Enzyme Nomenclature

Continued from EC 1.14.19.1-50

EC 1.14.19 (continued)


With oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water

Continued from:
EC 1.14.19.1 to EC 1.14.19.50

Contents

EC 1.14.19.51 (S)-corytuberine synthase
EC 1.14.19.52 camalexin synthase
EC 1.14.19.53 all-trans-retinol 3,4-desaturase
EC 1.14.19.54 1,2-dehydroreticuline synthase
EC 1.14.19.55 4-hydroxybenzoate brominase (decarboxylating)
EC 1.14.19.56 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] chlorinase
EC 1.14.19.57 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] brominase
EC 1.14.19.58 tryptophan 5-halogenase
EC 1.14.19.59 tryptophan 6-halogenase
EC 1.14.19.60 7-chloro-L-tryptophan 6-halogenase
EC 1.14.19.61 dihydrorhizobitoxine desaturase
EC 1.14.19.62 secologanin synthase
EC 1.14.19.63 pseudobaptigenin synthase
EC 1.14.19.64 (S)-stylopine synthase
EC 1.14.19.65 (S)-cheilanthifoline synthase
EC 1.14.19.66 berbamunine synthase
EC 1.14.19.67 salutaridine synthase
EC 1.14.19.68 (S)-canadine synthase
EC 1.14.19.69 biflaviolin synthase
EC 1.14.19.70 mycocyclosin synthase
EC 1.14.19.71 fumitremorgin C synthase
EC 1.14.19.72 (–)-pluviatolide synthase
EC 1.14.19.73 (S)-nandinine synthase
EC 1.14.19.74 (+)-piperitol/(+)-sesamin synthase
EC 1.14.19.75 very-long-chain acyl-lipid ω-9 desaturase
EC 1.14.19.76 flavone synthase II

EC 1.14.19.51

Accepted name: (S)-corytuberine synthase

Reaction: (S)-reticuline + [reduced NADPH—hemoprotein reductase] + O2 = (S)-corytuberine + [oxidized NADPH—hemoprotein reductase] + 2 H2O.

For diagram of reaction click here.

Other name(s): CYP80G2

Systematic name: (S)-reticuline,NADPH:oxygen oxidoreductase (C-C phenol-coupling; (S)-corytuberine-forming)

Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme is involved in the biosynthesis of the quaternary benzylisoquinoline alkaloid magnoflorine in the plant Coptis japonica. It is specific for (S)-reticuline.

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

References:

1. Ikezawa, N., Iwasa, K. and Sato, F. Molecular cloning and characterization of CYP80G2, a cytochrome P450 that catalyzes an intramolecular C-C phenol coupling of (S)-reticuline in magnoflorine biosynthesis, from cultured Coptis japonica cells. J. Biol. Chem. 283 (2008) 8810-8821. [PMID: 18230623]

[EC 1.14.19.51 created 2017]

EC 1.14.19.52

Accepted name: camalexin synthase

Reaction: 2-(L-cystein-S-yl)-2-(1H-indol-3-yl)acetonitrile + 2 [reduced NADPH —hemoprotein reductase] + 2 O2 = camalexin + hydrogen cyanide + CO2 + 2 [oxidized NADPH —hemoprotein reductase] + 4 H2O (overall reaction)
(1a) 2-(L-cystein-S-yl)-2-(1H-indol-3-yl)acetonitrile + [reduced NADPH —hemoprotein reductase] + O2 = (R)-dihydrocamalexate + hydrogen cyanide + [oxidized NADPH —hemoprotein reductase] + 2 H2O
(1b) (R)-dihydrocamalexate + [reduced NADPH —hemoprotein reductase] + O2 = camalexin + CO2 + [oxidized NADPH —hemoprotein reductase] + 2 H2O

Glossary: camalexin = 3-(thiazol-2-yl)indole
(R)-dihydrocamalexate = (4R)-2-(1H-indol-3-yl)-4,5-dihydrothiazole-4-carboxylate

Other name(s): CYP71B15 (gene name); bifunctional dihydrocamalexate synthase/camalexin synthase

Systematic name: 2-(cystein-S-yl)-2-(1H-indol-3-yl)-acetonitrile, [reduced NADPH —hemoprotein reductase]:oxygen oxidoreductase (camalexin-forming)

Comments: This cytochrome P-450 (heme thiolate) enzyme, which has been characterized from the plant Arabidopsis thaliana, catalyses the last two steps in the biosynthesis of camalexin, the main phytoalexin in that plant. The enzyme catalyses two successive oxidation events. During the first oxidation the enzyme introduces a C-N double bond, liberating hydrogen cyanide, and during the second oxidation it catalyses a decarboxylation.

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

References:

1. Schuhegger, R., Nafisi, M., Mansourova, M., Petersen, B.L., Olsen, C.E., Svatos, A., Halkier, B.A. and Glawischnig, E. CYP71B15 (PAD3) catalyzes the final step in camalexin biosynthesis. Plant Physiol. 141 (2006) 1248-1254. [PMID: 16766671]

2. Böttcher, C., Westphal, L., Schmotz, C., Prade, E., Scheel, D. and Glawischnig, E. The multifunctional enzyme CYP71B15 (PHYTOALEXIN DEFICIENT3) converts cysteine-indole-3-acetonitrile to camalexin in the indole-3-acetonitrile metabolic network of Arabidopsis thaliana. Plant Cell 21 (2009) 1830-1845. [PMID: 19567706]

[EC 1.14.19.52 created 2017]

EC 1.14.19.53

Accepted name: all-trans-retinol 3,4-desaturase

Reaction: all-trans-retinol + 2 reduced adrenodoxin + 2 H+ + O2 = all-trans-3,4-didehydroretinol + 2 oxidized adrenodoxin + 2 H2O

For diagram of reaction click here.

