Continued from EC 1.14.14.51 to EC 1.14.14.100
EC 1.14 Acting on paired donors with incorporation of molecular oxygen
Continued from:
EC 1.14.14.1 to EC 1.1.1.50
EC 1.14.14.51 to EC 1.14.14.100
Accepted name: dihydrochelirubine 12-monooxygenase
Reaction: dihydrochelirubine + [reduced NADPH—hemoprotein reductase] + O2 = 12-hydroxydihydrochelirubine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): dihydrochelirubine 12-hydroxylase
Systematic name: dihydrochelirubine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from the plant Thalictrum bulgaricum.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kammerer, L., De-Eknamkul, W. and Zenk, M.H. Enzymic 12-hydroxylation and 12-O-methylation of dihydrochelirubine in dihydromacarpine formation by Thalictrum bulgaricum. Phytochemistry 36 (1994) 1409-1416.
Accepted name: N-methylcoclaurine 3'-monooxygenase
Reaction: (S)-N-methylcoclaurine + [reduced NADPH—hemoprotein reductase] + O2 = (S)-3'-hydroxy-N-methylcoclaurine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): N-methylcoclaurine 3'-hydroxylase; CYP80B1 (gene name)
Systematic name: (S)-N-methylcoclaurine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3'-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein involved in benzylisoquinoline alkaloid synthesis in higher plants.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Pauli, H.H. and Kutchan, T.M. Molecular cloning and functional heterologous expression of two alleles encoding (S)-N-methylcoclaurine 3'-hydroxylase (CYP80B1), a new methyl jasmonate-inducible cytochrome P-450-dependent mono-oxygenase of benzylisoquinoline alkaloid biosynthesis. Plant J. 13 (1998) 793-801. [PMID: 9681018]
Accepted name: tabersonine 16-hydroxylase
Reaction: tabersonine + [reduced NADPH—hemoprotein reductase] + O2 = 16-hydroxytabersonine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): tabersonine-11-hydroxylase; T11H; CYP71D12 (gene name)
Systematic name: tabersonine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (16-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from the plant Madagascar periwinkle (Catharanthus roseus).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. St-Pierre, B. and De Luca, V. A cytochrome-P-450 monooxygenase catalyzes the first step in the conversion of tabersonine to vindoline in Catharanthus roseus. Plant Physiol. 109 (1995) 131-139. [PMID: 12228585]
2. Besseau, S., Kellner, F., Lanoue, A., Thamm, A.M., Salim, V., Schneider, B., Geu-Flores, F., Hofer, R., Guirimand, G., Guihur, A., Oudin, A., Glevarec, G., Foureau, E., Papon, N., Clastre, M., Giglioli-Guivarc'h, N., St-Pierre, B., Werck-Reichhart, D., Burlat, V., De Luca, V., O'Connor, S.E. and Courdavault, V. A pair of tabersonine 16-hydroxylases initiates the synthesis of vindoline in an organ-dependent manner in Catharanthus roseus. Plant Physiol. 163 (2013) 1792-1803. [PMID: 24108213]
Accepted name: vinorine hydroxylase
Reaction: vinorine + [reduced NADPH—hemoprotein reductase] + O2 = vomilenine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Systematic name: vinorine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (21α-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from the plant Rauvolfia serpentina. Forms a stage in the biosynthesis of the indole alkaloid ajmaline.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Falkenhagen, H. and Stöckligt, J. Enzymatic biosynthesis of vomilenine, a key intermediate of the ajmaline pathway, catalysed by a novel cytochrome P-450-dependent enzyme from plant cell cultures of Rauwolfia serpentina. Z. Naturforsch. C: Biosci. 50 (1995) 45-53.
Accepted name: taxane 10β-hydroxylase
Reaction: taxa-4(20),11-dien-5α-yl acetate + [reduced NADPH—hemoprotein reductase] + O2 = 10β-hydroxytaxa-4(20),11-dien-5α-yl acetate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): CYP725A1 (gene name); 5-α-taxadienol-10-β-hydroxylase
Systematic name: taxa-4(20),11-dien-5α-yl acetate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (10β-hydroxylating)
Comments: This microsomal cytochrome-P-450 (heme-thiolate) enzyme from the plant Taxus cuspidata is involved in the biosynthesis of the diterpenoid antineoplastic drug taxol (paclitaxel).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Wheeler, A.L., Long, R.M., Ketchum, R.E., Rithner, C.D., Williams, R.M. and Croteau, R. Taxol biosynthesis: differential transformations of taxadien-5α-ol and its acetate ester by cytochrome P450 hydroxylases from Taxus suspension cells. Arch. Biochem. Biophys. 390 (2001) 265. [PMID: 11396929]
2. Jennewein, S., Rithner, C.D., Williams, R.M. and Croteau, R.B. Taxol biosynthesis: taxane 13 α-hydroxylase is a cytochrome P450-dependent monooxygenase. Proc. Natl. Acad. Sci. USA 98 (2001) 13595. [PMID: 11707604]
3. Schoendorf, A., Rithner, C.D., Williams, R.M. and Croteau, R.B. Molecular cloning of a cytochrome P450 taxane 10β-hydroxylase cDNA from Taxus and functional expression in yeast. Proc. Natl. Acad. Sci. USA 98 (2001) 1501-1506. [PMID: 11171980]
Accepted name: taxane 13α-hydroxylase
Reaction: taxa-4(20),11-dien-5α-ol + [reduced NADPH—hemoprotein reductase] + O2 = taxa-4(20),11-dien-5α,13α-diol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): CYP725A2 (gene name)
Systematic name: taxa-4(20),11-dien-5α-ol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (13α-hydroxylating)
Comments: This cytochrome-P-450(heme-thiolate) enzyme from the plant Taxus cuspidata is involved in the biosynthesis of the diterpenoid antineoplastic drug taxol (paclitaxel).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Wheeler, A.L., Long, R.M., Ketchum, R.E., Rithner, C.D., Williams, R.M. and Croteau, R. Taxol biosynthesis: differential transformations of taxadien-5α-ol and its acetate ester by cytochrome P450 hydroxylases from Taxus suspension cells. Arch. Biochem. Biophys. 390 (2001) 265. [PMID: 11396929]
2. Jennewein, S., Rithner, C.D., Williams, R.M. and Croteau, R.B. Taxol biosynthesis: taxane 13 α-hydroxylase is a cytochrome P450-dependent monooxygenase. Proc. Natl. Acad. Sci. USA 98 (2001) 13595. [PMID: 11707604]
Accepted name: ent-kaurenoic acid monooxygenase
Reaction: ent-kaur-16-en-19-oate + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = gibberellin A12 + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) ent-kaur-16-en-19-oate + [reduced NADPH—hemoprotein reductase] + O2 = ent-7α-hydroxykaur-16-en-19-oate + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) ent-7α-hydroxykaur-16-en-19-oate + [reduced NADPH—hemoprotein reductase] + O2 = gibberellin A12 aldehyde + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) gibberellin A12 aldehyde + [reduced NADPH—hemoprotein reductase] + O2 = gibberellin A12 + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): KAO1 (gene name); CYP88A3 (gene name); ent-kaurenoic acid oxidase
Systematic name: ent-kaur-16-en-19-oate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from plants. Catalyses three sucessive oxidations of ent-kaurenoic acid. The second step includes a ring-B contraction giving the gibbane skeleton. In pumpkin (Cucurbita maxima) ent-6α,7α-dihydroxykaur-16-en-19-oate is also formed.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Helliwell, C.A., Chandler, P.M., Poole, A., Dennis, E.S. and Peacock, W.J. The CYP88A cytochrome P450, ent-kaurenoic acid oxidase, catalyzes three steps of the gibberellin biosynthesis pathway. Proc. Natl. Acad. Sci. USA 98 (2001) 2065-2070. [PMID: 11172076]
Accepted name: 2,5-diketocamphane 1,2-monooxygenase
Reaction: (+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O
For diagram of reaction click here.
