Continued from EC 1.14.19.1-50
EC 1.14.19.1 to EC 1.14.19.50
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]
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]
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]
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]
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]
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 + 2 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, PDB, 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]
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]
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]
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]
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]
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]
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]
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.
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.
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]
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]
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.
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]
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, PDB, 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]
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, PDB, 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]
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]
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]
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]
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]
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 (ω9,ω8-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]
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]
Accepted name: plasmanylethanolamine desaturase
Reaction: a plasmanylethanolamine + 2 ferrocytochrome b5 + O2 + 2 H+ = a plasmenylethanolamine + 2 ferricytochrome b5 + 2 H2O
Glossary: a plasmanylethanolamine = a 2-acyl-1-alkyl-sn-glycero-3-phosphoethanolamine
Other name(s): TMEM189 (gene name); 2-acyl-1-alkyl-sn-glycero-3-phosphoethanolamine desaturase; alkylacylglycerophosphoethanolamine desaturase; alkylacylglycero-phosphorylethanolamine dehydrogenase; alkyl-acylglycerophosphorylethanolamine dehydrogenase; 1-O-alkyl-2-acyl-sn-glycero-3-phosphorylethanolamine desaturase; 1-O-alkyl 2-acyl-sn-glycero-3-phosphorylethanolamine desaturase
Systematic name: plasmanylethanolamine,ferrocytochrome b5:oxygen oxidoreductase (plasmenylethanolamine-forming)
Comments: The enzyme catalyses the introduction of a double bond at position 1 of the alkyl group attached by an ether bond at the sn-1 position of plasmanylethanolamine, generating a vinyl ether-containing plasmenylethanolamine. The enzyme is found in animals and some bacteria, but not in plants, fungi, or most aerobic bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Stoffel, W. and LeKim, D. Studies on the biosynthesis of plasmalogens. Precursors in the biosynthesis of plasmalogens: on the stereospecificity of the biochemical dehydrogenation of the 1-O-alkyl glyceryl to the 1-O-alk-1'-enyl glyceryl ether bond. Hoppe-Seylers Z. Physiol. Chem. 352 (1971) 501-511. [PMID: 5550967]
2. Paltauf, F. Biosynthesis of plasmalogens from alkyl- and alkyl-acyl-glycerophosphoryl ethanolamine in the rat brain. FEBS Lett. 17 (1971) 118-120. [PMID: 11946011]
3. Paltuaf, F., Prough, R.A., Masters, B.S. and Johnston, J.M. Evidence for the participation of cytochrome b5 in plasmalogen biosynthesis. J. Biol. Chem. 249 (1974) 2661-2662. [PMID: 4150797]
4. Wykle, R.L. and Schremmer Lockmiller, J.M. The biosynthesis of plasmalogens by rat brain: involvement of the microsomal electron transport system. Biochim. Biophys. Acta 380 (1975) 291-298. [PMID: 235322]
5. Gallego-Garcia, A., Monera-Girona, A.J., Pajares-Martinez, E., Bastida-Martinez, E., Perez-Castano, R., Iniesta, A.A., Fontes, M., Padmanabhan, S. and Elias-Arnanz, M. A bacterial light response reveals an orphan desaturase for human plasmalogen synthesis. Science 366 (2019) 128-132. [PMID: 31604315]
Accepted name: decanoyl-[acyl-carrier protein] acetylenase
Reaction: decanoyl-[acyl-carrier protein] + 4 reduced ferredoxin [iron-sulfur] cluster + 2 O2 + 4 H+ = dec-9-ynoyl-[acyl-carrier protein] + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O (overall reaction)
(1a) decanoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = dec-9-enoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
(1b) dec-9-enoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = dec-9-ynoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Other name(s): ttuB (gene name) (ambiguous)
Systematic name: decanoyl-[acyl-carrier protein],reduced ferredoxin:oxygen oxidoreductase (9,10-dehydrogenating)
