydroxylase from pig liver microsomes. Eur. J. Biochem. 231 (1995) 855-861. [PMID: 7649186]

3. Kramer, W., Sauber, K., Baringhaus, K.H., Kurz, M., Stengelin, S., Lange, G., Corsiero, D., Girbig, F., Konig, W. and Weyland, C. Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure. J. Biol. Chem. 276 (2001) 7291-7301. [PMID: 11069906]

4. Lundell, K., Hansson, R. and Wikvall, K. Cloning and expression of a pig liver taurochenodeoxycholic acid 6α-hydroxylase (CYP4A21): a novel member of the CYP4A subfamily. J. Biol. Chem. 276 (2001) 9606-9612. [PMID: 11113117]

5. Lundell, K. and Wikvall, K. Gene structure of pig sterol 12α-hydroxylase (CYP8B1) and expression in fetal liver: comparison with expression of taurochenodeoxycholic acid 6α-hydroxylase (CYP4A21). Biochim. Biophys. Acta 1634 (2003) 86-96. [PMID: 14643796]

6. Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137-174. [PMID: 12543708]

[EC 1.14.14.57 created 2005 asEC 1.14.13.97, transferred 2018 to EC 1.14.14.57]

EC 1.14.14.58

Accepted name: trimethyltridecatetraene synthase

Reaction: (6E,10E)-geranyllinalool + [reduced NADPH—hemoprotein reductase] + O2 = (3E,7E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + [oxidized NADPH—hemoprotein reductase] + but-3-en-2-one + 2 H2O

For diagram of reaction click here.

Glossary: (6E,10E)-geranyllinalool = (6E,10E)-3,7,11,15-tetramethylhexadeca-1,6,10,14-tetraen-3-ol

Other name(s): CYP82G1; CYP92C5; CYP92C6; DMNT/TMTT homoterpene synthase

Systematic name: (6E,10E)-geranyllinalool,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase

Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plants Arabidopsis thaliana (thale cress) and Zea mays (maize). It forms this C16 homoterpene in response to herbivore attack. In vitro some variants of the enzyme also convert (3S,6E)-nerolidol to (3E)-4,8-dimethylnona-1,3,7-triene (see EC 1.14.14.59, dimethylnonatriene synthase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Lee, S., Badieyan, S., Bevan, D.R., Herde, M., Gatz, C. and Tholl, D. Herbivore-induced and floral homoterpene volatiles are biosynthesized by a single P450 enzyme (CYP82G1) in Arabidopsis. Proc. Natl Acad. Sci. USA 107 (2010) 21205-21210. [PMID: 21088219]

2. Richter, A., Schaff, C., Zhang, Z., Lipka, A.E., Tian, F., Kollner, T.G., Schnee, C., Preiss, S., Irmisch, S., Jander, G., Boland, W., Gershenzon, J., Buckler, E.S. and Degenhardt, J. Characterization of biosynthetic pathways for the production of the volatile homoterpenes DMNT and TMTT in Zea mays. Plant Cell 28 (2016) 2651-2665. [PMID: 27662898]

[EC 1.14.14.58 created 2018]

EC 1.14.14.59

Accepted name: dimethylnonatriene synthase

Reaction: (3S,6E)-nerolidol + [reduced NADPH—hemoprotein reductase] + O2 = (3E)-4,8-dimethylnona-1,3,7-triene + [oxidized NADPH—hemoprotein reductase] + but-3-en-2-one + 2 H2O

For diagram of reaction click here.

Other name(s): CYP82G1; CYP92C5; DMNT/TMTT homoterpene synthase

Systematic name: (3S,6E)-nerolidol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase

Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plants Arabidopsis thaliana (thale cress) and Zea mays (maize). It forms this C11 homoterpene in response to herbivore attack. In vitro the enzyme also converts (6E,10E)-geranyllinalool to (3E,7E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene (see EC 1.14.14.58, trimethyltridecatetraene synthase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Lee, S., Badieyan, S., Bevan, D.R., Herde, M., Gatz, C. and Tholl, D. Herbivore-induced and floral homoterpene volatiles are biosynthesized by a single P450 enzyme (CYP82G1) in Arabidopsis. Proc. Natl Acad. Sci. USA 107 (2010) 21205-21210. [PMID: 21088219]

2. Richter, A., Schaff, C., Zhang, Z., Lipka, A.E., Tian, F., Kollner, T.G., Schnee, C., Preiss, S., Irmisch, S., Jander, G., Boland, W., Gershenzon, J., Buckler, E.S. and Degenhardt, J. Characterization of biosynthetic pathways for the production of the volatile homoterpenes DMNT and TMTT in Zea mays. Plant Cell 28 (2016) 2651-2665. [PMID: 27662898]

[EC 1.14.14.59 created 2018]

EC 1.14.14.60

Accepted name: ferruginol monooxygenase

Reaction: ferruginol + [reduced NADPH—hemoprotein reductase] + O2 = 11-hydroxyferruginol + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Glossary: ferruginol = abieta-8,11,13-trien-12-ol

Other name(s): CYP76AH24; CYP76AH3

Systematic name: ferruginol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (11-hydroxyferruginol forming)

Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plants Salvia pomifera (apple sage) and Salvia miltiorrhiza (danshen). 11-Hydroxyferruginol is a precursor of carnosic acid, a potent antioxidant.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Ignea, C., Athanasakoglou, A., Ioannou, E., Georgantea, P., Trikka, F.A., Loupassaki, S., Roussis, V., Makris, A.M. and Kampranis, S.C. Carnosic acid biosynthesis elucidated by a synthetic biology platform. Proc. Natl Acad. Sci. USA 113 (2016) 3681-3686. [PMID: 26976595]

2. Scheler, U., Brandt, W., Porzel, A., Rothe, K., Manzano, D., Bozic, D., Papaefthimiou, D., Balcke, G.U., Henning, A., Lohse, S., Marillonnet, S., Kanellis, A.K., Ferrer, A. and Tissier, A. Elucidation of the biosynthesis of carnosic acid and its reconstitution in yeast. Nat Commun 7 (2016) 12942. [PMID: 27703160]

3. Guo, J., Ma, X., Cai, Y., Ma, Y., Zhan, Z., Zhou, Y.J., Liu, W., Guan, M., Yang, J., Cui, G., Kang, L., Yang, L., Shen, Y., Tang, J., Lin, H., Ma, X., Jin, B., Liu, Z., Peters, R.J., Zhao, Z.K. and Huang, L. Cytochrome P450 promiscuity leads to a bifurcating biosynthetic pathway for tanshinones. New Phytol. 210 (2016) 525-534. [PMID: 26682704]

[EC 1.14.14.60 created 2018]

EC 1.14.14.61

Accepted name: carnosic acid synthase

Reaction: 11-hydroxyferruginol + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = carnosic acid + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O

For diagram of reaction click here.

Glossary: carnosic acid = 11,12-dihydroxyabieta-8,11,13-trien-20-oic acid

Other name(s): CYP76AK6; CYP76AK7; CYP76AK8

Systematic name: 11-hydroxyferruginol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase

Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plants Salvia pomifera (apple sage), S. miltiorrhiza (red sage), S. fruticosa (Greek sage) and Rosmarinus officinalis (Rosemary).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Ignea, C., Athanasakoglou, A., Ioannou, E., Georgantea, P., Trikka, F.A., Loupassaki, S., Roussis, V., Makris, A.M. and Kampranis, S.C. Carnosic acid biosynthesis elucidated by a synthetic biology platform. Proc. Natl Acad. Sci. USA 113 (2016) 3681-3686. [PMID: 26976595]

2. Scheler, U., Brandt, W., Porzel, A., Rothe, K., Manzano, D., Bozic, D., Papaefthimiou, D., Balcke, G.U., Henning, A., Lohse, S., Marillonnet, S., Kanellis, A.K., Ferrer, A. and Tissier, A. Elucidation of the biosynthesis of carnosic acid and its reconstitution in yeast. Nat Commun 7 (2016) 12942. [PMID: 27703160]

[EC 1.14.14.61 created 2018]

EC 1.14.14.62

Accepted name: salviol synthase

Reaction: ferruginol + [reduced NADPH—hemoprotein reductase] + O2 = salviol + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Glossary: salviol = abieta-8,11,13-triene-2α,12-diol

Other name(s): CYP71BE52

Systematic name: ferruginol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (salviol forming)

Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Salvia pomifera (apple sage).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Ignea, C., Athanasakoglou, A., Ioannou, E., Georgantea, P., Trikka, F.A., Loupassaki, S., Roussis, V., Makris, A.M. and Kampranis, S.C. Carnosic acid biosynthesis elucidated by a synthetic biology platform. Proc. Natl Acad. Sci. USA 113 (2016) 3681-3686. [PMID: 26976595]

[EC 1.14.14.62 created 2018]

EC 1.14.14.63

Accepted name: β-amyrin 16β-monooxygenase

Reaction: β-amyrin + [reduced NADPH—hemoprotein reductase] + O2 = maniladiol + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Glossary: cochalic acid = 3β,16β-dihydroxyolean-12-en-28-oic acid
maniladiol = 16β-hydroxy-β-amyrin = olean-12-ene-3β,16β-diol

Other name(s): CYP716A141

Systematic name: β-amyrin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (maniladiol forming)

Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Platycodon grandiflorus (baloon flower). The enzyme is also able to oxidize oleanolic acid to cochalic acid.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Tamura, K., Teranishi, Y., Ueda, S., Suzuki, H., Kawano, N., Yoshimatsu, K., Saito, K., Kawahara, N., Muranaka, T. and Seki, H. Cytochrome P450 monooxygenase CYP716A141 is a unique β-amyrin C-16β oxidase Involved in triterpenoid saponin biosynthesis in Platycodon grandiflorus. Plant Cell Physiol 58 (2017) 874-884. [PMID: 28371833]

[EC 1.14.14.63 created 2018]

EC 1.14.14.64

Accepted name: β-amyrin 6β-monooxygenase

Reaction: β-amyrin + [reduced NADPH—hemoprotein reductase] + O2 = daturadiol + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Glossary: daturadiol = 6β-hydroxy-β-amyrin = olean-12-ene-3β,6β-diol

Other name(s): CYP716E26

Systematic name: β-amyrin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (daturadiol forming)

Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Solanum lycopersicum (tomato).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Yasumoto, S., Seki, H., Shimizu, Y., Fukushima, E.O. and Muranaka, T. Functional characterization of CYP716 family P450 enzymes in triterpenoid biosynthesis in tomato. Front. Plant Sci. 8 (2017) 21. [PMID: 28194155]

[EC 1.14.14.64 created 2018]

EC 1.14.14.65

Accepted name: sugiol synthase

Reaction: ferruginol + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = sugiol + 2 [oxidized NADPH—hemoprotein reductase] + 3 H2O

For diagram of reaction click here.

Glossary: ferruginol = abieta-8,11,13-trien-12-ol
sugiol = 12-hydroxyabieta-8,11,13-trien-7-one

Other name(s): CYP76AH3

Systematic name: ferruginol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (sugiol forming)

Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Salvia miltiorrhiza (danshen). The enzyme also oxidizes 11-hydroxyferruginol to 11-hydroxysugiol. It also oxidizes at C-12 of ferruginol (EC 1.14.14.60 ferruginol monooxygenase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Guo, J., Ma, X., Cai, Y., Ma, Y., Zhan, Z., Zhou, Y.J., Liu, W., Guan, M., Yang, J., Cui, G., Kang, L., Yang, L., Shen, Y., Tang, J., Lin, H., Ma, X., Jin, B., Liu, Z., Peters, R.J., Zhao, Z.K. and Huang, L. Cytochrome P450 promiscuity leads to a bifurcating biosynthetic pathway for tanshinones. New Phytol. 210 (2016) 525-534. [PMID: 26682704]

[EC 1.14.14.65 created 2018]

EC 1.14.14.66

Accepted name: marmesin synthase

Reaction: demethylsuberosin + [reduced NADPH—hemoprotein reductase] + O2 = (+)-marmesin + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Glossary: demethylsuberosin = 7-hydroxy-6-prenyl-1-benzopyran-2-one
(+)-marmesin = (S)-2-(2-hydroxypropan-2-yl)-2,3-dihydro-7H-furo[3,2-g]chromen-7-one

Systematic name: demethylsuberosin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase

Comments: A P-450 monoxygenase involved in psoralen biosynthesis, see EC 1.14.13.102, psoralen synthase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Hamerski, D. and Matern, U. Elicitor-induced biosynthesis of psoralens in Ammi majus L. suspension cultures. Microsomal conversion of demethylsuberosin into (+)marmesin and psoralen. Eur. J. Biochem. 171 (1988) 369-375. [PMID: 2828055]

[EC 1.14.14.66 created 2018]

EC 1.14.14.67

Accepted name: 11-hydroxysugiol 20-monooxygenase

Reaction: 11-hydroxysugiol + [reduced NADPH—hemoprotein reductase] + O2 = 11,20-dihydroxysugiol + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Glossary: ferruginol = abieta-8,11,13-trien-12-ol
sugiol = 12-hydroxyabieta-8,11,13-trien-7-one

Other name(s): CYP76AK1

Systematic name: 11-hydroxysugiol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (11,20-dihydroxysugiol forming)

Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Salvia miltiorrhiza (danshen). The enzyme also oxidizes 11-hydroxyferruginol to 11,20-dihydroxyferruginol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Guo, J., Ma, X., Cai, Y., Ma, Y., Zhan, Z., Zhou, Y.J., Liu, W., Guan, M., Yang, J., Cui, G., Kang, L., Yang, L., Shen, Y., Tang, J., Lin, H., Ma, X., Jin, B., Liu, Z., Peters, R.J., Zhao, Z.K. and Huang, L. Cytochrome P450 promiscuity leads to a bifurcating biosynthetic pathway for tanshinones. New Phytol. 210 (2016) 525-534. [PMID: 26682704]

[EC 1.14.14.67 created 2018]

EC 1.14.14.68

Accepted name: syn-pimaradiene 3-monooxygenase

Reaction: 9β-pimara-7,15-diene + [reduced NADPH—hemoprotein reductase] + O2 = 9β-pimara-7,15-diene-3β-ol + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Glossary: syn-pimara-7,15-diene = 9β-pimara-7,15-diene

Other name(s): CYP701A8

Systematic name: 9β-pimara7,15-diene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (9β-pimara-7,15-diene-3β-ol forming)

Comments: A cytochrome P-450 (heme-thiolate) protein isolated from rice, Oryza sativa.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kitaoka, N., Wu, Y., Xu, M. and Peters, R.J. Optimization of recombinant expression enables discovery of novel cytochrome P450 activity in rice diterpenoid biosynthesis. Appl. Microbiol. Biotechnol. 99 (2015) 7549-7558. [PMID: 25758958]

[EC 1.14.14.68 created 2018]

EC 1.14.14.69

Accepted name: ent-cassadiene hydroxylase

Reaction: ent-cassa-12,15-diene + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = ent-3β-hydroxycassa-12,15-dien-2-one + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) ent-cassa-12,15-diene + [reduced NADPH—hemoprotein reductase] + O2 = ent-cassa-12,15-dien-2β-ol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) ent-cassa-12,15-dien-2β-ol + [reduced NADPH—hemoprotein reductase] + O2 = ent-cassa-12,15-dien-2-one + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1b′) ent-cassa-12,15-dien-2β-ol + [reduced NADPH—hemoprotein reductase] + O2 = ent-cassa-12,15-diene-2β,3β-diol + [oxidized NADPH—hemoprotein reductase] + H2O
(1c) ent-cassa-12,15-dien-2-one + [reduced NADPH—hemoprotein reductase] + O2 = ent-3β-hydroxycassa-12,15-dien-2-one + [oxidized NADPH—hemoprotein reductase] + H2O
(1c′) ent-cassa-12,15-diene-2β,3β-diol + [reduced NADPH—hemoprotein reductase] + O2 = ent-3β-hydroxycassa-12,15-dien-2-one + [oxidized NADPH—hemoprotein reductase] + 2 H2O

For diagram of reaction click here.