Glossary: (+)-bornane-2,5-dione = 2,5-diketocamphane
Other name(s): 2,5-diketocamphane lactonizing enzyme; ketolactonase I (ambiguous); 2,5-diketocamphane 1,2-monooxygenase oxygenating component; 2,5-DKCMO; camP (gene name); camphor 1,2-monooxygenase; camphor ketolactonase I
Systematic name: (+)-bornane-2,5-dione,FMNH2:oxygen oxidoreductase (1,2-lactonizing)
Comments: A Baeyer-Villiger monooxygenase isolated from camphor-grown strains of Pseudomonas putida and encoded on the cam plasmid. Involved in the degradation of (+)-camphor. Requires a dedicated NADH-FMN reductase [cf. EC 1.5.1.42, FMN reductase (NADH)] [1-3]. Can accept several bicyclic ketones including (+)- and (–)-camphor [6] and adamantanone [4]. The product spontaneously converts to [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Conrad, H.E., DuBus, R., Namtvedt, M.J. and Gunsalus, I.C. Mixed function oxidation. II. Separation and properties of the enzymes catalyzing camphor lactonizaton. J. Biol. Chem. 240 (1965) 495-503. [PMID: 14253460]
2. Yu, C.A. and Gunsalus, I.C. Monoxygenases. VII. Camphor ketolactonase I and the role of three protein components. J. Biol. Chem. 244 (1969) 6149-6152. [PMID: 4310834]
3. Taylor, D.G. and Trudgill, P.W. Camphor revisited: studies of 2,5-diketocamphane 1,2-monooxygenase from Pseudomonas putida ATCC 17453. J. Bacteriol. 165 (1986) 489-497. [PMID: 3944058]
4. Selifonov, S.A. Microbial oxidation of adamantanone by Pseudomonas putida carrying the camphor catabolic plasmid. Biochem. Biophys. Res. Commun. 186 (1992) 1429-1436. [PMID: 1510672]
5. Jones, K.H., Smith, R.T. and Trudgill, P.W. Diketocamphane enantiomer-specific ’Baeyer-Villiger’ monooxygenases from camphor-grown Pseudomonas putida ATCC 17453. J. Gen. Microbiol. 139 (1993) 797-805. [PMID: 8515237]
6. Kadow, M., Sass, S., Schmidt, M. and Bornscheuer, U.T. Recombinant expression and purification of the 2,5-diketocamphane 1,2-monooxygenase from the camphor metabolizing Pseudomonas putida strain NCIMB 10007. AMB Express 1 (2011) 13. [PMID: 21906366]
7. Iwaki, H., Grosse, S., Bergeron, H., Leisch, H., Morley, K., Hasegawa, Y. and Lau, P.C. Camphor pathway redux: functional recombinant expression of 2,5- and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions. Appl. Environ. Microbiol. 79 (2013) 3282-3293. [PMID: 23524667]
Accepted name: 3-hydroxyindolin-2-one monooxygenase
Reaction: 3-hydroxyindolin-2-one + [reduced NADPH—hemoprotein reductase] + O2 = 2-hydroxy-2H-1,4-benzoxazin-3(4H)-one [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: 2-hydroxy-2H-1,4-benzoxazin-3(4H)-one = HBOA
Other name(s): BX4 (gene name); CYP71C1 (gene name)
Systematic name: 3-hydroxyindolin-2-one,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2-hydroxy-2H-1,4-benzoxazin-3(4H)-one-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poaceae (grasses).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Glawischnig, E., Grun, S., Frey, M. and Gierl, A. Cytochrome P450 monooxygenases of DIBOA biosynthesis: specificity and conservation among grasses. Phytochemistry 50 (1999) 925-930. [PMID: 10385992]
2. Frey, M., Chomet, P., Glawischnig, E., Stettner, C., Grün, S., Winklmair, A., Eisenreich, W., Bacher, A., Meeley, R.B., Briggs, S.P., Simcox, K. and Gierl, A. Analysis of a chemical plant defense mechanism in grasses. Science 277 (1997) 696-699. [PMID: 9235894]
3. Spiteller, P., Glawischnig, E., Gierl, A. and Steglich, W. Studies on the biosynthesis of 2-hydroxy-1,4-benzoxazin-3-one (HBOA) from 3-hydroxyindolin-2-one in Zea mays. Phytochemistry 57 (2001) 373-376. [PMID: 11393516]
Accepted name: 2-hydroxy-1,4-benzoxazin-3-one monooxygenase
Reaction: 2-hydroxy-2H-1,4-benzoxazin-3(4H)-one + [reduced NADPH—hemoprotein reductase] + O2 = 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one = DIBOA
2-hydroxy-2H-1,4-benzoxazin-3(4H)-one = HBOA
Other name(s): BX5 (gene name); CYP71C3 (gene name)
Systematic name: 2-hydroxy-2H-1,4-benzoxazin-3(4H)-one,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poaceae (grasses).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Bailey, B.A. and Larson, R.L. Maize microsomal benzoxazinone N-monooxygenase. Plant Physiol. 95 (1991) 792-796. [PMID: 16668055]
2. Glawischnig, E., Grun, S., Frey, M. and Gierl, A. Cytochrome P450 monooxygenases of DIBOA biosynthesis: specificity and conservation among grasses. Phytochemistry 50 (1999) 925-930. [PMID: 10385992]
Accepted name: 9β-pimara-7,15-diene oxidase
Reaction: 9β-pimara-7,15-diene + 3 O2 + 3 [reduced NADPH—hemoprotein reductase] = 9β-pimara-7,15-dien-19-oate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) 9β-pimara-7,15-diene + O2 + [reduced NADPH—hemoprotein reductase] = 9β-pimara-7,15-dien-19-ol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 9β-pimara-7,15-dien-19-ol + O2 + [reduced NADPH—hemoprotein reductase] = 9β-pimara-7,15-dien-19-al + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) 9β-pimara-7,15-dien-19-al + O2 + [reduced NADPH—hemoprotein reductase] = 9β-pimara-7,15-dien-19-oate + [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): CYP99A3; 9β-pimara-7,15-diene monooxygenase
Systematic name: 9β-pimara-7,15-diene,[reduced NADPH—hemoprotein reductase]:oxygen 19-oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from rice (Oryza sativa) is involved in the biosynthesis of the phytoalexin momilactone. It also acts similarly on 9β-stemod-13(17)-ene.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Wang, Q., Hillwig, M.L. and Peters, R.J. CYP99A3: functional identification of a diterpene oxidase from the momilactone biosynthetic gene cluster in rice. Plant J. 65 (2011) 87-95. [PMID: 21175892]
Accepted name: ent-cassa-12,15-diene 11-hydroxylase