Other name(s): CYP27C1 (gene name)

Systematic name: all-trans-retinol,reduced adrenodoxin:oxygen 3,4-oxidoreductase

Comments: A cytochrome P-450 (heme thiolate) enzyme found in vertebrates. The enzyme is also active with retinal and retinoic acid.

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

References:

1. Enright, J.M., Toomey, M.B., Sato, S.Y., Temple, S.E., Allen, J.R., Fujiwara, R., Kramlinger, V.M., Nagy, L.D., Johnson, K.M., Xiao, Y., How, M.J., Johnson, S.L., Roberts, N.W., Kefalov, V.J., Guengerich, F.P. and Corbo, J.C. Cyp27c1 red-shifts the spectral sensitivity of photoreceptors by converting vitamin A1 into A2. Curr. Biol. 25 (2015) 3048-3057. [PMID: 26549260]

2. Kramlinger, V.M., Nagy, L.D., Fujiwara, R., Johnson, K.M., Phan, T.T., Xiao, Y., Enright, J.M., Toomey, M.B., Corbo, J.C. and Guengerich, F.P. Human cytochrome P450 27C1 catalyzes 3,4-desaturation of retinoids. FEBS Lett. 590 (2016) 1304-1312. [PMID: 27059013]

[EC 1.14.19.53 created 2018]

EC 1.14.19.54

Accepted name: 1,2-dehydroreticuline synthase

Reaction: (S)-reticuline + [reduced NADPH—hemoprotein reductase] + O2 = 1,2-dehydroreticuline + [oxidized NADPH—hemoprotein reductase] + 2 H2O

For diagram of reaction click here.

Glossary: reticuline = 1-(3-hydroxy-4-methoxybenzyl)-6-methoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-7-ol

Other name(s): STORR; CYP82Y2 (gene name); DRS (gene name)

Systematic name: (S)-reticuline,[reduced NADPH—hemoprotein reductase]:oxygen 1,2-oxidoreductase

Comments: A P-450 (heme-thiolate) cytochrome. The enzyme from Papaver rhoeas (field poppy) is specific for (S)-reticuline and does not act on the (R)-form. The enzyme from Papaver somniferum (opium poppy), which is involved in the biosynthesis of morphine and related alkaloids, forms a fusion protein with EC 1.5.1.27, 1,2-dehydroreticulinium reductase (NADPH), which catalyses the reduction of 1,2-dehydroreticuline to (R)-reticuline, thus forming an epimerase system that converts (S)-reticuline to (R)-reticuline.

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

References:

1. Hirata, K., Poeaknapo, C., Schmidt, J. and Zenk, M.H. 1,2-Dehydroreticuline synthase, the branch point enzyme opening the morphinan biosynthetic pathway. Phytochemistry 65 (2004) 1039-1046. [PMID: 15110683]

2. Winzer, T., Kern, M., King, A.J., Larson, T.R., Teodor, R.I., Donninger, S.L., Li, Y., Dowle, A.A., Cartwright, J., Bates, R., Ashford, D., Thomas, J., Walker, C., Bowser, T.A. and Graham, I.A. Morphinan biosynthesis in opium poppy requires a P450-oxidoreductase fusion protein. Science 349 (2015) 309-312. [PMID: 26113639]

3. Farrow, S.C., Hagel, J.M., Beaudoin, G.A., Burns, D.C. and Facchini, P.J. Stereochemical inversion of (S)-reticuline by a cytochrome P450 fusion in opium poppy. Nat. Chem. Biol. 11 (2015) 728-732. [PMID: 26147354]

[EC 1.14.19.54 created 2018]

EC 1.14.19.55

Accepted name: 4-hydroxybenzoate brominase (decarboxylating)

Reaction: (1) 4-hydroxybenzoate + 2 NADPH + 2 bromide + 2 O2 + 2 H+ = 2,4-dibromophenol + 2 NADP+ + CO2 + 4 H2O (overall reaction)
(1a) 4-hydroxybenzoate + NADPH + bromide + O2 + H+ = 3-bromo-4-hydroxybenzoate + NADP+ + 2 H2O
(1b) 3-bromo-4-hydroxybenzoate + NADPH + bromide + O2 + H+ = 2,4-dibromophenol + NADP+ + CO2 + 2 H2O
(2) 3,4-dihydroxybenzoate + 2 NADPH + 2 bromide + 2 O2 + 2 H+ = 3,5-dibromobenzene-1,2-diol + 2 NADP+ + CO2 + 4 H2O (overall reaction)
(2a) 3,4-dihydroxybenzoate + NADPH + bromide + O2 + H+ = 3-bromo-4,5-dihydroxybenzoate + NADP+ + 2 H2O
(2b) 3-bromo-4,5-dihydroxybenzoate + NADPH + bromide + O2 + H+ = 3,5-dibromobenzene-1,2-diol + NADP+ + CO2 + 2 H2O

Other name(s): bmp5 (gene name)

Systematic name: 4-hydroxybenzoate:NADPH oxidoreductase (brominating, decarboxylating)

Comments: Contains FAD. The enzyme, described from epiphytic marine bacteria of the genera Pseudoalteromonas and Marinomonas, is an unusual single-component FAD-dependent halogenase that contains a distinct NAD(P)H binding domain and does not require an additional flavin reductase for activity. The enzyme catalyses a bromination of its substrate, followed by a second bromination concurrent with decarboxylation.