Other name(s): CYP71Z7

Systematic name: ent-cassa-12,15-diene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ent-3β-hydroxycassa-12,15-dien-2-one forming)

Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Oryza sativa (rice) that is involved in phytocassanes biosynthesis. Depending on the order of activities, the enzyme may form either ent-cassa-12,15-dien-2-one or ent-cassa-12,15-diene-2β,3β-diol as an intermediate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kitaoka, N., Wu, Y., Xu, M. and Peters, R.J. Optimization of recombinant expression enables discovery of novel cytochrome P450 activity in rice diterpenoid biosynthesis. Appl. Microbiol. Biotechnol. 99 (2015) 7549-7558. [PMID: 25758958]

[EC 1.14.14.69 created 2018]

EC 1.14.14.70

Accepted name: ent-sandaracopimaradiene 3-hydroxylase

Reaction: ent-sandaracopimaradiene + [reduced NADPH—hemoprotein reductase] + O2 = ent-sandaracopimaradien-3β-ol + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Glossary: ent-sandaracopimaradiene = ent-13α-pimara-8(14),15-diene = (4aR,4bR,7S,10aR)-7-ethenyl-1,1,4a,7-tetramethyl-1,2,3,4,4a,4b,5,6,7,9,10,10a-dodecahydrophenanthrene

Other name(s): CYP701A; OsKOL4

Systematic name: ent-sandaracopimaradiene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ent-sandaracopimaradien-3β-ol forming)

Comments: A cytochrome P-450 (heme-thiolate) protein isolated from Oryza sativa (rice). Participates in the pathway for the biosynthesis of oryzalexins, a group of related phytoalexins produced by rice. Can also use 9β-pimara-7,15-diene as substrate (cf. EC 1.14.14.68, syn-pimaradiene 3-monooxygenase).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Wang, Q., Hillwig, M.L., Wu, Y. and Peters, R.J. CYP701A8: a rice ent-kaurene oxidase paralog diverted to more specialized diterpenoid metabolism. Plant Physiol. 158 (2012) 1418-1425. [PMID: 22247270]

2. Wu, Y., Wang, Q., Hillwig, M.L. and Peters, R.J. Picking sides: distinct roles for CYP76M6 and CYP76M8 in rice oryzalexin biosynthesis. Biochem. J. 454 (2013) 209-216. [PMID: 23795884]

[EC 1.14.14.70 created 2014 as EC 1.14.13.191, transferred 2018 to EC 1.14.14.70]

EC 1.14.14.71

Accepted name: cucurbitadienol 11-hydroxylase

Reaction: cucurbitadienol + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = 11-oxocucurbitadienol + 2 [oxidized NADPH—hemoprotein reductase] + 3 H2O (overall reaction) (26 April 2018)
(1a) cucurbitadienol + [reduced NADPH—hemoprotein reductase] + O2 = 11-hydroxycucurbitadienol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 11-hydroxycucurbitadienol + [reduced NADPH—hemoprotein reductase] + O2 = 11-oxocucurbitadienol + [oxidized NADPH—hemoprotein reductase] + 2 H2O

For diagram of reaction click here.

Glossary: 11-oxocucurbitadienol = 3β-hydroxycucurbita-7,24-dien-11-one

Other name(s): CYP87D18

Systematic name: cucurbitadienol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (11-oxocucurbitadienol forming)

Comments: Isolated from the plant Siraitia grosvenorii (monk fruit).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Zhang, J., Dai, L., Yang, J., Liu, C., Men, Y., Zeng, Y., Cai, Y., Zhu, Y. and Sun, Y. Oxidation of cucurbitadienol catalyzed by CYP87D18 in the biosynthesis of mogrosides from Siraitia grosvenorii. Plant Cell Physiol 57 (2016) 1000-1007. [PMID: 26903528]

[EC 1.14.14.71 created 2018]

EC 1.14.14.72

Accepted name: drimenol monooxygenase

Reaction: drimenol + [reduced NADPH—hemoprotein reductase] + O2 = drimendiol + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Glossary: drimendiol = drim-7-ene-11,12-diol

Other name(s): PhDOX1

Systematic name: drimenol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (drimendiol forming)

Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Persicaria hydropiper (water pepper).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Henquet, M.GL., Prota, N., van der Hooft, J.JJ., Varbanova-Herde, M., Hulzink, R.JM., de Vos, M., Prins, M., de Both, M.TJ., Franssen, M.CR., Bouwmeester, H. and Jongsma, M. Identification of a drimenol synthase and drimenol oxidase from Persicaria hydropiper, involved in the biosynthesis of insect deterrent drimanes. Plant J. 90 (2017) 1052-1063. [PMID: 28258968]

[EC 1.14.14.72 created 2018]

EC 1.14.14.73

Accepted name: albendazole monooxygenase (sulfoxide-forming)

Reaction: (1) albendazole + [reduced NADPH—hemoprotein reductase] + O2 = albendazole S-oxide + [oxidized NADPH—hemoprotein reductase] + H2O
(2) fenbendazole + [reduced NADPH—hemoprotein reductase] + O2 = fenbendazole S-oxide + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Glossary: albendazole = methyl [5-(propylsulfanyl)-1H-benzimidazol-2-yl]carbamate
fenbendazole = methyl [5-(phenylsulfanyl)-1H-benzimidazol-2-yl]carbamate

Other name(s): albendazole sulfoxidase (ambiguous); albendazole hydroxylase (ambiguous); CYP3A4 (gene name); CYP2J2 (gene name); CYP1A2 (gene name)

Systematic name: albendazole,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (sulfoxide-forming)

Comments: This is one of the activities carried out by some microsomal cytochrome P-450 monooxygenases. A similar conversion is also carried out by a different microsomal enzyme (EC 1.14.13.32, albendazole monooxygenase (flavin-containing)), but it is estimated that cytochrome P-450s are responsible for 70% of the activity.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Moroni, P., Buronfosse, T., Longin-Sauvageon, C., Delatour, P. and Benoit, E. Chiral sulfoxidation of albendazole by the flavin adenine dinucleotide-containing and cytochrome P450-dependent monooxygenases from rat liver microsomes. Drug Metab. Dispos. 23 (1995) 160-165. [PMID: 7736906]

2. Rawden, H.C., Kokwaro, G.O., Ward, S.A. and Edwards, G. Relative contribution of cytochromes P-450 and flavin-containing monoxygenases to the metabolism of albendazole by human liver microsomes. Br. J. Clin. Pharmacol. 49 (2000) 313-322. [PMID: 10759686]

3. Asteinza, J., Camacho-Carranza, R., Reyes-Reyes, R.E., Dorado-Gonzalez, V., V. and Espinosa-Aguirre, J.J. Induction of cytochrome P450 enzymes by albendazole treatment in the rat. Environ Toxicol Pharmacol 9 (2000) 31-37. [PMID: 11137466]

4. Lee, C.A., Neul, D., Clouser-Roche, A., Dalvie, D., Wester, M.R., Jiang, Y., Jones, J.P., 3rd, Freiwald, S., Zientek, M. and Totah, R.A. Identification of novel substrates for human cytochrome P450 2J2. Drug Metab. Dispos. 38 (2010) 347-356. [PMID: 19923256]

5. Wu, Z., Lee, D., Joo, J., Shin, J.H., Kang, W., Oh, S., Lee, D.Y., Lee, S.J., Yea, S.S., Lee, H.S., Lee, T. and Liu, K.H. CYP2J2 and CYP2C19 are the major enzymes responsible for metabolism of albendazole and fenbendazole in human liver microsomes and recombinant P450 assay systems. Antimicrob. Agents Chemother. 57 (2013) 5448-5456. [PMID: 23959307]

[EC 1.14.14.73 created 2018]

EC 1.14.14.74

Accepted name: albendazole monooxygenase (hydroxylating)

Reaction: albendazole + [reduced NADPH—hemoprotein reductase] + O2 = hydroxyalbendazole + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Glossary: albendazole = methyl [5-(propylsulfanyl)-1H-benzimidazol-2-yl]carbamate
hydroxyalbendazole = methyl [5-(3-hydroxypropylsulfanyl)-1H-benzimidazol-2-yl]carbamate

Other name(s): CYP2J2 (gene name)

Systematic name: albendazole,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (hydroxylating)

Comments: CYP2J2 is a microsomal cytochrome P-450 monooxygenase that catalyses the hydroxylation of the terminal carbon of the propylsulfanyl chain in albendazole, a broad-spectrum anthelmintic used against gastrointestinal nematodes and the larval stages of cestodes. cf. EC 1.14.14.73, albendazole monooxygenase (sulfoxide-forming).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Wu, Z., Lee, D., Joo, J., Shin, J.H., Kang, W., Oh, S., Lee, D.Y., Lee, S.J., Yea, S.S., Lee, H.S., Lee, T. and Liu, K.H. CYP2J2 and CYP2C19 are the major enzymes responsible for metabolism of albendazole and fenbendazole in human liver microsomes and recombinant P450 assay systems. Antimicrob. Agents Chemother. 57 (2013) 5448-5456. [PMID: 23959307]