Reaction: ent-cassa-12,15-diene + O2 + [reduced NADPH—hemoprotein reductase] = ent-11β-hydroxycassa-12,15-diene + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): ent-cassadiene C11α-hydroxylase; CYP76M7
Systematic name: ent-cassa-12,15-diene,[reduced NADPH—hemoprotein reductase]:oxygen 11-oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from rice (Oryza sativa) is involved in the biosynthesis of the antifungal phytocassanes.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Swaminathan, S., Morrone, D., Wang, Q., Fulton, D.B. and Peters, R.J. CYP76M7 is an ent-cassadiene C11α-hydroxylase defining a second multifunctional diterpenoid biosynthetic gene cluster in rice. Plant Cell 21 (2009) 3315-3325. [PMID: 19825834]
Accepted name: α-humulene 10-hydroxylase
Reaction: α-humulene + O2 + [reduced NADPH—hemoprotein reductase] = 10-hydroxy-α-humulene + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): CYP71BA1
Systematic name: α-humulene,[reduced NADPH—hemoprotein reductase]:oxygen 10-oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein. The recommended numbering of humulene gives 10-hydroxy-α-humulene as the product rather than 8-hydroxy-α-humulene as used by the reference. See Section F: Natural Product Nomenclature.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yu, F., Okamoto, S., Harada, H., Yamasaki, K., Misawa, N. and Utsumi, R. Zingiber zerumbet CYP71BA1 catalyzes the conversion of α-humulene to 8-hydroxy-α-humulene in zerumbone biosynthesis. Cell. Mol. Life Sci. 68 (2011) 1033-1040. [PMID: 20730551]
Accepted name: amorpha-4,11-diene 12-monooxygenase
Reaction: amorpha-4,11-diene + 3 O2 + 3 [reduced NADPH—hemoprotein reductase] = artemisinate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) amorpha-4,11-diene + O2 + [reduced NADPH—hemoprotein reductase] = artemisinic alcohol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) artemisinic alcohol + O2 + [reduced NADPH—hemoprotein reductase] = artemisinic aldehyde + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) artemisinic aldehyde + O2 + [reduced NADPH—hemoprotein reductase] = artemisinate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): CYP71AV1
Systematic name: amorpha-4,11-diene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. Cloned from the plant Artemisia annua (sweet wormwood). Part of the biosynthetic pathway of artemisinin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Teoh, K.H., Polichuk, D.R., Reed, D.W., Nowak, G. and Covello, P.S. Artemisia annua L. (Asteraceae) trichome-specific cDNAs reveal CYP71AV1, a cytochrome P450 with a key role in the biosynthesis of the antimalarial sesquiterpene lactone artemisinin. FEBS Lett. 580 (2006) 1411-1416. [PMID: 16458889]
Accepted name: 11-oxo-β-amyrin 30-oxidase
Reaction: 11-oxo-β-amyrin + 3 O2 + 3 [reduced NADPH—hemoprotein reductase] = glycyrrhetinate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) 11-oxo-β-amyrin + O2 + [reduced NADPH—hemoprotein reductase] = 30-hydroxy-11-oxo-β-amyrin + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 30-hydroxy-11-oxo-β-amyrin + O2 + [reduced NADPH—hemoprotein reductase] = glycyrrhetaldehyde + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) glycyrrhetaldehyde + O2 + [reduced NADPH—hemoprotein reductase] = glycyrrhetinate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): CYP72A; CYP72A154; 11-oxo-β-amyrin 30-monooxygenase
Systematic name: 11-oxo-β-amyrin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (30-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from the plant Glycyrrhiza uralensis (licorice) is involved in the biosynthesis of the triterpenoid saponin glycyrrhizin. The enzyme from the plant Medicago truncatula can also hydroxylate β-amyrin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Seki, H., Sawai, S., Ohyama, K., Mizutani, M., Ohnishi, T., Sudo, H., Fukushima, E.O., Akashi, T., Aoki, T., Saito, K. and Muranaka, T. Triterpene functional genomics in licorice for identification of CYP72A154 involved in the biosynthesis of glycyrrhizin. Plant Cell 23 (2011) 4112-4123. [PMID: 22128119]
Accepted name: averantin hydroxylase
Reaction: (1) (1'S)-averantin + [reduced NADPH—hemoprotein reductase] + O2 = (1'S,5'S)-5'-hydroxyaverantin + [oxidized NADPH—hemoprotein reductase] + H2O
(2) (1'S)-averantin + [reduced NADPH—hemoprotein reductase] + O2 = (1'S,5'R)-5'-hydroxyaverantin + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: averantin = 1,3,6,8-tetrahydroxy-2-[(1S)-1-hydroxyhexyl]anthracene-9,10-dione
Other name(s): AVN hydroxylase; avnA (gene name); CYP60A1
Systematic name: (1'S)-averantin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (5'-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the saprophytic mold Aspergillus parasiticus. Involved in aflatoxin biosynthesis. Does not react with (1'R)-averantin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yabe, K., Matsuyama, Y., Ando, Y., Nakajima, H. and Hamasaki, T. Stereochemistry during aflatoxin biosynthesis: conversion of norsolorinic acid to averufin. Appl. Environ. Microbiol. 59 (1993) 2486-2492. [PMID: 8368836]
2. Yu, J., Chang, P.K., Cary, J.W., Bhatnagar, D. and Cleveland, T.E. avnA, a gene encoding a cytochrome P-450 monooxygenase, is involved in the conversion of averantin to averufin in aflatoxin biosynthesis in Aspergillus parasiticus. Appl. Environ. Microbiol. 63 (1997) 1349-1356. [PMID: 9097431]
Accepted name: aflatoxin B synthase
Reaction: (1) 8-O-methylsterigmatocystin + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = aflatoxin B1 + 2 [oxidized NADPH—hemoprotein reductase] + H2O + methanol + CO2
(2) 8-O-methyldihydrosterigmatocystin + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = aflatoxin B2 + 2 [oxidized NADPH—hemoprotein reductase] + H2O + methanol + CO2
For diagram of reaction click here.