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

References:

1. Agarwal, V., El Gamal, A.A., Yamanaka, K., Poth, D., Kersten, R.D., Schorn, M., Allen, E.E. and Moore, B.S. Biosynthesis of polybrominated aromatic organic compounds by marine bacteria. Nat. Chem. Biol. 10 (2014) 640-647. [PMID: 24974229]

2. Agarwal, V. and Moore, B.S. Enzymatic synthesis of polybrominated dioxins from the marine environment. ACS Chem. Biol. 9 (2014) 1980-1984. [PMID: 25061970]

[EC 1.14.19.55 created 2018]

EC 1.14.19.56

Accepted name: 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] chlorinase

Reaction: 1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + 2 FADH2 + 2 chloride + 2 O2 = 4,5-dichloro-1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + 2 FAD + 4 H2O (overall reaction)
(1a) 1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + FADH2 + chloride + O2 = 5-chloro-1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + FAD + 2 H2O
(1b) 5-chloro-1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + FADH2 + chloride + O2 = 4,5-dichloro-1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + FAD + H2O

Glossary: pyoluteorin = 4,5-dichloro-1H-pyrrol-2-yl 2,6-dihydroxyphenyl

Other name(s): pltA (gene name)

Systematic name: 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein]:FADH2 oxidoreductase (chlorinating)

Comments: The enzyme, characterized from the bacterium Pseudomonas protegens Pf-5, is a flavin-dependent chlorinase that participates in the biosynthesis of the antibacterial and antifungal compound pyoluteorin.

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

References:

1. Nowak-Thompson, B., Chaney, N., Wing, J.S., Gould, S.J. and Loper, J.E. Characterization of the pyoluteorin biosynthetic gene cluster of Pseudomonas fluorescens Pf-5. J. Bacteriol. 181 (1999) 2166-2174. [PMID: 10094695]

2. Dorrestein, P.C., Yeh, E., Garneau-Tsodikova, S., Kelleher, N.L. and Walsh, C.T. Dichlorination of a pyrrolyl-S-carrier protein by FADH2-dependent halogenase PltA during pyoluteorin biosynthesis. Proc. Natl Acad. Sci. USA 102 (2005) 13843-13848. [PMID: 16162666]

3. Pang, A.H., Garneau-Tsodikova, S. and Tsodikov, O.V. Crystal structure of halogenase PltA from the pyoluteorin biosynthetic pathway. J. Struct. Biol. 192 (2015) 349-357. [PMID: 26416533]

[EC 1.14.19.56 created 2018]

EC 1.14.19.57

Accepted name: 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] brominase

Reaction: 1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + 3 FADH2 + 3 bromide + 3 O2 = 3,4,5-tribromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + 3 FAD + 6 H2O (overall reaction)
(1a) 1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FADH2 + bromide + O2 = 5-bromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FAD + 2 H2O
(1b) 5-bromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FADH2 + bromide + O2 = 4,5-dibromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FAD + 2 H2O
(1c) 4,5-dibromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FADH2 + bromide + O2 = 3,4,5-tribromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FAD + 2 H2O

Other name(s): bmp2 (gene name)

Systematic name: 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein]:FADH2 oxidoreductase (brominating)

Comments: The enzyme, characterized from marine bacteria of the Pseudoalteromonas genus, belongs to a family of FAD-dependent halogenases that act on acyl-carrier protein-tethered substrates. It catalyses three successive rounds of bromination. While the order has not been verified, it is believed to resemble that of EC 1.14.19.56, S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] chlorinase, due to significant sequence homology. Reduced FAD is provided in situ by a dedicated reductase and diffuses into the active site, where it reacts with the oxygen and bromide ion, resulting in formation of a bromoamine intermediate on a catalytic lysine side chain, and the eventual transfer of the bromide to the substrate. The enzyme from Pseudoalteromonas luteoviolacea 2ta16 is specific for bromide and does not accept chloride.

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

References:

1. Agarwal, V., El Gamal, A.A., Yamanaka, K., Poth, D., Kersten, R.D., Schorn, M., Allen, E.E. and Moore, B.S. Biosynthesis of polybrominated aromatic organic compounds by marine bacteria. Nat. Chem. Biol. 10 (2014) 640-647. [PMID: 24974229]

[EC 1.14.19.57 created 2018]

EC 1.14.19.58

Accepted name: tryptophan 5-halogenase

Reaction: L-tryptophan + FADH2 + chloride + O2 + H+ = 5-chloro-L-tryptophan + FAD + 2 H2O

For diagram of reaction click here.

Other name(s): pyrH (gene name)

Systematic name: L-tryptophan:FADH2 oxidoreductase (5-halogenating)

Comments: A flavin-dependent halogenase. The enzyme from the bacterium Streptomyces rugosporus catalyses halogenation of the C-5 position of tryptophan during the biosynthesis of the antibiotic compound pyrroindomycin B. It utilizes molecular oxygen to oxidize the FADH2 cofactor, giving C4a-hydroperoxyflavin, which then reacts with chloride to produce a hypochlorite ion. The latter reacts with an active site lysine to generate a chloramine, which chlorinates the substrate. cf. EC 1.14.19.59, tryptophan 6-halogenase and EC 1.14.19.9, tryptophan 7-halogenase.