[EC 1.14.14.74 created 2018]

EC 1.14.14.75

Accepted name: fenbendazole monooxygenase (4'-hydroxylating)

Reaction: fenbendazole + [reduced NADPH—hemoprotein reductase] + O2 = 4'-hydroxyfenbendazole + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Glossary: fenbendazole = methyl [5-(phenylsulfanyl)-1H-benzimidazol-2-yl]carbamate
4'-hydroxyfenbendazole = methyl [5-(4-hydroxyphenylsulfanyl)-1H-benzimidazol-2-yl]carbamate
albendazole = methyl [5-(propylsulfanyl)-1H-benzimidazol-2-yl]carbamate

Other name(s): CYP2C19 (gene name)

Systematic name: fenbendazole,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (4'-hydroxylating)

Comments: CYP2C19 is microsomal cytochrome P-450 monooxygenase that catalyses the hydroxylation of the benzene ring of fenbendazole, a broad-spectrum anthelmintic used against gastrointestinal nematodes and the larval stages of cestodes. This activity is also carried out by CYP2J2. cf. EC 1.14.14.74, albendazole monooxygenase (hydroxylating). CYP2C19 does not act on albendazole.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Wu, Z., Lee, D., Joo, J., Shin, J.H., Kang, W., Oh, S., Lee, D.Y., Lee, S.J., Yea, S.S., Lee, H.S., Lee, T. and Liu, K.H. CYP2J2 and CYP2C19 are the major enzymes responsible for metabolism of albendazole and fenbendazole in human liver microsomes and recombinant P450 assay systems. Antimicrob. Agents Chemother. 57 (2013) 5448-5456. [PMID: 23959307]

[EC 1.14.14.75 created 2018]

EC 1.14.14.76

Accepted name: ent-isokaurene C2/C3-hydroxylase

Reaction: ent-isokaurene + 2 O2 + 2 [reduced NADPH—hemoprotein reductase] = ent-isokaurene-2β,3β-diol + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) ent-isokaurene + O2 + [reduced NADPH—hemoprotein reductase] = ent-isokauren-2β-ol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) ent-isokauren-2β-ol + O2 + [reduced NADPH—hemoprotein reductase] = ent-isokaurene-2β,3β-diol + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Other name(s): CYP71Z6; ent-isokaurene C2-hydroxylase

Systematic name: ent-isokaurene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ent-isokaurene-2β,3β-diol forming)

Comments: This cytochrome P-450 (heme thiolate) enzyme has been characterized from the plant Oryza sativa (rice). It may be involved in production of oryzadione.

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]

2. Kitaoka, N., Wu, Y., Xu, M. and Peters, R.J. Optimization of recombinant expression enables discovery of novel cytochrome P450 activity in rice diterpenoid biosynthesis. Appl. Microbiol. Biotechnol. 99 (2015) 7549-7558. [PMID: 25758958]

[EC 1.14.14.76 created 2012 as EC 1.14.13.143, transferred 2018 to EC 1.14.14.76]

EC 1.14.14.77

Accepted name: phenylacetonitrile α-monooxygenase

Reaction: phenylacetonitrile + [reduced NADPH—hemoprotein reductase] + O2 = (R)-mandelonitrile + [oxidized NADPH—hemoprotein reductase] + H2O

Other name(s): CYP3201B1 (gene name)

Systematic name: phenylacetonitrile,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase [(R)-mandelonitrile-forming]

Comments: The enzyme has been characterized from the cyanogenic millipede Chamberlinius hualienensis. Unlike plant enzymes that can catalyse this reaction (EC 1.14.14.44, phenylacetaldehyde oxime monooxygenase), this enzyme cannot act on phenylacetaldehyde oximes. It can accept (4-hydroxyphenyl)acetonitrile, (2-methylphenyl)acetonitrile, and (3-methylphenyl)acetonitrile as substrates at a lower rate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Yamaguchi, T., Kuwahara, Y. and Asano, Y. A novel cytochrome P450, CYP3201B1, is involved in (R)-mandelonitrile biosynthesis in a cyanogenic millipede. FEBS Open Bio 7 (2017) 335-347. [PMID: 28286729]

[EC 1.14.14.77 created 2018]

EC 1.14.14.78

Accepted name: phylloquinone ω-hydroxylase

Reaction: phylloquinone + [reduced NADPH—hemoprotein reductase] + O2 = ω-hydroxyphylloquinone + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Other name(s): vitamin K1 ω-hydroxylase; CYP4F2; CYP4F11

Systematic name: phylloquinone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ω-hydroxyphylloquinone forming)

Comments: A cytochrome P-450 (heme-thiolate) protein. Isolated from human tissue. The enzyme will also act on menaquinone-4. Prolonged action of CYP4F2, but not CYP4F11, on the ω hydroxyl group oxidizes it to the corresponding carboxylic acid. CYP4F2 also oxidizes leukotriene B4; see EC 1.14.13.30, leukotriene-B4 20-monooxygenase [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Jin, R., Koop, D.R., Raucy, J.L. and Lasker, J.M. Role of human CYP4F2 in hepatic catabolism of the proinflammatory agent leukotriene B4. Arch. Biochem. Biophys. 359 (1998) 89-98. [PMID: 9799565]

2. Tang, Z., Salamanca-Pinzon, S.G., Wu, Z.L., Xiao, Y. and Guengerich, F.P. Human cytochrome P450 4F11: heterologous expression in bacteria, purification, and characterization of catalytic function. Arch. Biochem. Biophys. 494 (2010) 86-93. [PMID: 19932081]

3. Edson, K.Z., Prasad, B., Unadkat, J.D., Suhara, Y., Okano, T., Guengerich, F.P. and Rettie, A.E. Cytochrome P450-dependent catabolism of vitamin K: ω-hydroxylation catalyzed by human CYP4F2 and CYP4F11. Biochemistry 52 (2013) 8276-8285. [PMID: 24138531]

[EC 1.14.14.78 created 2014 as EC 1.14.13.194, transferred 2018 to EC 1.14.14.78]

EC 1.14.14.79

Accepted name: docosahexaenoic acid ω-hydroxylase

Reaction: docosahexaenoate + [reduced NADPH—hemoprotein reductase] + O2 = 22-hydroxydocosahexaenoate + [oxidized NADPH—hemoprotein reductase] + H2O

Glossary: docosahexaenoate = (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoate
icosapentaenoate = (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoate

Other name(s): CYP4F3B; CYP4V2; docosahexaenoate,NADPH:O2 oxidoreductase (22-hydroxydocosahexaenoate forming)

Systematic name: docosahexaenoate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (22-hydroxydocosahexaenoate forming)

Comments: A cytochrome P-450 (heme-thiolate) protein isolated from human eye tissue. Defects in the enzyme are associated with Bietti crystalline corneoretinal dystrophy. The enzyme also produces some 21-hydroxydocosahexaenoate. Acts in a similar way on icosapentaenoic acid.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Nakano, M., Kelly, E.J., Wiek, C., Hanenberg, H. and Rettie, A.E. CYP4V2 in Bietti’s crystalline dystrophy: ocular localization, metabolism of ω-3-polyunsaturated fatty acids, and functional deficit of the p.H331P variant. Mol. Pharmacol. 82 (2012) 679-686. [PMID: 22772592]

[EC 1.14.14.79 created 2014 as EC 1.14.13.199, transferred 2018 to EC 1.14.14.79]

EC 1.14.14.80

Accepted name: long-chain fatty acid ω-monooxygenase

Reaction: a long-chain fatty acid + [reduced NADPH—hemoprotein reductase] + O2 = an ω-hydroxy-long-chain fatty acid + [oxidized NADPH—hemoprotein reductase] + H2O

Other name(s): CYP704B1 (gene name); CYP52M1 (gene name); CYP4A (gene name); CYP86A (gene name)

Systematic name: long-chain fatty acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ω-hydroxylating)