Glossary: aflatoxin B1 = (6aR,9aS)-4-methoxy-2,3,6a,9a-tetrahydrocyclopenta[c]furo[3',2':4,5]furo[2,3-h][1]benzopyran-1,11-dione
aflatoxin B2 = (6aR,9aS)-4-methoxy-2,3,6a,8,9,9a-hexahydrocyclopenta[c]furo[3',2':4,5]furo[2,3-h][1]benzopyran-1,11-dione
8-O-methylsterigmatocystin = 6,8-dimethoxy-3a,12c-dihydrofuro[3',2':4,5]furo[2,3-c]xanthen-7-one
8-O-methyldihydrosterigmatocystin = 6,8-dimethoxy-1,2,3a,12c-tetrahydrofuro[3',2':4,5]furo[2,3-c]xanthen-7-one
Other name(s): ordA (gene name)
Systematic name: 8-O-methylsterigmatocystin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (aflatoxin-B forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. Isolated from the mold Aspergillus parasiticus.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Bhatnagar, D., Cleveland, T.E. and Kingston, D.G. Enzymological evidence for separate pathways for aflatoxin B1 and B2 biosynthesis. Biochemistry 30 (1991) 4343-4350. [PMID: 1902378]
2. Yu, J., Chang, P.K., Ehrlich, K.C., Cary, J.W., Montalbano, B., Dyer, J.M., Bhatnagar, D. and Cleveland, T.E. Characterization of the critical amino acids of an Aspergillus parasiticus cytochrome P-450 monooxygenase encoded by ordA that is involved in the biosynthesis of aflatoxins B1, G1, B2, and G2. Appl. Environ. Microbiol. 64 (1998) 4834-4841. [PMID: 9835571]
3. Udwary, D.W., Casillas, L. K. and Townsend, C.A. Synthesis of 11-hydroxyl O-methylsterigmatocystin and the role of a cytochrome P-450 in the final step of aflatoxin biosynthesis. J. Am. Chem. Soc. 124 (2002) 5294-5303. [PMID: 11996570]
Accepted name: tryprostatin B 6-hydroxylase
Reaction: tryprostatin B + [reduced NADPH—hemoprotein reductase] + O2 = 6-hydroxytryprostatin B + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: tryprostatin B = (3S,8aS)-3-{[2-(3-methylbut-2-en-1-yl)-1H-indol-3-yl]methyl}hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
6-hydroxytryprostatin B = (3S,8aS)-3-{[6-hydroxy-2-(3-methylbut-2-en-1-yl)-1H-indol-3-yl]methyl}hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
Other name(s): ftmC (gene name)
Systematic name: tryprostatin B,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6-hydroxytryprostatin B-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. Involved in the biosynthetic pathways of several indole alkaloids such as tryprostatins, 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: fumitremorgin C monooxygenase
Reaction: fumitremorgin C + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = 12α,13α-dihydroxyfumitremorgin C + 2 [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of reaction click here.
Glossary: fumitremorgin C = (5aS,12S,14aS)-9-methoxy-12-(2-methylprop-1-en-1-yl)-1,2,3,5a,6,11,12,14a-octahydro-5H,14H-pyrrolo[1'',2'':4',5']pyrazino[1',2':1,6]pyrido[3,4-b]indole-5,14-dione
12α,13α-dihydroxyfumitremorgin = (5aR,6S,12S,14aS)-5a,6-dihydroxy-9-methoxy-12-(2-methylprop-1-en-1-yl)-1,2,3,5a,6,11,12,14a-octahydro-5H,14H-pyrrolo[1'',2'':4',5']pyrazino[1',2':1,6]pyrido[3,4-b]indole-5,14-dione
Other name(s): ftmG (gene name)
Systematic name: fumitremorgin C,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12α,13α-dihydroxyfumitremorgin C-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. Involved in the biosynthetic pathway of the indole alkaloid verruculogen.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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: dammarenediol 12-hydroxylase
Reaction: dammarenediol-II + [reduced NADPH—hemoprotein reductase] + O2 = protopanaxadiol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: dammarenediol-II = dammar-24-ene-3β,20-diol
protopanaxadiol = dammar-24-ene-3β,12β,20-triol
Other name(s): protopanaxadiol synthase; CYP716A47
Systematic name: dammarenediol-II,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12β-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from ginseng (Panax ginseng). Involved in the biosynthetic pathway of ginsenosides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Han, J.Y., Kim, H.J., Kwon, Y.S. and Choi, Y.E. The Cyt P450 enzyme CYP716A47 catalyzes the formation of protopanaxadiol from dammarenediol-II during ginsenoside biosynthesis in Panax ginseng. Plant Cell Physiol 52 (2011) 2062-2073. [PMID: 22039120]
Accepted name: protopanaxadiol 6-hydroxylase
Reaction: protopanaxadiol + [reduced NADPH—hemoprotein reductase] + O2 = protopanaxatriol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: protopanaxadiol = dammar-24-ene-3β,12β,20-triol
protopanaxatriol = dammar-24-ene-3β,6α,12β,20-tetrol
Other name(s): protopanaxatriol synthase; P6H; CYP716A53v2
Systematic name: protopanaxadiol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6α-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the rhizomes of ginseng (Panax ginseng). Involved in the biosynthetic pathway of ginsenosides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yue, C.J., Zhou, X. and Zhong, J.J. Protopanaxadiol 6-hydroxylase and its role in regulating the ginsenoside heterogeneity in Panax notoginseng cells. Biotechnol. Bioeng. 100 (2008) 933-940. [PMID: 18351680]
2. Han, J.Y., Hwang, H.S., Choi, S.W., Kim, H.J. and Choi, Y.E. Cytochrome P450 CYP716A53v2 catalyzes the formation of protopanaxatriol from protopanaxadiol during ginsenoside biosynthesis in Panax ginseng. Plant Cell Physiol 53 (2012) 1535-1545. [PMID: 22875608]
Accepted name: oryzalexin E synthase