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

References:

1. Zehner, S., Kotzsch, A., Bister, B., Sussmuth, R.D., Mendez, C., Salas, J.A. and van Pee, K.H. A regioselective tryptophan 5-halogenase is involved in pyrroindomycin biosynthesis in Streptomyces rugosporus LL-42D005. Chem. Biol. 12 (2005) 445-452. [PMID: 15850981]

2. Zhu, X., De Laurentis, W., Leang, K., Herrmann, J., Ihlefeld, K., van Pee, K.H. and Naismith, J.H. Structural insights into regioselectivity in the enzymatic chlorination of tryptophan. J. Mol. Biol. 391 (2009) 74-85. [PMID: 19501593]

[EC 1.14.19.58 created 2018]

EC 1.14.19.59

Accepted name: tryptophan 6-halogenase

Reaction: (1) L-tryptophan + FADH2 + chloride + O2 + H+ = 6-chloro-L-tryptophan + FAD + 2 H2O
(2) D-tryptophan + FADH2 + chloride + O2 + H+ = 6-chloro-D-tryptophan + FAD + 2 H2O

Other name(s): sttH (gene name); thdH (gene name)

Systematic name: L-tryptophan:FADH2 oxidoreductase (6-halogenating)

Comments: The enzyme is a flavin-dependent halogenase that has been described from several bacterial species. It utilizes molecular oxygen to oxidize the FADH2 cofactor, giving C4a-hydroperoxyflavin, which then reacts with chloride to produce a hypochlorite ion. The latter reacts with an active site lysine to generate a chloramine, which chlorinates the substrate. cf. EC 1.14.19.58, tryptophan 5-halogenase, and EC 1.14.19.9, tryptophan 7-halogenase.

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

References:

1. Zeng, J. and Zhan, J. Characterization of a tryptophan 6-halogenase from Streptomyces toxytricini. Biotechnol. Lett. 33 (2011) 1607-1613. [PMID: 21424165]

2. Milbredt, D., Patallo, E.P. and van Pee, K.H. A tryptophan 6-halogenase and an amidotransferase are involved in thienodolin biosynthesis. Chembiochem 15 (2014) 1011-1020. [PMID: 24692213]

3. Shepherd, S.A., Menon, B.R., Fisk, H., Struck, A.W., Levy, C., Leys, D. and Micklefield, J. A structure-guided switch in the regioselectivity of a tryptophan halogenase. Chembiochem 17 (2016) 821-824. [PMID: 26840773]

[EC 1.14.19.59 created 2018]

EC 1.14.19.60

Accepted name: 7-chloro-L-tryptophan 6-halogenase

Reaction: 7-chloro-L-tryptophan + FADH2 + chloride + O2 + H+ = 6,7-dichloro-L-tryptophan + FAD + 2 H2O

For diagram of reaction click here.

Other name(s): ktzR (gene name)

Systematic name: 7-chloro-L-tryptophan:FADH2 oxidoreductase (6-halogenating)

Comments: An FAD-dependent halogenase. The enzyme, characterized from the bacterium Kutzneria sp. 744, works in tandem with EC 1.14.19.9, tryptophan 7-halogenase, (ktzQ) to generate 6,7-dichloro-L-tryptophan, which is incorporated as a pyrroloindoline in the kutznerides family of natural products. It has a 120-fold preference for 7-chloro-L-tryptophan over L-tryptophan as substrate.

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

References:

1. Heemstra, J.R., Jr. and Walsh, C.T. Tandem action of the O2- and FADH2-dependent halogenases KtzQ and KtzR produce 6,7-dichlorotryptophan for kutzneride assembly. J. Am. Chem. Soc. 130 (2008) 14024-14025. [PMID: 18828589]

[EC 1.14.19.60 created 2018]

EC 1.14.19.61

Accepted name: dihydrorhizobitoxine desaturase

Reaction: dihydrorhizobitoxine + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = rhizobitoxine + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O

Glossary: dihydrorhizobitoxine = (2S)-2-amino-4-[(2R)-2-amino-3-hydroxypropoxy]butanoate
rhizobitoxine = (2S,3E)-2-amino-4-[(2R)-2-amino-3-hydroxypropoxy]but-3-enoate

Other name(s): rtxC (gene name)

Systematic name: dihydrorhizobitoxine,ferredoxin:oxygen oxidoreductase (3,4 trans-dehydrogenating)

Comments: The enzyme, characterized from the bacterium Bradyrhizobium elkanii, catalyses the final step in the biosynthesis of the nodulation enhancer compound rhizobitoxine.

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

References:

1. Yasuta, T., Okazaki, S., Mitsui, H., Yuhashi, K., Ezura, H. and Minamisawa, K. DNA sequence and mutational analysis of rhizobitoxine biosynthesis genes in Bradyrhizobium elkanii. Appl. Environ. Microbiol. 67 (2001) 4999-5009. [PMID: 11679318]

2. Okazaki, S., Sugawara, M. and Minamisawa, K. Bradyrhizobium elkanii rtxC gene is required for expression of symbiotic phenotypes in the final step of rhizobitoxine biosynthesis. Appl. Environ. Microbiol. 70 (2004) 535-541. [PMID: 14711685]

[EC 1.14.19.61 created 2018]

EC 1.14.19.62

Accepted name: secologanin synthase

Reaction: loganin + [reduced NADPH—hemoprotein reductase] + O2 = secologanin + [oxidized NADPH—hemoprotein reductase] + 2 H2O

For diagram of reaction click here.

Systematic name: loganin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ring-cleaving)

Comments: A P-450 (heme-thiolate) protein. Secologanin is the precursor of the monoterpenoid indole alkaloids and ipecac alkaloids.

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

References:

1. Yamamoto, H., Katano, N., Ooi, Y. and Inoue, K. Transformation of loganin and 7-deoxyloganin into secologanin by Lonicera japonica cell suspension cultures. Phytochemistry 50 (1999) 417-422.