Comments: A cytochrome P-450 (heme thiolate) enzyme. The plant enzyme CYP704B1, which is involved in the synthesis of sporopollenin, a complex polymer found at the outer layer of spores and pollen, acts on palmitate (18:0), stearate (18:0) and oleate (18:1). The plant enzyme CYP86A1 also acts on laurate (12:0). The enzyme from the yeast Starmerella bombicola (CYP52M1) acts on C16 to C20 saturated and unsaturated fatty acids and can also hydroxylate the (ω-1) position. The mammalian enzyme CYP4A acts on laurate (12:0), myristate (14:0), palmitate (16:0), oleate (18:1), and arachidonate (20:4).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Benveniste, I., Tijet, N., Adas, F., Philipps, G., Salaun, J.P. and Durst, F. CYP86A1 from Arabidopsis thaliana encodes a cytochrome P450-dependent fatty acid ω-hydroxylase. Biochem. Biophys. Res. Commun. 243 (1998) 688-693. [PMID: 9500987]

2. Hoch, U., Zhang, Z., Kroetz, D.L. and Ortiz de Montellano, P.R. Structural determination of the substrate specificities and regioselectivities of the rat and human fatty acid ω-hydroxylases. Arch. Biochem. Biophys. 373 (2000) 63-71. [PMID: 10620324]

3. Dobritsa, A.A., Shrestha, J., Morant, M., Pinot, F., Matsuno, M., Swanson, R., Møller, B.L. and Preuss, D. CYP704B1 is a long-chain fatty acid ω-hydroxylase essential for sporopollenin synthesis in pollen of Arabidopsis. Plant Physiol. 151 (2009) 574-589. [PMID: 19700560]

4. Huang, F.C., Peter, A. and Schwab, W. Expression and characterization of CYP52 genes involved in the biosynthesis of sophorolipid and alkane metabolism from Starmerella bombicola. Appl. Environ. Microbiol. 80 (2014) 766-776. [PMID: 24242247]

[EC 1.14.14.80 created 2015 as EC 1.14.13.205, transferred 2018 to EC 1.14.14.80]

EC 1.14.14.81

Accepted name: flavanoid 3',5'-hydroxylase

Reaction: a flavanone + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = a 3',5'-dihydroxyflavanone + 2 [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) a flavanone + [reduced NADPH—hemoprotein reductase] + O2 = a 3'-hydroxyflavanone + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) a 3'-hydroxyflavanone + [reduced NADPH—hemoprotein reductase] + O2 = a 3',5'-dihydroxyflavanone + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here or click here or click here.

Other name(s): flavonoid 3',5'-hydroxylase

Systematic name: flavanone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3',5'-dihydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. The 3',5'-dihydroxyflavanone is formed via the 3'-hydroxyflavanone. In Petunia hybrida the enzyme acts on naringenin, eriodictyol, dihydroquercetin (taxifolin) and dihydrokaempferol (aromadendrin). The enzyme catalyses the hydroxylation of 5,7,4'-trihydroxyflavanone (naringenin) at either the 3' position to form eriodictyol or at both the 3' and 5' positions to form 5,7,3',4',5'-pentahydroxyflavanone (dihydrotricetin). The enzyme also catalyses the hydroxylation of 3,5,7,3',4'-pentahydroxyflavanone (taxifolin) at the 5' position, forming ampelopsin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Menting, J., Scopes, R.K. and Stevenson, T.W. Characterization of flavonoid 3',5'-hydroxylase in microsomal membrane fraction of Petunia hybrida flowers. Plant Physiol. 106 (1994) 633-642. [PMID: 12232356]

2. Shimada, Y., Nakano-Shimada, R., Ohbayashi, M., Okinaka, Y., Kiyokawa, S. and Kikuchi, Y. Expression of chimeric P450 genes encoding flavonoid-3', 5'-hydroxylase in transgenic tobacco and petunia plants1. FEBS Lett. 461 (1999) 241-245. [PMID: 10567704]

3. de Vetten, N., ter Horst, J., van Schaik, H.P., de Boer, A., Mol, J. and Koes, R. A cytochrome b5 is required for full activity of flavonoid 3', 5'-hydroxylase, a cytochrome P450 involved in the formation of blue flower colors. Proc. Natl. Acad. Sci. USA 96 (1999) 778-783. [PMID: 9892710]

[EC 1.14.14.81 created 2004 as EC 1.14.13.88, transferred 2018 to EC 1.14.14.81]

EC 1.14.14.82

Accepted name: flavonoid 3'-monooxygenase

Reaction: a flavonoid + [reduced NADPH—hemoprotein reductase] + O2 = a 3'-hydroxyflavonoid + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here or click here.

Other name(s): CYP75B1 (gene name); flavonoid 3'-hydroxylase; flavonoid 3-hydroxylase (incorrect); NADPH:flavonoid-3'-hydroxylase (incorrect); flavonoid 3-monooxygenase (incorrect)

Systematic name: flavonoid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3'-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. Acts on a number of flavonoids, including the flavanone naringenin and the flavone apigenin. Does not act on 4-coumarate or 4-coumaroyl-CoA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Forkmann, G., Heller, W. and Grisebach, H. Anthocyanin biosynthesis in flowers of Matthiola incana flavanone 3- and flavonoid 3'-hydroxylases. Z. Naturforsch. C: Biosci. 35 (1980) 691-695.

2. Brugliera, F., Barri-Rewell, G., Holton, T.A. and Mason, J.G. Isolation and characterization of a flavonoid 3'-hydroxylase cDNA clone corresponding to the Ht1 locus of Petunia hybrida. Plant J. 19 (1999) 441-451. [PMID: 10504566]

3. Schoenbohm, C., Martens, S., Eder, C., Forkmann, G. and Weisshaar, B. Identification of the Arabidopsis thaliana flavonoid 3'-hydroxylase gene and functional expression of the encoded P450 enzyme. Biol. Chem. 381 (2000) 749-753. [PMID: 11030432]

[EC 1.14.14.82 created 1983 as EC 1.14.13.21, transferred 2018 to EC 1.14.14.82]

EC 1.14.14.83

Accepted name: geraniol 8-hydroxylase

Reaction: geraniol + [reduced NADPH—hemoprotein reductase] + O2 = (6E)-8-hydroxygeraniol + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Other name(s): CYP76B6 (gene name); G10H (gene name)

Systematic name: geraniol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (8-hydroxylating)

Comments: A cytochrome P-450 (heme thiolate) protein found in plants. Also hydroxylates nerol and citronellol, cf. EC 1.14.14.84, linalool 8-monooxygenase. The recommended numbering of geraniol gives 8-hydroxygeraniol as the product rather than 10-hydroxygeraniol as used by references 1-3. See prenol nomenclature Pr-1. The cloned enzyme also catalysed, but less efficiently, the 3'-hydroxylation of naringenin (cf. EC 1.14.14.82, flavonoid 3'-monooxygenase) [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Collu, G., Unver, N., Peltenburg-Looman, A.M., van der Heijden, R., Verpoorte, R. and Memelink, J. Geraniol 10-hydroxylase, a cytochrome P450 enzyme involved in terpenoid indole alkaloid biosynthesis. FEBS Lett. 508 (2001) 215-220. [PMID: 11718718]

2. Wang, J., Liu, Y., Cai, Y., Zhang, F., Xia, G. and Xiang, F. Cloning and functional analysis of geraniol 10-hydroxylase, a cytochrome P450 from Swertia mussotii Franch. Biosci. Biotechnol. Biochem. 74 (2010) 1583-1590. [PMID: 20699579]

3. Sung, P.H., Huang, F.C., Do, Y.Y. and Huang, P.L. Functional expression of geraniol 10-hydroxylase reveals its dual function in the biosynthesis of terpenoid and phenylpropanoid. J. Agric. Food Chem. 59 (2011) 4637-4643. [PMID: 21504162]

[EC 1.14.14.83 created 2012 as EC 1.14.13.152, transferred 2018 to EC 1.14.14.83]

EC 1.14.14.84

Accepted name: linalool 8-monooxygenase

Reaction: linalool + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = (6E)-8-oxolinalool + 2 [oxidized NADPH—hemoprotein reductase] + 3 H2O (overall reaction)
(1a) linalool + [reduced NADPH—hemoprotein reductase] + O2 = (6E)-8-hydroxylinalool + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) (6E)-8-hydroxylinalool + [reduced NADPH—hemoprotein reductase] + O2 = (6E)-8-oxolinalool + [oxidized NADPH—hemoprotein reductase] + 2 H2O

For diagram of reaction click here.