Reaction: ent-sandaracopimaradien-3β-ol + [reduced NADPH—hemoprotein reductase] + O2 = oryzalexin E + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: oryzalexin E = ent-sandaracopimaradiene-3β,9α-diol = (3R,4aR,4bS,7S,10aR)-7-ethenyl-1,1,4a,7-tetramethyl-1,2,3,4,4a,4b,5,6,7,9,10,10a-dodecahydrophenanthren-2,4b-diol
ent-sandaracopimaradien-3β-ol = (3R,4aR,4bR,7S,10aS)-7-ethenyl-1,1,4a,7-tetramethyl-1,2,3,4,4a,4b,5,6,7,9,10,10a-dodecahydrophenanthren-2-ol
Other name(s): CYP76M6
Systematic name: ent-sandaracopimaradien-3β-ol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (oryzalexin E forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. Isolated from Oryza sativa (rice). Oryzalexin E is a phytoalexin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. 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]
Accepted name: oryzalexin D synthase
Reaction: ent-sandaracopimaradien-3β-ol + [reduced NADPH—hemoprotein reductase] + O2 = oryzalexin D + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: oryzalexin D = ent-sandaracopimaradiene-3β,7α-diol = (3R,4aR,4bS,7S,9S,10aS)-7-ethenyl-1,1,4a,7-tetramethyl-1,2,3,4,4a,4b,5,6,7,9,10,10a-dodecahydrophenanthren-2,9-diol
ent-sandaracopimaradien-3β-ol = (3R,4aR,4bR,7S,10aS)-7-ethenyl-1,1,4a,7-tetramethyl-1,2,3,4,4a,4b,5,6,7,9,10,10a-dodecahydrophenanthren-2-ol
Other name(s): CYP76M8
Systematic name: ent-sandaracopimaradien-3β-ol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (oryzalexin D forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. Isolated from Oryza sativa (rice). Oryzalexin D is a phytoalexin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. 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]
Accepted name: dihydromonacolin L hydroxylase
Reaction: dihydromonacolin L acid + O2 + [reduced NADPH—hemoprotein reductase] = monacolin L acid + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) dihydromonacolin L acid + O2 + [reduced NADPH—hemoprotein reductase] = 3α-hydroxy-3,5-dihydromonacolin L acid + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 3α-hydroxy-3,5-dihydromonacolin L acid = monacolin L acid + H2O (spontaneous)
For diagram of reaction click here.
Glossary: dihydromonacolin L acid = (3R,5R)-7-[(1S,2S,4aR,6R,8aS)-2,6-dimethyl-1,2,4a,5,6,7,8,8a-octahydronaphthalen1yl]-3,5-dihydroxyheptanoate
monacolin L acid = (3R,5R)-7-[(1S,2S,6R,8aR)-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
3α-hydroxy-3,5-dihydromonacolin L = (3R,5R)-7-[(1R,2R,3S,6R,8aR)-3-hydroxy-2,6-dimethyl-1,2,3,5,6,7,8,8a-octahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
Other name(s): LovA (ambiguous)
Systematic name: dihydromonacolin L acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The dehydration of 3α-hydroxy-3,5-dihydromonacolin L acid is believed to be spontaneous [1,2]. The enzyme from fungi also catalyses the reaction of EC 1.14.14.125, monacolin L hydroxylase [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Treiber, L.R., Reamer, R.A., Rooney, C.S. and Ramjit, H.G. Origin of monacolin L from Aspergillus terreus cultures. J. Antibiot. (Tokyo) 42 (1989) 30-36. [PMID: 2921224]
2. Nakamura, T., Komagata, D., Murakawa, S., Sakai, K. and Endo, A. Isolation and biosynthesis of 3α-hydroxy-3,5-dihydromonacolin L. J. Antibiot. (Tokyo) 43 (1990) 1597-1600. [PMID: 2276977]
3. Barriuso, J., Nguyen, D.T., Li, J.W., Roberts, J.N., MacNevin, G., Chaytor, J.L., Marcus, S.L., Vederas, J.C. and Ro, D.K. Double oxidation of the cyclic nonaketide dihydromonacolin L to monacolin J by a single cytochrome P450 monooxygenase, LovA. J. Am. Chem. Soc. 133 (2011) 8078-8081. [PMID: 21495633]
Accepted name: monacolin L hydroxylase
Reaction: monacolin L acid + O2 + [reduced NADPH—hemoprotein reductase] = monacolin J acid + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: monacolin L acid = (3R,5R)-7-[(1S,2S,6R,8aR)-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid
monacolin J acid = (3R,5R)-7-[(1S,2S,6R,8S,8aR)-8-hydroxy-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid
Other name(s): LovA (ambiguous)
Systematic name: monacolin L acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (8-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from fungi also catalyses the reaction of EC 1.14.14.124, dihydromonacolin L hydroxylase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Barriuso, J., Nguyen, D.T., Li, J.W., Roberts, J.N., MacNevin, G., Chaytor, J.L., Marcus, S.L., Vederas, J.C. and Ro, D.K. Double oxidation of the cyclic nonaketide dihydromonacolin L to monacolin J by a single cytochrome P450 monooxygenase, LovA. J. Am. Chem. Soc. 133 (2011) 8078-8081. [PMID: 21495633]
Accepted name: β-amyrin 28-monooxygenase
Reaction: β-amyrin + 3 O2 + 3 [reduced NADPH—hemoprotein reductase] = oleanolate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) β-amyrin + O2 + [reduced NADPH—hemoprotein reductase] = erythrodiol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) erythrodiol + O2 + [reduced NADPH—hemoprotein reductase] = oleanolic aldehyde + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) oleanolic aldehyde + O2 + [reduced NADPH—hemoprotein reductase] = oleanolate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): CYP716A52v2; CYP716A12; CYP16A75; β-amyrin 28-oxidase