2. Yamamoto, H., Katano, N., Ooi, A. and Inoue, K. Secologanin synthase which catalyzes the oxidative cleavage of loganin into secologanin is a cytochrome P-450. Phytochemistry 53 (2000) 7-12. [PMID: 10656401]

3. Irmler, S., Schroder, G., St-Pierre, B., Crouch, N.P., Hotze, M., Schmidt, J., Strack, D., Matern, U. and Schroder, J. Indole alkaloid biosynthesis in Catharanthus roseus: new enzyme activities and identification of cytochrome P-450 CYP72A1 as secologanin synthase. Plant J. 24 (2000) 797-804. [PMID: 11135113]

[EC 1.14.19.62 created 2002 as EC 1.3.3.9, transferred 2018 to EC 1.14.19.62]

EC 1.14.19.63

Accepted name: pseudobaptigenin synthase

Reaction: (1) calycosin + [reduced NADPH—hemoprotein reductase] + O2 = pseudobaptigenin + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(2) pratensein + [reduced NADPH-hemoprotein reductase] + O2 = 5-hydroxypseudobaptigenin + [oxidized NADPH—hemoprotein reductase] + 2 H2O

Glossary: calycosin = 3'-hydroxyformononetin
pratensein = 3'-hydroxybiochanin A

Systematic name: calycosin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (methylenedioxy-bridge-forming)

Comments: A cytochrome P-450 (heme-thiolate) enzyme catalysing an oxidative reaction that does not incorporate oxygen into the product. Catalyses a step in the biosynthesis of (–)-maackiain, the main pterocarpan phytoalexin in chickpea (Cicer arietinum).

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

References:

1. Clemens S., Barz W. Cytochrome P450-dependent methylenedioxy bridge formation in Cicer arietinum. Phytochemistry 41 (1996) 457-460.

[EC 1.14.19.63 created 2011 as EC 1.14.21.8, transferred 2018 to EC 1.14.19.63]

EC 1.14.19.64

Accepted name: (S)-stylopine synthase

Reaction: (S)-cheilanthifoline + [reduced NADPH—hemoprotein reductase] + O2 = (S)-stylopine + [oxidized NADPH—hemoprotein reductase] + 2 H2O

For diagram of reaction click here.

Other name(s): (S)-cheilanthifoline oxidase (methylenedioxy-bridge-forming)

Systematic name: (S)-cheilanthifoline,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (methylenedioxy-bridge-forming)

Comments: A cytochrome P-450 (heme-thiolate) protein catalysing an oxidative reaction that does not incorporate oxygen into the product. Forms the second methylenedioxy bridge of the protoberberine alkaloid stylopine from oxidative ring closure of adjacent phenolic and methoxy groups of cheilanthifoline.

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

References:

1. Bauer, W. and Zenk, M.H. Two methylenedioxy bridge-forming cytochrome P-450 dependent enzymes are involved in (S)-stylopine biosynthesis. Phytochemistry 30 (1991) 2953-2961.

[EC 1.14.19.64 created 1999 as EC 1.1.3.32, transferred 2002 to EC 1.14.21.1, transferred 2018 to EC 1.14.19.64]

EC 1.14.19.65

Accepted name: (S)-cheilanthifoline synthase

Reaction: (S)-scoulerine + [reduced NADPH—hemoprotein reductase] + O2 = (S)-cheilanthifoline + [oxidized NADPH—hemoprotein reductase] + 2 H2O

For diagram of reaction click here.

Other name(s): CYP719A14 (gene name); (S)-scoulerine oxidase (methylenedioxy-bridge-forming) (ambiguous); (S)-scoulerine,NADPH:oxygen oxidoreductase (methylenedioxy-bridge-forming) (ambiguous)

Systematic name: (S)-scoulerine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase [(S)-cheilanthifoline-forming]

Comments: A cytochrome P-450 (heme-thiolate) protein catalysing an oxidative reaction that does not incorporate oxygen into the product. Forms the methylenedioxy bridge of the protoberberine alkaloid cheilanthifoline by the oxidative ring closure of adjacent phenolic and methoxy groups of scoulerine. cf. EC 1.14.19.73, (S)-nandinine synthase, which catalyses a similar reaction at the other side of the (S)-scoulerine molecule, forming (S)-nandinine.

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

References:

1. Bauer, W. and Zenk, M.H. Two methylenedioxy bridge-forming cytochrome P-450 dependent enzymes are involved in (S)-stylopine biosynthesis. Phytochemistry 30 (1991) 2953-2961.

2. Diaz Chavez, M.L., Rolf, M., Gesell, A. and Kutchan, T.M. Characterization of two methylenedioxy bridge-forming cytochrome P450-dependent enzymes of alkaloid formation in the Mexican prickly poppy Argemone mexicana. Arch. Biochem. Biophys. 507 (2011) 186-193. [PMID: 21094631]

[EC 1.14.19.65 created 1999 as EC 1.1.3.33, transferred 2002 to EC 1.14.21.2, modified 2016, transferred 2018 to EC 1.14.19.65]

EC 1.14.19.66

Accepted name: berbamunine synthase

Reaction: (S)-N-methylcoclaurine + (R)-N-methylcoclaurine + [reduced NADPH—hemoprotein reductase] + O2 = berbamunine + [oxidized NADPH—hemoprotein reductase] + 2 H2O

For diagram of reaction click here.

Other name(s): (S)-N-methylcoclaurine oxidase (C-O phenol-coupling)

Systematic name: (S)-N-methylcoclaurine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (C-O phenol-coupling)

Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. Forms the bisbenzylisoquinoline alkaloid berbamunine by phenol oxidation of N-methylcoclaurine without the incorporation of oxygen into the product. Reaction of two molecules of (R)-N-methylcoclaurine gives the dimer guattagaumerine.