Glossary: linalool = 3,7-dimethylocta-1,6-dien-3-ol

Other name(s): P-450lin; CYP111

Systematic name: linalool,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (8-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. The secondary electron donor is a specific [2Fe-2S] ferredoxin from the same bacterial strain.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Ullah, A.J., Murray, R.I., Bhattacharyya, P.K., Wagner, G.C. and Gunsalus, I.C. Protein components of a cytochrome P-450 linalool 8-methyl hydroxylase. J. Biol. Chem. 265 (1990) 1345-1351. [PMID: 2295633]

2. Ropp, J.D., Gunsalus, I.C. and Sligar, S.G. Cloning and expression of a member of a new cytochrome P-450 family: cytochrome P-450lin (CYP111) from Pseudomonas incognita. J. Bacteriol. 175 (1993) 6028-6037. [PMID: 8376348]

[EC 1.14.14.84 created 1989 as EC 1.14.99.28, transferred 2012 to EC 1.14.13.151, transferred 2018 to EC 1.14.14.84]

EC 1.14.14.85

Accepted name: 7-deoxyloganate 7-hydroxylase

Reaction: 7-deoxyloganate + [reduced NADPH—hemoprotein reductase] + O2 = loganate + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here

Glossary: logonate = (1S,4aS,6S,7R,7aS)-1-(β-D-glucopyranosyloxy)-6-hydroxy-7-methyl-1,4a,5,6,7,7a-hexahydrocyclopenta[c]pyran-4-carboxylate

Other name(s): CYP72A224 (gene name); 7-deoxyloganin 7-hydroxylase (incorrect); 7-deoxyloganin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (7α-hydroxylating) (incorrect)

Systematic name: 7-deoxyloganate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (7α-hydroxylating)

Comments: The enzyme, characterized from the plant Catharanthus roseus, is a cytochrome P-450 (heme-thiolate) enzyme. It catalyses a reaction in the pathway leading to biosynthesis of monoterpenoid indole alkaloids.

Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number: 335305-40-3

References:

1. Katano, N., Yamamoto, H., Iio, R. and Inoue, K. 7-Deoxyloganin 7-hydroxylase in Lonicera japonica cell cultures. Phytochemistry 58 (2001) 53-58. [PMID: 11524113]

2. Miettinen, K., Dong, L., Navrot, N., Schneider, T., Burlat, V., Pollier, J., Woittiez, L., van der Krol, S., Lugan, R., Ilc, T., Verpoorte, R., Oksman-Caldentey, K.M., Martinoia, E., Bouwmeester, H., Goossens, A., Memelink, J. and Werck-Reichhart, D. The seco-iridoid pathway from Catharanthus roseus. Nat Commun 5 (2014) 3606. [PMID: 24710322]

[EC 1.14.14.85 created 2002 as EC 1.14.13.74, transferred 2018 to EC 1.14.14.85, modified 2018]

EC 1.14.14.86

Accepted name: ent-kaurene monooxygenase

Reaction: ent-kaur-16-ene + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = ent-kaur-16-en-19-oate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) ent-kaur-16-ene + [reduced NADPH—hemoprotein reductase] + O2 = ent-kaur-16-en-19-ol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) ent-kaur-16-en-19-ol + [reduced NADPH—hemoprotein reductase] + O2 = ent-kaur-16-en-19-al + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) ent-kaur-16-en-19-al + [reduced NADPH—hemoprotein reductase] + O2 = ent-kaur-16-en-19-oate + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Other name(s): ent-kaurene oxidase (misleading)

Systematic name: ent-kaur-16-ene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (hydroxylating)

Comments: A cytochrome P-450 (heme thiolate) protein found in plants. Catalyses three successive oxidations of the 4-methyl group of ent-kaurene giving kaurenoic acid.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Ashman, P.J., Mackenzie, A. and Bramley, P.M. Characterization of ent-kaurene oxidase activity from Gibberella fujikuroi. Biochim. Biophys. Acta 1036 (1990) 151-157. [PMID: 2223832]

2. Archer, C., Ashman, P.J., Hedden, P., Bowyer, J.R. and Bramley, P.M. Purification of ent-kaurene oxidase from Gibberella fujikuroi and Cucurbita maxima. Biochem. Soc. Trans. 20 (1992) 218. [PMID: 1397591]

3. Helliwell, C.A., Poole, A., Peacock, W.J. and Dennis, E.S. Arabidopsis ent-kaurene oxidase catalyzes three steps of gibberellin biosynthesis. Plant Physiol. 119 (1999) 507-510. [PMID: 9952446]

[EC 1.14.14.86 created 2002 as EC 1.14.13.78, transferred 2018 to EC 1.14.14.86]

EC 1.14.14.87

Accepted name: 2-hydroxyisoflavanone synthase

Reaction: (1) liquiritigenin + O2 + [reduced NADPH—hemoprotein reductase] = 2,4',7-trihydroxyisoflavanone + H2O + [oxidized NADPH—hemoprotein reductase]
(2) (2S)-naringenin + O2 + [reduced NADPH—hemoprotein reductase] = 2,4',5,7-tetrahydroxyisoflavanone + H2O + [oxidized NADPH—hemoprotein reductase]

For diagram of reaction click here.

Glossary: liquiritigenin = 4',7-dihydroxyflavanone
(2S)-naringenin = 4',5,7-dihydroxyflavanone
2,4',5,7-tetrahydroxyisoflavanone = 2-hydroxy-2,3-dihydrogenistein

Other name(s): CYP93C; IFS; isoflavonoid synthase

Systematic name: liquiritigenin, [reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (hydroxylating, aryl migration)

Comments: A cytochrome P-450 (heme thiolate) protein found in plants. The reaction involves the migration of the 2-phenyl group of the flavanone to the 3-position of the isoflavanone. The 2-hydroxyl group is derived from the oxygen molecule. EC 4.2.1.105, 2-hydroxyisoflavanone dehydratase, acts on the products with loss of water and formation of genistein and daidzein, respectively.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kochs, G. and Grisebach, H. Enzymic synthesis of isoflavones. Eur. J. Biochem. 155 (1986) 311-318. [PMID: 3956488]

2. 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]

3. Steele, C. L., Gijzen, M., Qutob, D. and Dixon, R.A. Molecular characterization of the enzyme catalyzing the aryl migration reaction of isoflavonoid biosynthesis in soybean. Arch. Biochem. Biophys. 367 (1999) 146-150. [PMID: 10375412]

4. 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]

5. 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]

[EC 1.14.14.87 created 2011 as EC 1.14.13.136, modified 2013, transferred 2018 to EC 1.14.14.87]

EC 1.14.14.88

Accepted name: isoflavone 3'-hydroxylase

Reaction: formononetin + [reduced NADPH—hemoprotein reductase] + O2 = calycosin + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Glossary: calycosin = 3'-hydroxyformononetin

Other name(s): isoflavone 3'-monooxygenase; CYP81E9

Systematic name: formononetin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3'-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein. Also acts on biochanin A and other isoflavones with a 4'-methoxy group. Involved in the biosynthesis of the pterocarpin phytoalexins medicarpin and maackiain.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Hinderer, W., Flentje, U. and Barz, W. Microsomal isoflavone 2'-hydroxylases and 3'-hydroxylases from chickpea (Cicer arietinum L) cell-suspensions induced for pterocarpan phytoalexin formation. FEBS Lett. 214 (1987) 101-106.

[EC 1.14.14.88 created 1992 as EC 1.14.13.52, transferred 2018 to EC 1.14.14.88]

EC 1.14.14.89

Accepted name: 4'-methoxyisoflavone 2'-hydroxylase

Reaction: formononetin + [reduced NADPH—hemoprotein reductase] + O2 = 2'-hydroxyformononetin + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Other name(s): CYP81E1 (gene name); CYP81E3 (gene name); CYP81E7 (gene name); isoflavone 2'-monooxygenase (ambiguous); isoflavone 2'-hydroxylase (ambiguous)

Systematic name: formononetin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2'-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein. Acts on isoflavones with a 4'-methoxy group, such as formononetin and biochanin A. Involved in the biosynthesis of the pterocarpin phytoalexins medicarpin and maackiain. EC 1.14.14.90, isoflavone 2'-hydroxylase, is less specific and acts on other isoflavones as well as 4'-methoxyisoflavones.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Hinderer, W., Flentje, U. and Barz, W. Microsomal isoflavone 2'-hydroxylases and 3'-hydroxylases from chickpea (Cicer arietinum L) cell-suspensions induced for pterocarpan phytoalexin formation. FEBS Lett. 214 (1987) 101-106.