Systematic name: β-amyrin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (28-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. The enzyme is involved in the biosynthesis of oleanane-type triterpenoids, such as ginsenoside Ro. The enzyme from Medicago truncatula (barrel medic) (CYP716A12) can also convert α-amyrin and lupeol to ursolic acid and betulinic acid, respectively. The enzyme from Maesa lanceolata (false assegai) (CYP16A75) does not catalyse the reaction to completion, resulting in accumulation of both intermediates.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Fukushima, E.O., Seki, H., Ohyama, K., Ono, E., Umemoto, N., Mizutani, M., Saito, K. and Muranaka, T. CYP716A subfamily members are multifunctional oxidases in triterpenoid biosynthesis. Plant Cell Physiol 52 (2011) 2050-2061. [PMID: 22039103]
2. Han, J.Y., Kim, M.J., Ban, Y.W., Hwang, H.S. and Choi, Y.E. The involvement of β-amyrin 28-oxidase (CYP716A52v2) in oleanane-type ginsenoside biosynthesis in Panax ginseng. Plant Cell Physiol 54 (2013) 2034-2046. [PMID: 24092881]
3. Moses, T., Pollier, J., Faizal, A., Apers, S., Pieters, L., Thevelein, J.M., Geelen, D. and Goossens, A. Unraveling the triterpenoid saponin biosynthesis of the African shrub Maesa lanceolata. Mol. Plant 8 (2015) 122-135. [PMID: 25578277]
Accepted name: methyl farnesoate epoxidase
Reaction: methyl (2E,6E)-farnesoate + [reduced NADPH—hemoprotein reductase] + O2 = juvenile hormone III + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: juvenile hormone III = methyl (2E,6E,10R)-10,11-epoxy-3,7,11-trimethyldodeca-2,6-dienoate
Other name(s): CYP15A1
Systematic name: methyl (2E,6E)-farnesoate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme, found in insects except for Lepidoptera (moths and butterflies) is specific for methyl farnesoate (cf. EC 1.14.14.128, farnesoate epoxidase) [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Helvig, C., Koener, J.F., Unnithan, G.C. and Feyereisen, R. CYP15A1, the cytochrome P450 that catalyzes epoxidation of methyl farnesoate to juvenile hormone III in cockroach corpora allata. Proc. Natl. Acad. Sci. USA 101 (2004) 4024-4029. [PMID: 15024118]
2. Daimon, T. and Shinoda, T. Function, diversity, and application of insect juvenile hormone epoxidases (CYP15). Biotechnol. Appl. Biochem. 60 (2013) 82-91. [PMID: 23586995]
Accepted name: farnesoate epoxidase
Reaction: (2E,6E)-farnesoate + [reduced NADPH—hemoprotein reductase] + O2 = juvenile-hormone-III carboxylate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: juvenile-hormone-III carboxylate = (2E,6E,10R)-10,11-epoxy-3,7,11-trimethyldodeca-2,6-dienoate
Other name(s): CYP15C1
Systematic name: (2E,6E)-farnesoate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme, found in Lepidoptera (moths and butterflies), is specific for farnesoate (cf. EC 1.14.14.127, methyl farnesoate epoxidase) [1,2]. It is involved in the synthesis of juvenile hormone.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Daimon, T., Kozaki, T., Niwa, R., Kobayashi, I., Furuta, K., Namiki, T., Uchino, K., Banno, Y., Katsuma, S., Tamura, T., Mita, K., Sezutsu, H., Nakayama, M., Itoyama, K., Shimada, T. and Shinoda, T. Precocious metamorphosis in the juvenile hormone-deficient mutant of the silkworm, Bombyx mori. PLoS Genet 8 (2012) e1002486. [PMID: 22412378]
2. Daimon, T. and Shinoda, T. Function, diversity, and application of insect juvenile hormone epoxidases (CYP15). Biotechnol. Appl. Biochem. 60 (2013) 82-91. [PMID: 23586995]
Accepted name: long-chain acyl-CoA ω-monooxygenase
Reaction: (1) oleoyl-CoA + [reduced NADPH—hemoprotein reductase] + O2 = 18-hydroxyoleoyl-CoA + [oxidized NADPH—hemoprotein reductase] + H2O
(2) linoleoyl-CoA + [reduced NADPH—hemoprotein reductase] + O2 = 18-hydroxylinoleoyl-CoA + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): long-chain acyl-CoA ω-hydroxylase; CYP86A22 (gene name)
Systematic name: long-chain acyl-CoA,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ω-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzymes from solanaceous plants are involved in the biosynthesis of stigmatic estolide, a lipid-based polyester that forms a major component of the exudate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Han, J., Clement, J.M., Li, J., King, A., Ng, S. and Jaworski, J.G. The cytochrome P450 CYP86A22 is a fatty acyl-CoA ω-hydroxylase essential for estolide synthesis in the stigma of Petunia hybrida. J. Biol. Chem. 285 (2010) 3986-3996. [PMID: 19940120]
Accepted name: laurate 7-monooxygenase
Reaction: dodecanoate + [reduced NADPH—hemoprotein reductase] + O2 = 7-hydroxydodecanoate + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: laurate = dodecanoate
Other name(s): CYP703A2 (gene name)
Systematic name: dodecanoate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (7-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. The enzyme is involved in the synthesis of sporopollenin - a complex polymer found at the outer layer of spores and pollen. It can also act on decanoate (C10), myristate (C14), and palmitate (C16) with lower activity. The enzyme also produces a small amount of products that are hydroxylated at neighboring positions (C-6, C-8 and C-9).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Morant, M., Jørgensen, K., Schaller, H., Pinot, F., Møller, B.L., Werck-Reichhart, D. and Bak, S. CYP703 is an ancient cytochrome P450 in land plants catalyzing in-chain hydroxylation of lauric acid to provide building blocks for sporopollenin synthesis in pollen. Plant Cell 19 (2007) 1473-1487. [PMID: 17496121]