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

References:

1. Stadler, R. and Zenk, M.H. The purification and characterization of a unique cytochrome P-450 enzyme from Berberis stolifera plant cell cultures. J. Biol. Chem. 268 (1993) 823-831. [PMID: 8380416]

[EC 1.14.19.66 created 1999 as EC 1.1.3.34, transferred 2002 to EC 1.14.21.3, transferred 2018 to EC 1.14.19.66]

EC 1.14.19.67

Accepted name: salutaridine synthase

Reaction: (R)-reticuline + [reduced NADPH—hemoprotein reductase] + O2 = salutaridine + [oxidized NADPH—hemoprotein reductase] + 2 H2O

For diagram of reaction click here.

Other name(s): (R)-reticuline oxidase (C-C phenol-coupling)

Systematic name: (R)-reticuline,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (C-C phenol-coupling)

Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. Forms the morphinan alkaloid salutaridine by intramolecular phenol oxidation of reticuline without the incorporation of oxygen into the product.

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

References:

1. Gerady, R. and Zenk, M.H. Formation of salutaridine from (R)-reticuline by a membrane-bound cytochrome P-450 enzyme from Papaver somniferum. Phytochemistry 32 (1993) 79-86.

[EC 1.14.19.67 created 1999 as EC 1.1.3.35, transferred 2002 to EC 1.14.21.4, transferred 2018 to EC 1.14.19.67]

EC 1.14.19.68

Accepted name: (S)-canadine synthase

Reaction: (S)-tetrahydrocolumbamine + [reduced NADPH—hemoprotein reductase] + O2 = (S)-canadine + [oxidized NADPH—hemoprotein reductase] + 2 H2O

For diagram of reaction click here.

Other name(s): (S)-tetrahydroberberine synthase; (S)-tetrahydrocolumbamine oxidase (methylenedioxy-bridge-forming); CYP719A (gene name)

Systematic name: (S)-tetrahydrocolumbamine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (methylenedioxy-bridge-forming)

Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. The enzyme catalyses an oxidative reaction that does not incorporate oxygen into the product. Oxidation of the methoxyphenol group of the alkaloid tetrahydrocolumbamine results in the formation of the methylenedioxy bridge of canadine.

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

References:

1. Rueffer, M. and Zenk, M.H. Canadine synthase from Thalictrum tuberosum cell cultures catalyses the formation of the methylenedioxy bridge in berberine synthesis. Phytochemistry 36 (1994) 1219-1223.

2. Ikezawa, N., Tanaka, M., Nagayoshi, M., Shinkyo, R., Sakaki, T., Inouye, K. and Sato, F. Molecular cloning and characterization of CYP719, a methylenedioxy bridge-forming enzyme that belongs to a novel P450 family, from cultured Coptis japonica cells. J. Biol. Chem 278 (2003) 38557-38565. [PMID: 12732624]

3. Dang, T.T. and Facchini, P.J. Cloning and characterization of canadine synthase involved in noscapine biosynthesis in opium poppy. FEBS Lett. 588 (2014) 198-204. [PMID: 24316226]

[EC 1.14.19.68 created 1999 as EC 1.1.3.36, transferred 2002 to EC 1.14.21.5, transferred 2018 to EC 1.14.19.68]

EC 1.14.19.69

Accepted name: biflaviolin synthase

Reaction: (1) 2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 3,3'-biflaviolin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
(2) 2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 3,8'-biflaviolin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O

For diagram of reaction click here.

Glossary: flaviolin = 4,5,7-trihydroxynaphthalene-1,2-dione
3,3'-biflaviolin = 3,3',6,6',8,8'-hexahydroxy-2,2'-binaphthalene-1,1',4,4'-tetraone
3,8'-biflaviolin = 2,3',4,6',7,8'-hexahydroxy-1,2'-binaphthalene-1',4',5,8-tetraone

Other name(s): CYP158A2 (gene name); cytochrome P450 158A2

Systematic name: flaviolin,reduced ferredoxin:oxygen oxidoreductase

Comments: This cytochrome-P-450 (heme-thiolate) enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyses a phenol oxidation C-C coupling reaction, which results in the polymerization of flaviolin to form biflaviolin or triflaviolin without the incorporation of oxygen into the product [1,3]. The products are highly conjugated pigments that protect the bacterium from the deleterious effects of UV irradiation [1].

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

References:

1. Zhao, B., Guengerich, F.P., Bellamine, A., Lamb, D.C., Izumikawa, M., Lei, L., Podust, L.M., Sundaramoorthy, M., Kalaitzis, J.A., Reddy, L.M., Kelly, S.L., Moore, B.S., Stec, D., Voehler, M., Falck, J.R., Shimada, T. and Waterman, M.R. Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2. J. Biol. Chem. 280 (2005) 11599-11607. [PMID: 15659395]

2. Zhao, B., Guengerich, F.P., Voehler, M. and Waterman, M.R. Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer. J. Biol. Chem. 280 (2005) 42188-42197. [PMID: 16239228]

3. Zhao, B., Lamb, D.C., Lei, L., Kelly, S.L., Yuan, H., Hachey, D.L. and Waterman, M.R. Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2. Biochemistry 46 (2007) 8725-8733. [PMID: 17614370]

[EC 1.14.19.69 created 2008 as EC 1.14.21.7, transferred 2018 to EC 1.14.19.69]

EC 1.14.19.70

Accepted name: mycocyclosin synthase

Reaction: cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O

For diagram of reaction click here.