2. Akashi, T., Aoki, T. and Ayabe, S.-I. CYP81E1, a cytochrome P450 cDNA of licorice (Glycyrrhiza echinata L.), encodes isoflavone 2'-hydroxylase. Biochem. Biophys. Res. Commun. 251 (1998) 67-70. [PMID: 9790908]

3. Liu, C.J., Huhman, D., Sumner, L.W. and Dixon, R.A. Regiospecific hydroxylation of isoflavones by cytochrome p450 81E enzymes from Medicago truncatula. Plant J. 36 (2003) 471-484. [PMID: 14617078]

[EC 1.14.14.89 created 1992 as EC 1.14.13.53, modified 2005, transferred 2018 to EC 1.14.14.89]

EC 1.14.14.90

Accepted name: isoflavone 2'-hydroxylase

Reaction: an isoflavone + [reduced NADPH—hemoprotein reductase] + O2 = a 2'-hydroxyisoflavone + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Other name(s): isoflavone 2'-monooxygenase; CYP81E1; CYP Ge-3

Systematic name: isoflavone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2'-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein. Acts on daidzein, formononetin and genistein. EC 1.14.14.89, 4'-methoxyisoflavone 2'-hydroxylase, has the same reaction but is more specific as it requires a 4'-methoxyisoflavone.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Akashi, T., Aoki, T. and Ayabe, S.-I. CYP81E1, a cytochrome P450 cDNA of licorice (Glycyrrhiza echinata L.), encodes isoflavone 2'-hydroxylase. Biochem. Biophys. Res. Commun. 251 (1998) 67-70. [PMID: 9790908]

[EC 1.14.14.90 created 2005 as EC 1.14.13.89, transferred 2018 to EC 1.14.14.90]

EC 1.14.14.91

Accepted name: trans-cinnamate 4-monooxygenase

Reaction: trans-cinnamate + [reduced NADPH—hemoprotein reductase] + O2 = 4-hydroxycinnamate + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Other name(s): cinnamic acid 4-hydroxylase; CA4H; cytochrome P450 cinnamate 4-hydroxylase; cinnamate 4-hydroxylase; cinnamate 4-monooxygenase; cinnamate hydroxylase; cinnamic 4-hydroxylase; cinnamic acid 4-monooxygenase; cinnamic acid p-hydroxylase; t-cinnamic acid hydroxylase; trans-cinnamate 4-hydroxylase; trans-cinnamic acid 4-hydroxylase; CYP73A1 (gene name)

Systematic name: trans-cinnamate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (4-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. The enzyme is involved in flavonoid biosynthesis.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Potts, J.R.M., Weklych, R. and Conn, E.E. The 4-hydroxylation of cinnamic acid by sorghum microsomes and the requirement for cytochrome P-450. J. Biol. Chem. 249 (1974) 5019-5026. [PMID: 4153152]

2. Russell, D.W. and Conn, E.E. The cinnamic acid 4-hydroxylase of pea seedlings. Arch. Biochem. Biophys. 122 (1967) 256-268. [PMID: 4383827]

3. Pierrel, M.A., Batard, Y., Kazmaier, M., Mignotte-Vieux, C., Durst, F. and Werck-Reichhart, D. Catalytic properties of the plant cytochrome P450 CYP73 expressed in yeast. Substrate specificity of a cinnamate hydroxylase. Eur. J. Biochem. 224 (1994) 835-844. [PMID: 7925408]

[EC 1.14.14.91 created 1976 as EC 1.14.13.11, transferred 2018 to EC 1.14.14.91]

EC 1.14.14.92

Accepted name: benzoate 4-monooxygenase

Reaction: benzoate + [reduced NADPH—hemoprotein reductase] + O2 = 4-hydroxybenzoate + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Other name(s): benzoic acid 4-hydroxylase; benzoate 4-hydroxylase; benzoic 4-hydroxylase; benzoate-p-hydroxylase; p-hydroxybenzoate hydroxylase; CYP53A1 (gene name)

Systematic name: benzoate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (4-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein found in Aspergillus fungi.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Reddy, C.C. and Vaidyanathan, C.S. Purification, properties and induction of a specific benzoate-4-hydroxylase from Aspergillus niger (UBC 814). Biochim. Biophys. Acta 384 (1975) 46-57. [PMID: 236777]

2. Faber, B.W., van Gorcom, R.F. and Duine, J.A. Purification and characterization of benzoate-para-hydroxylase, a cytochrome P450 (CYP53A1), from Aspergillus niger. Arch. Biochem. Biophys. 394 (2001) 245-254. [PMID: 11594739]

[EC 1.14.14.92 created 1976 as EC 1.14.13.12, transferred 2018 to EC 1.14.14.92]

EC 1.14.14.93

Accepted name: 3,9-dihydroxypterocarpan 6a-monooxygenase

Reaction: (6aR,11aR)-3,9-dihydroxypterocarpan + [reduced NADPH—hemoprotein reductase] + O2 = (6aS,11aS)-3,6a,9-trihydroxypterocarpan + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Other name(s): 3,9-dihydroxypterocarpan 6a-hydroxylase; 3,9-dihydroxypterocarpan 6α-monooxygenase (erroneous); CYP93A1 (gene name)

Systematic name: (6aR,11aR)-3,9-dihydroxypterocarpan,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6a-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein found in soybean. The product of the reaction is the biosynthetic precursor of the glyceollin phytoalexins.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Hagmann, M.-L., Heller, W. and Grisebach, H. Induction of phytoalexin synthesis in soybean. Stereospecific 3,9-dihydroxypterocarpan 6a-hydroxylase from elicitor-induced soybean cell cultures. Eur. J. Biochem. 142 (1984) 127-131. [PMID: 6540173]

2. Schopfer, C.R., Kochs, G., Lottspeich, F. and Ebel, J. Molecular characterization and functional expression of dihydroxypterocarpan 6a-hydroxylase, an enzyme specific for pterocarpanoid phytoalexin biosynthesis in soybean (Glycine max L.). FEBS Lett. 432 (1998) 182-186. [PMID: 9720921]

[EC 1.14.14.93 created 1989 as EC 1.14.13.28, transferred 2018 to EC 1.14.14.93]

EC 1.14.14.94

Accepted name: leukotriene-B4 20-monooxygenase

Reaction: (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + [reduced NADPH—hemoprotein reductase] + O2 = (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + [oxidized NADPH—hemoprotein reductase] + H2O

Other name(s): leukotriene-B4 20-hydroxylase; leucotriene-B4 ω-hydroxylase; LTB4 20-hydroxylase; LTB4 ω-hydroxylase; CYP4F2 (gene name); CYP4F3 (gene name)

Systematic name: (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (20-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein found in mammals.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Romano, M.C., Eckardt, R.D., Bender, P.E., Leonard, T.B., Straub, K.M. and Newton, J.F. Biochemical characterization of hepatic microsomal leukotriene B4 hydroxylases. J. Biol. Chem. 262 (1987) 1590-1595. [PMID: 3027095]

2. Shak, S. and Goldstein, I.M. Leukotriene B4 ω-hydroxylase in human polymorphonuclear leukocytes. Partial purification and identification as a cytochrome P-450. J. Clin. Invest. 76 (1985) 1218-1228. [PMID: 4044832]

3. Soberman, R.J., Harper, T.W., Murphy, R.C. and Austen, K.F. Identification and functional characterization of leukotriene B4 20-hydroxylase of human polymorphonuclear leukocytes. Proc. Natl Acad. Sci. USA 82 (1985) 2292-2295. [PMID: 2986111]

[EC 1.14.14.94 created 1989 as EC 1.14.13.30, transferred 2018 to EC 1.14.14.94]