Accepted name: bursehernin 5'-monooxygenase
Reaction: (–)-bursehernin + [reduced NADPH—hemoprotein reductase] + O2 = (–)-5'-demethylyatein + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: (–)-bursehernin = (3R,4R)-4-(2H-1,3-benzodioxol-5-ylmethyl)-3-[(3,4-dimethoxyphenyl)methyl]oxolan-2-one
(–)-5'-demethylyatein = (3R,4R)-4-(2H-1,3-benzodioxol-5-ylmethyl)-3-[(3-hydroxy-4,5-dimethoxyphenyl)methyl]oxolan-2-one
(–)-yaetin = (3R,4R)-4-(2H-1,3-benzodioxol-5-ylmethyl)-3-[(3,4,5-trimethoxyphenyl)methyl]oxolan-2-one
Other name(s): CYP71CU1 (gene name); bursehernin 5'-hydroxylase
Systematic name: (–)-bursehernin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (5'-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein characterized from the plant Sinopodophyllum hexandrum. The enzyme is involved in the biosynthetic pathway 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. Lau, W. and Sattely, E.S. Six enzymes from mayapple that complete the biosynthetic pathway to the etoposide aglycone. Science 349 (2015) 1224-1228. [PMID: 26359402]
Accepted name: (–)-4'-demethyl-deoxypodophyllotoxin 4-hydroxylase
Reaction: (–)-4'-demethyldeoxypodophyllotoxin + [reduced NADPH—hemoprotein reductase] + O2 = (–)-4'-demethylepipodophyllotoxin + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: (–)-4'-demethyldeoxypodophyllotoxin = (5R,5aR,8aR)-5-(4-hydroxy-3,5-dimethoxyphenyl)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
(–)-4'-demethylepipodophyllotoxin = (5R,5aR,8aR,9S)-9-hydroxy-5-(4-hydroxy-3,5-dimethoxyphenyl)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
Other name(s): CYP82D61 (gene name)
Systematic name: (–)-deoxypodophyllotoxin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (4-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein characterized from the plant Sinopodophyllum hexandrum. The enzyme produces the direct precursor to etoposide, a potent anticancer drug. It can also act on (–)-deoxypodophyllotoxin with lower efficiency.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Lau, W. and Sattely, E.S. Six enzymes from mayapple that complete the biosynthetic pathway to the etoposide aglycone. Science 349 (2015) 1224-1228. [PMID: 26359402]
Accepted name: 1,8-cineole 2-endo-monooxygenase
Reaction: 1,8-cineole + [reduced flavodoxin] + O2 = 2-endo-hydroxy-1,8-cineole + [oxidized flavodoxin] + H2O
For diagram of reaction click here.
Glossary: 1,8-cineole = 1,3,3-trimethyl-2-oxabicyclo[2.2.2]octane
2-endo-hydroxy-1,8-cineole = (1R,4S,6R)-1,3,3-trimethyl-2-oxabicyclo[2.2.2]octan-6-ol
Other name(s): P450cin; CYP176A; CYP176A1
Systematic name: 1,8-cineole,[reduced flavodoxin]:oxygen oxidoreductase (2-endo-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein that uses a flavodoxin-like redox partner to reduce the heme iron. Isolated from the bacterium Citrobacter braakii, which can use 1,8-cineole as the sole source of carbon.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Hawkes, D.B., Adams, G.W., Burlingame, A.L., Ortiz de Montellano, P.R. and De Voss, J.J. Cytochrome P450cin (CYP176A), isolation, expression, and characterization. J. Biol. Chem. 277 (2002) 27725-27732. [PMID: 12016226]
2. Meharenna, Y.T., Li, H., Hawkes, D.B., Pearson, A.G., De Voss, J. and Poulos, T.L. Crystal structure of P450cin in a complex with its substrate, 1,8-cineole, a close structural homologue to D-camphor, the substrate for P450cam. Biochemistry 43 (2004) 9487-9494. [PMID: 15260491]
3. Kimmich, N., Das, A., Sevrioukova, I., Meharenna, Y., Sligar, S.G. and Poulos, T.L. Electron transfer between cytochrome P450cin and its FMN-containing redox partner, cindoxin. J. Biol. Chem. 282 (2007) 27006-27011. [PMID: 17606612]
4. Meharenna, Y.T., Slessor, K.E., Cavaignac, S.M., Poulos, T.L. and De Voss, J.J. The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin. J. Biol. Chem. 283 (2008) 10804-10812. [PMID: 18270198]
Accepted name: β-amyrin 24-hydroxylase
Reaction: (1) β-amyrin + [reduced NADPH—hemoprotein reductase] + O2 = 24-hydroxy-β-amyrin + [oxidized NADPH—hemoprotein reductase] + H2O
(2) sophoradiol + [reduced NADPH—hemoprotein reductase] + O2 = 24-hydroxysophoradiol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: 24-hydroxy-β-amyrin = olean-12-ene-3β,24-diol
24-hydroxysophoradiol = soyasapogenol B
Other name(s): sophoradiol 24-hydroxylase; CYP93E1
Systematic name: β-amyrin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (24-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. Found in plants and participates in the biosynthesis of soybean saponins.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Shibuya, M., Hoshino, M., Katsube, Y., Hayashi, H., Kushiro, T. and Ebizuka, Y. Identification of β-amyrin and sophoradiol 24-hydroxylase by expressed sequence tag mining and functional expression assay. FEBS J. 273 (2006) 948-959. [PMID: 16478469]
Accepted name: glyceollin synthase
Reaction: (1) (6aS,11aS)-3,6a,9-trihydroxy-2-prenylpterocarpan + [reduced NADPH—hemoprotein reductase] + O2 = glyceollin II + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(2) (6aS,11aS)-3,6a,9-trihydroxy-2-prenylpterocarpan + [reduced NADPH—hemoprotein reductase] + O2 = glyceollin III + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(3) (6aS,11aS)-3,6a,9-trihydroxy-4-prenylpterocarpan + [reduced NADPH—hemoprotein reductase] + O2 = glyceollin I + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of reaction click here.