Glossary: mycocyclosin = (1S,14S)-6,9-dihydroxy-15,17-diazatetracyclo[12.2.2.13,7.18,12]icosa-3(20),4,6,8(19),9,11-hexaene-16,18-dione

Other name(s): CYP121; rv2276 (gene name)

Systematic name: cyclo(L-tyrosyl-L-tyrosyl),reduced ferredoxin:oxygen oxidoreductase (diarylbridge-forming)

Comments: A cytochrome P-450 (heme-thiolate) protein from the bacterium Mycobacterium tuberculosis catalysing an oxidative reaction that does not incorporate oxygen into the product.

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

References:

1. Belin, P., Le Du, M.H., Fielding, A., Lequin, O., Jacquet, M., Charbonnier, J.B., Lecoq, A., Thai, R., Courcon, M., Masson, C., Dugave, C., Genet, R., Pernodet, J.L. and Gondry, M. Identification and structural basis of the reaction catalyzed by CYP121, an essential cytochrome P450 in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 106 (2009) 7426-7431. [PMID: 19416919]

[EC 1.14.19.70 created 2013 as EC 1.14.21.9, transferred 2018 to EC 1.14.19.70]

EC 1.14.19.71

Accepted name: fumitremorgin C synthase

Reaction: tryprostatin A + [reduced NADPH—hemoprotein reductase] + O2 = fumitremorgin C + [oxidized NADPH—hemoprotein reductase] + 2 H2O

For diagram of reaction click here.

Glossary: tryprostatin A = (3S,8aS)-3-{[6-methoxy-2-(3-methylbut-2-en-1-yl)-1H-indol-3-yl]methyl}hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
fumitremorgin C = (5aS,12S,14aS)-9-methoxy-12-(2-methylprop-1-en-1-yl)-1,2,3,5a,6,11,12,14a-octahydro-5H,14H-pyrrolo[1'',2'':4',5']pyrazino[1',2':1,6]pyrido[3,4-b]indole-5,14-dione

Other name(s): ftmE (gene name)

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

Comments: A cytochrome P-450 (heme-thiolate) protein. The protein from the fungus Aspergillus fumigatus also has activity with tryprostatin B forming demethoxyfumitremorgin C. Involved in the biosynthetic pathways of several indole alkaloids such as fumitremorgins and verruculogen.

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

References:

1. Kato, N., Suzuki, H., Takagi, H., Asami, Y., Kakeya, H., Uramoto, M., Usui, T., Takahashi, S., Sugimoto, Y. and Osada, H. Identification of cytochrome P450s required for fumitremorgin biosynthesis in Aspergillus fumigatus. ChemBioChem. 10 (2009) 920-928. [PMID: 19226505]

[EC 1.14.19.71 created 2013 as EC 1.14.21.10, transferred 2018 to EC 1.14.19.71]

EC 1.14.19.72

Accepted name: (–)-pluviatolide synthase

Reaction: (–)-matairesinol + [reduced NADPH—hemoprotein reductase] + O2 = (–)-pluviatolide + [oxidized NADPH—hemoprotein reductase] + 2 H2O

For diagram of reaction click here.

Glossary: (–)-matairesinol = 3R,4R)-3,4-bis[(4-hydroxy-3-methoxyphenyl)methyl]oxolan-2-one
(–)-pluviatolide = ((3R,4R)-4-(2H-1,3-benzodioxol-5-ylmethyl)-3-[(4-hydroxy-3-methoxyphenyl)methyl]oxolan-2-one

Other name(s): CYP719A23 (gene name)

Systematic name: (–)-matairesinol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (methylenedioxy-bridge-forming)

Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from the plants Sinopodophyllum hexandrum and Podophyllum peltatum catalyses the formation of a methylenedioxy-bridge. It is involved in the biosynthesis of podophyllotoxin, a non-alkaloid toxin lignan whose derivatives are important anticancer drugs.

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

References:

1. Marques, J.V., Kim, K.W., Lee, C., Costa, M.A., May, G.D., Crow, J.A., Davin, L.B. and Lewis, N.G. Next generation sequencing in predicting gene function in podophyllotoxin biosynthesis. J. Biol. Chem. 288 (2013) 466-479. [PMID: 23161544]

[EC 1.14.19.72 created 2016 as EC 1.14.21.11, transferred 2018 to EC 1.14.19.72]

EC 1.14.19.73

Accepted name: (S)-nandinine synthase

Reaction: (S)-scoulerine + [reduced NADPH—hemoprotein reductase] + O2 = (S)-nandinine + [oxidized NADPH—hemoprotein reductase] + 2 H2O

For diagram of reaction click here.

Glossary: (S)-scoulerine = (13aS)-3,10-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquino[3,2-a]isoquinoline-2,9-diol
(S)-cheilanthifoline = (6aS)-9-methoxy-6,11,12,14-tetrahydro-2H,6aH-[1,3]dioxolo[4,5-h]isoquino[2,1-b]isoquinolin-8-ol

Other name(s): CYP719A3

Systematic name: (S)-scoulerine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase [(S)-nandinine-forming]

Comments: A cytochrome P-450 (heme-thiolate) enzyme found in plants. The enzyme catalyses an oxidative reaction that does not incorporate oxygen into the product. Forms the methylenedioxy bridge of the protoberberine alkaloid (S)-nandinine by the oxidative ring closure of adjacent phenolic and methoxy groups of (S)-scoulerine. cf. EC 1.14.19.65, (S)-cheilanthifoline synthase, which catalyses a similar reaction at the other side of the (S)-scoulerine molecule, forming (S)-cheilanthifoline.