EC 1.14.14.95

Accepted name: germacrene A hydroxylase

Reaction: (+)-germacrene A + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = germacra-1(10),4,11(13)-trien-12-oate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) (+)-germacrene A + O2 + [reduced NADPH—hemoprotein reductase] = germacra-1(10),4,11(13)-trien-12-ol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) germacra-1(10),4,11(13)-trien-12-ol + O2 + [reduced NADPH—hemoprotein reductase] = germacra-1(10),4,11(13)-trien-12-al + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) germacra-1(10),4,11(13)-trien-12-al + O2 + [reduced NADPH—hemoprotein reductase] = germacra-1(10),4,11(13)-trien-12-oate + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Other name(s): GAO (gene name)

Systematic name: (+)-germacrene-A,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein. This plant enzyme catalyses three steps in a pathway that leads to the biosynthesis of many sesquiterpenoid lactones.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. 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]

2. Liu, Q., Manzano, D., Tanic, N., Pesic, M., Bankovic, J., Pateraki, I., Ricard, L., Ferrer, A., de Vos, R., van de Krol, S. and Bouwmeester, H. Elucidation and in planta reconstitution of the parthenolide biosynthetic pathway. Metab. Eng. 23 (2014) 145-153. [PMID: 24704560]

[EC 1.14.14.95 created 2011 as EC 1.14.13.123, transferred 2018 to EC 1.14.14.95]

EC 1.14.14.96

Accepted name: 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase

Reaction: trans-5-O-(4-coumaroyl)-D-quinate + [reduced NADPH—hemoprotein reductase] + O2 = trans-5-O-caffeoyl-D-quinate + [oxidized NADPH—hemoprotein reductase] + H2O

Other name(s): 5-O-(4-coumaroyl)-D-quinate/shikimate 3'-hydroxylase; coumaroylquinate(coumaroylshikimate) 3'-monooxygenase; CYP98A3 (gene name)

Systematic name: trans-5-O-(4-coumaroyl)-D-quinate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3'-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein, found in plants. It also acts on trans-5-O-(4-coumaroyl)shikimate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kühnl, T., Koch, U., Heller, W. and Wellman, E. Chlorogenic acid biosynthesis: characterization of a light-induced microsomal 5-O-(4-coumaroyl)-D-quinate/shikimate 3'-hydroxylase from carrot (Daucus carota L.) cell suspension cultures. Arch. Biochem. Biophys. 258 (1987) 226-232. [PMID: 2821918]

2. Schoch, G., Goepfert, S., Morant, M., Hehn, A., Meyer, D., Ullmann, P. and Werck-Reichhart, D. CYP98A3 from Arabidopsis thaliana is a 3'-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway. J. Biol. Chem 276 (2001) 36566-36574. [PMID: 11429408]

3. Franke, R., Humphreys, J.M., Hemm, M.R., Denault, J.W., Ruegger, M.O., Cusumano, J.C. and Chapple, C. The Arabidopsis REF8 gene encodes the 3-hydroxylase of phenylpropanoid metabolism. Plant J. 30 (2002) 33-45. [PMID: 11967091]

4. Matsuno, M., Compagnon, V., Schoch, G.A., Schmitt, M., Debayle, D., Bassard, J.E., Pollet, B., Hehn, A., Heintz, D., Ullmann, P., Lapierre, C., Bernier, F., Ehlting, J. and Werck-Reichhart, D. Evolution of a novel phenolic pathway for pollen development. Science 325 (2009) 1688-1692. [PMID: 19779199]

[EC 1.14.14.96 created 1990 as EC 1.14.13.36, transferred 2018 to EC 1.14.14.96]

EC 1.14.14.97

Accepted name: methyltetrahydroprotoberberine 14-monooxygenase

Reaction: (S)-N-methylcanadine + [reduced NADPH—hemoprotein reductase] + O2 = allocryptopine + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here or click here.

Other name(s): methyltetrahydroprotoberberine 14-hydroxylase; (S)-cis-N-methyltetrahydroberberine 14-monooxygenase; (S)-cis-N-methyltetrahydroprotoberberine-14-hydroxylase; CYP82N4 (gene name)

Systematic name: (S)-N-methylcanadine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (14-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein found in plants.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Rueffer, M. and Zenk, M.H. Enzymatic formation of protopines by a microsomal cytochrome-P-450 system of Corydalis vaginans. Tetrahedron Lett. 28 (1987) 5307-5310.

2. Beaudoin, G.A. and Facchini, P.J. Isolation and characterization of a cDNA encoding (S)-cis-N-methylstylopine 14-hydroxylase from opium poppy, a key enzyme in sanguinarine biosynthesis. Biochem. Biophys. Res. Commun. 431 (2013) 597-603. [PMID: 23313486]

[EC 1.14.14.97 created 1990 as EC 1.14.13.37, transferred 2018 to EC 1.14.14.97]

EC 1.14.14.98

Accepted name: protopine 6-monooxygenase

Reaction: protopine + [reduced NADPH—hemoprotein reductase] + O2 = 6-hydroxyprotopine + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Other name(s): protopine 6-hydroxylase; CYP82N2 (gene name)

Systematic name: protopine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein involved in benzophenanthridine alkaloid synthesis in higher plants.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Tanahashi, T. and Zenk, M.H. Elicitor induction and characterization of microsomal protopine-6-hydroxylase, the central enzyme in benzophenanthridine alkaloid biosynthesis. Phytochemistry 29 (1990) 1113-1122.

2. Takemura, T., Ikezawa, N., Iwasa, K. and Sato, F. Molecular cloning and characterization of a cytochrome P450 in sanguinarine biosynthesis from Eschscholzia californica cells. Phytochemistry 91 (2013) 100-108. [PMID: 22421633]

[EC 1.14.14.98 created 1999 as EC 1.14.13.55, transferred 2018 to EC 1.14.14.98]

EC 1.14.14.99

Accepted name: (S)-limonene 3-monooxygenase

Reaction: (S)-limonene + [reduced NADPH—hemoprotein reductase] + O2 = (–)-trans-isopiperitenol + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Glossary: limonene = a monoterpenoid
(S)-limonene = (–)-limonene

Other name(s): (–)-limonene 3-hydroxylase; (–)-limonene 3-monooxygenase; CYP71D15 (gene name)

Systematic name: (S)-limonene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein from peppermint (Mentha piperita).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Karp, F., Mihaliak, C.A., Harris, J.L. and Croteau, R. Monoterpene biosynthesis: specificity of the hydroxylations of (–)-limonene by enzyme preparations from peppermint (Mentha piperita), spearmint (Mentha spicata), and perilla (Perilla frutescens) leaves. Arch. Biochem. Biophys. 276 (1990) 219-226. [PMID: 2297225]

2. Lupien, S., Karp, F., Wildung, M. and Croteau, R. Regiospecific cytochrome P450 limonene hydroxylases from mint (Mentha) species: cDNA isolation, characterization, and functional expression of (–)-4S-limonene-3-hydroxylase and (–)-4S-limonene-6-hydroxylase. Arch. Biochem. Biophys. 368 (1999) 181-192. [PMID: 10415126]

3. Wust, M., Little, D.B., Schalk, M. and Croteau, R. Hydroxylation of limonene enantiomers and analogs by recombinant (–)-limonene 3- and 6-hydroxylases from mint (Mentha) species: evidence for catalysis within sterically constrained active sites. Arch. Biochem. Biophys. 387 (2001) 125-136. [PMID: 11368174]

[EC 1.14.14.99 created 1992 as EC 1.14.13.47, modified 2003, transferred 2018 1.14.14.99]

EC 1.14.14.100

Accepted name: dihydrosanguinarine 10-monooxygenase

Reaction: dihydrosanguinarine + [reduced NADPH—hemoprotein reductase] + O2 = 10-hydroxydihydrosanguinarine + [oxidized NADPH—hemoprotein reductase] + H2O

For diagram of reaction click here.

Other name(s): dihydrosanguinarine 10-hydroxylase

Systematic name: dihydrosanguinarine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (10-hydroxylating)

Comments: A cytochrome P-450 (heme-thiolate) protein involved in benzophenanthridine alkaloid synthesis in higher plants.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. De-Eknamkul, W., Tanahashi, T. and Zenk, M.H. Enzymic 10-hydroxylation and 10-O-methylation of dihydrosanguinarine in dihydrochelirubine formation by Eschscholtzia. Phytochemistry 31 (1992) 2713-2717.

[EC 1.14.14.100 created 1999 as EC 1.14.13.56, transferred 2018 to EC 1.14.14.100]


Continued with EC 1.14.14.101 - EC 1.14.14.171
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