Comments: The enzyme, characterized from the bacterium Teredinibacter turnerae, is specific for decanoyl-[acyl-carrier protein]. Activity is maximal when decanoate is loaded onto a dedicated acyl-carrier protein (TtuC), which is encoded by a gene in the same operon.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Zhu, X., Su, M., Manickam, K. and Zhang, W. Bacterial genome mining of enzymatic tools for alkyne biosynthesis. ACS Chem. Biol. 10 (2015) 2785-2793. [PMID: 26441143]
Accepted name: 3β,22α-dihydroxysteroid 3-dehydrogenase
Reaction: (1) (22S)-22-hydroxycampesterol + [reduced NADPH-hemoprotein reductase] + O2 = (22S)-22-hydroxycampest-4-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
(2) 6-deoxoteasterone + [reduced NADPH-hemoprotein reductase] + O2 = 3-dehydro-6-deoxoteasterone + [oxidized NADPH-hemoprotein reductase] + 2 H2O
Glossary: 6-deoxoteasterone = (22R,23R)-5α-campestane-3β,22,23-triol
Other name(s): CYP90A1 (gene name)
Systematic name: 3β,22α-dihydroxysteroid,[reduced NADPH-hemoprotein reductase]:oxygen 3-oxidoreductase
Comments: This cytochrome P-450 (heme-thiolate) enzyme, characterized from the plant Arabidopsis thaliana, catalyses C-3 dehydrogenation of all 3β-hydroxy brassinosteroid synthesis intermediates with 22-hydroxylated or 22,23-dihydroxylated side chains.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Ohnishi, T., Godza, B., Watanabe, B., Fujioka, S., Hategan, L., Ide, K., Shibata, K., Yokota, T., Szekeres, M. and Mizutani, M. CYP90A1/CPD, a brassinosteroid biosynthetic cytochrome P450 of Arabidopsis, catalyzes C-3 oxidation. J. Biol. Chem. 287 (2012) 31551-31560. [PMID: 22822057]
Accepted name: (19E)-geissoschizine oxidase
Reaction: (19E)-geissoschizine + O2 + [reduced NADPH-hemoprotein reductase] = akuammicine + formate + H2O + [oxidized NADPH-hemoprotein reductase] (overall reaction)
(1a) (19E)-geissoschizine + O2 + [reduced NADPH-hemoprotein reductase] = 3,17-didehydrostemmadenine + 2 H2O + [oxidized NADPH-hemoprotein reductase]
(1b) 3,17-didehydrostemmadenine = 17-dehydropreakuammicine (spontaneous)
(1c) 17-dehydropreakuammicine + H2O = 17-dehydropreakuammicine hydrate (spontaneous)
(1d) 17-dehydropreakuammicine hydrate = akuammicine + formate (spontaneous)
For diagram of reaction, click here and mechanism click here
Glossary: (19E)-geissoschizine = methyl (16ξ,19E)-16-formylcoryn-19-en-17-oate
Other name(s): GO (gene name); CYP71D1V1 (gene name)
Systematic name: (19E)-geissoschizine,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (akuammicine-forming)
Comments: A cytochrome P-450 (heme-thiolate) enzyme characterized from the plant Catharanthus roseus (Madagascar periwinkle), that participates in the biosynthesis of a number of monoterpene alkaloids, as well as the bisindole alkaloids vinblastine and vincristine. The enzyme generates a nine-carbon ring that contains a nitrogen atom. The direct product of the enzyme, 3,17-didehydrostemmadenine, is unstable, and in the absence of other enzymes becomes akuammicine non-enzymically. However, in the presence of two dehydrogenases it is converted to stemmadenine via 17-dehydrostemmadenine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Tatsis, E.C., Carqueijeiro, I., Duge de Bernonville, T., Franke, J., Dang, T.T., Oudin, A., Lanoue, A., Lafontaine, F., Stavrinides, A.K., Clastre, M., Courdavault, V. and O'Connor, S.E. A three enzyme system to generate the Strychnos alkaloid scaffold from a central biosynthetic intermediate. Nat. Commun. 8 (2017) 316. [PMID: 28827772]
2. Qu, Y., Easson, M.EA.M., Simionescu, R., Hajicek, J., Thamm, A.MK., Salim, V. and De Luca, V. Solution of the multistep pathway for assembly of corynanthean, strychnos, iboga, and aspidosperma monoterpenoid indole alkaloids from 19E-geissoschizine. Proc. Natl. Acad. Sci. USA 115 (2018) 3180-3185. [PMID: 29511102]
3. Salim, V., Jarecki, S.A., Vick, M. and Miller, R. Advances in metabolic engineering of plant monoterpene indole alkaloids. Biology (Basel) 12 (2023) . [PMID: 37626942]
Accepted name: polyneuridine aldehyde synthase
Reaction: (19E)-geissoschizine + [oxidized NADPH—hemoprotein reductase] + O2 = polyneuridine aldehyde + [reduced NADPH—hemoprotein reductase] + 2 H2O
For diagram of reaction click here
Other name(s): SBE (gene name); sarpagan bridge enzyme; CYP71AY4; CYP71AY5
Systematic name: (19E)-geissoschizine:[oxidized NADPH—hemoprotein reductase] oxidoreductase (polyneuridine aldehyde forming)
Comments: A heme-thiolate protein (P-450). The enzyme, characterized from the plants Rauwolfia serpentina (Indian snakeroot) and Gelsemium sempervirens (yellow jessamine), is involved in the biosynthesis of monoterpenoid indole alkaloids of the sarpagan, ajmalan and alstophyllan classes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Dang, T.T., Franke, J., Carqueijeiro, I.ST., Langley, C., Courdavault, V. and O'Connor, S.E. Sarpagan bridge enzyme has substrate-controlled cyclization and aromatization modes. Nat. Chem. Biol. 14 (2018) 760-763. [PMID: 29942076]