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

References:

1. Ikezawa, N., Iwasa, K. and Sato, F. Molecular cloning and characterization of methylenedioxy bridge-forming enzymes involved in stylopine biosynthesis in Eschscholzia californica. FEBS J. 274 (2007) 1019-1035. [PMID: 17250743]

2. Diaz Chavez, M.L., Rolf, M., Gesell, A. and Kutchan, T.M. Characterization of two methylenedioxy bridge-forming cytochrome P450-dependent enzymes of alkaloid formation in the Mexican prickly poppy Argemone mexicana. Arch. Biochem. Biophys. 507 (2011) 186-193. [PMID: 21094631]

[EC 1.14.19.73 created 2016 as EC 1.14.21.12, transferred 2018 to EC 1.14.19.73]

EC 1.14.19.74

Accepted name: (+)-piperitol/(+)-sesamin synthase

Reaction: (1) (+)-pinoresinol + [reduced NADPH-hemoprotein reductase]l + O2 = (+)-piperitol + [oxidized NADPH-hemoprotein reductase] + 2 H2O
(2) (+)-piperitol + [reduced NADPH-hemoprotein reductase] + O2 = (+)-sesamin + [oxidized NADPH-hemoprotein reductase] + 2 H2O

For diagram of reaction click here.

Other name(s): CYP81Q1; CYP81Q2; PS; PSS; SS; piperitol synthase; sesamin synthase

Systematic name: (+)-pinoresinol,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (cyclizing)

Comments: A cytochrome P-450 (heme-thiolate) protein. Isolated from Sesamum indicum (sesame) and S. radiatum (black sesame).

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

References:

1. Ono, E., Nakai, M., Fukui, Y., Tomimori, N., Fukuchi-Mizutani, M., Saito, M., Satake, H., Tanaka, T., Katsuta, M., Umezawa, T. and Tanaka, Y. Formation of two methylenedioxy bridges by a Sesamum CYP81Q protein yielding a furofuran lignan, (+)-sesamin. Proc. Natl Acad. Sci. USA 103 (2006) 10116-10121. [PMID: 16785429]

[EC 1.14.19.74 created 2018]

EC 1.14.19.75

Accepted name: very-long-chain acyl-lipid ω-9 desaturase

Reaction: (1) 1-hexacosanoyl-2-acyl-[phosphoglycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = 1-[(17Z)-hexacos-17-enoyl]-2-acyl-[phosphoglycerolipid] + 2 ferricytochrome b5 + 2 H2O
(2) 1-tetracosanoyl-2-acyl-[phosphoglycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = 1-[(15Z)-tetracos-15-enoyl]-2-acyl-[phosphoglycerolipid] + 2 ferricytochrome b5 + 2 H2O

Other name(s): ADS2 (gene name)

Systematic name: very-long-chain acyl-[glycerolipid],ferrocytochrome b5:oxygen oxidoreductase (ω98-cis-dehydrogenating)

Comments: The enzyme, characterized from the plant Arabidopsis thaliana, acts on both 24:0 and 26:0 fatty acids, introducing a cis double bond at a position 9 carbons from the methyl end. These very-long-chain fatty acids are found as a minor component of seed lipids, but also in the membrane phosphatidylethanolamine and phosphatidylserine, in sphingolipids, as precursors and components of cuticular and epicuticular waxes, and in suberin.

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

References:

1. Fukuchi-Mizutani, M., Tasaka, Y., Tanaka, Y., Ashikari, T., Kusumi, T. and Murata, N. Characterization of δA9 acyl-lipid desaturase homologues from Arabidopsis thaliana. Plant Cell Physiol 39 (1998) 247-253. [PMID: 9559566]

2. Smith, M.A., Dauk, M., Ramadan, H., Yang, H., Seamons, L.E., Haslam, R.P., Beaudoin, F., Ramirez-Erosa, I. and Forseille, L. Involvement of Arabidopsis acyl-coenzyme A desaturase-like2 (At2g31360) in the biosynthesis of the very-long-chain monounsaturated fatty acid components of membrane lipids. Plant Physiol. 161 (2013) 81-96. [PMID: 23175755]

[EC 1.14.19.75 created 2018]

EC 1.14.19.76

Accepted name: flavone synthase II

Reaction: a flavanone + [reduced NADPH—hemoprotein reductase] + O2 = a flavone + [oxidized NADPH—hemoprotein reductase] + 2 H2O

For diagram of reaction click here.

Other name(s): CYP93B16 (gene name); CYP93G1 (gene name); FNS II

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

Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. The rice enzyme channels flavanones to the biosynthesis of tricin O-linked conjugates. cf. EC 1.14.20.5, flavone synthase I.

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

References:

1. Martens, S. and Forkmann, G. Cloning and expression of flavone synthase II from Gerbera hybrids. Plant J. 20 (1999) 611-618. [PMID: 10652133]

2. Fliegmann, J., Furtwangler, K., Malterer, G., Cantarello, C., Schuler, G., Ebel, J. and Mithofer, A. Flavone synthase II (CYP93B16) from soybean (Glycine max L.). Phytochemistry 71 (2010) 508-514. [PMID: 20132953]

3. Lam, P.Y., Zhu, F.Y., Chan, W.L., Liu, H. and Lo, C. Cytochrome P450 93G1 is a flavone synthase II that channels flavanones to the biosynthesis of tricin O-linked conjugates in rice. Plant Physiol. 165 (2014) 1315-1327. [PMID: 24843076]

[EC 1.14.19.76 created 2018]


Continued with EC 1.14.20 and EC 1.14.21
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