Systematic name: (6aS,11aS)-3,6a,9-trihydroxy-2-prenylpterocarpan,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (cyclizing)
Comments: A cytochrome p-450 (heme-thiolate) protein prified from soybean.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Welle, R. and Grisebach, H. Induction of phytoalexin synthesis in soybean: enzymatic cyclization of prenylated pterocarpans to glyceollin isomers. Arch. Biochem. Biophys. 263 (1988) 191-198. [PMID: 3369863]
Accepted name: deoxysarpagine hydroxylase
Reaction: 10-deoxysarpagine + [reduced NADPH—hemoprotein reductase] + O2 = sarpagine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): DOSH
Systematic name: 10-deoxysarpagine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (10-hydroxylating)
Comments: A cytohrome P-450 (heme-thiolate) protein isolated from the plant Rauvolfia serpentina.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yu, B., Ruppert, M. and Stöckigt, J. Deoxysarpagine hydroxylase — a novel enzyme closing a short side pathway of alkaloid biosynthesis in Rauvolfia. Bioorg. Med. Chem. 10 (2002) 2479-2483. [PMID: 12057637]
Accepted name: (+)-abscisic acid 8'-hydroxylase
Reaction: (+)-abscisate + [reduced NADPH—hemoprotein reductase] + O2 = 8'-hydroxyabscisate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): (+)-ABA 8'-hydroxylase; ABA 8'-hydroxylase; CYP707A1 (gene name)
Systematic name: abscisate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (8'-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. Catalyses the first step in the oxidative degradation of abscisic acid and is considered to be the pivotal enzyme in controlling the rate of degradation of this plant hormone [1]. CO inhibits the reaction, but its effects can be reversed by the presence of blue light [1]. The 8'-hydroxyabscisate formed can be converted into (–)-phaseic acid, most probably spontaneously.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Cutler, A.J., Squires, T.M., Loewen, M.K. and Balsevich, J.J. Induction of (+)-abscisic acid 8' hydroxylase by (+)-abscisic acid in cultured maize cells. J. Exp. Bot. 48 (1997) 1787-1795.
2. Krochko, J.E., Abrams, G.D., Loewen, M.K., Abrams, S.R. and Cutler, A.J. (+)-Abscisic acid 8'-hydroxylase is a cytochrome P450 monooxygenase. Plant Physiol. 118 (1998) 849-860. [PMID: 9808729]
3. Saito, S., Hirai, N., Matsumoto, C., Ohigashi, H., Ohta, D., Sakata, K. and Mizutani, M. Arabidopsis CYP707As encode (+)-abscisic acid 8'-hydroxylase, a key enzyme in the oxidative catabolism of abscisic acid. Plant Physiol. 134 (2004) 1439-1449. [PMID: 15064374]
Accepted name: lithocholate 6β-hydroxylase
Reaction: lithocholate + [reduced NADPH—hemoprotein reductase] + O2 = 6β-hydroxylithocholate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: lithocholate = 3α-hydroxy-5β-cholan-24-oate
6β-hydroxylithocholate = murideoxycholate = 3α,6β-dihydroxy-5β-cholan-24-oate
Other name(s): lithocholate 6β-monooxygenase; CYP3A10; 6β-hydroxylase; cytochrome P450 3A10/lithocholic acid 6β-hydroxylase
Systematic name: lithocholate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6β-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from Mesocricetus auratus (golden hamster). Expression of the gene for this enzyme is 50-fold higher in male compared to female hamsters [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Teixeira, J. and Gil, G. Cloning, expression, and regulation of lithocholic acid 6β-hydroxylase. J. Biol. Chem. 266 (1991) 21030-21036. [PMID: 1840595]
2. Chang, T.K., Teixeira, J., Gil, G. and Waxman, D.J. The lithocholic acid 6beta-hydroxylase cytochrome P-450, CYP 3A10, is an active catalyst of steroid-hormone 6β-hydroxylation. Biochem. J. 291 (1993) 429-433. [PMID: 8484723]
3. Subramanian, A., Wang, J. and Gil, G. STAT 5 and NF-Y are involved in expression and growth hormone-mediated sexually dimorphic regulation of cytochrome P450 3A10/lithocholic acid 6β-hydroxylase. Nucleic Acids Res. 26 (1998) 2173-2178. [PMID: 9547277]
4. Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137-174. [PMID: 12543708]
Accepted name: 5β-cholestane-3α,7α-diol 12α-hydroxylase
Reaction: (1) 5β-cholestane-3α,7α-diol + [reduced NADPH—hemoprotein reductase] + O2 = 5β-cholestane-3α,7α,12α-triol + [oxidized NADPH—hemoprotein reductase] + H2O
(2) 7α-hydroxycholest-4-en-3-one + [reduced NADPH—hemoprotein reductase] + O2 = 7α,12α-dihydroxycholest-4-en-3-one + [oxidized NADPH—hemoprotein reductase] + H2O
(3) chenodeoxycholate + [reduced NADPH—hemoprotein reductase] + O2 = cholate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here
Glossary: chenodeoxycholate = 3α,7α-dihydroxy-5β-cholan-24-oate
cholate = 3α,7α-12α-trihydroxy-5β-cholan-24-oate
Other name(s): 5β-cholestane-3α,7α-diol 12α-monooxygenase; sterol 12α-hydroxylase (ambiguous); CYP8B1; cytochrome P450 8B1; 7α-hydroxycholest-4-en-3-one 12α-hydroxylase; 7α-hydroxy-4-cholesten-3-one 12α-monooxygenase; chenodeoxycholate 12α monooxygenase
Systematic name: 5β-cholestane-3α,7α-diol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12α-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in mammals. This is the key enzyme in the biosynthesis of the bile acid cholate. The enzyme can also hydroxylate 5β-cholestane-3α,7α-diol at the 25 and 26 position, but to a lesser extent [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Hansson, R. and Wikvall, K. Hydroxylations in biosynthesis and metabolism of bile acids. Catalytic properties of different forms of cytochrome P-450. J. Biol. Chem. 255 (1980) 1643-1649. [PMID: 6766451]
2. Hansson, R. and Wikvall, K. Hydroxylations in biosynthesis of bile acids. Cytochrome P-450 LM4 and 12α-hydroxylation of 5β-cholestane-3α,7α-diol. Eur. J. Biochem. 125 (1982) 423-429. [PMID: 6811268]
3. Ishida, H., Noshiro, M., Okuda, K. and Coon, M.J. Purification and characterization of 7α-hydroxy-4-cholesten-3-one 12α-hydroxylase. J. Biol. Chem. 267 (1992) 21319-21323. [PMID: 1400444]
4. Eggertsen, G., Olin, M., Andersson, U., Ishida, H., Kubota, S., Hellman, U., Okuda, K.I. and Björkhem, I. Molecular cloning and expression of rabbit sterol 12α-hydroxylase. J. Biol. Chem. 271 (1996) 32269-32275. [PMID: 8943286]
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. del Castillo-Olivares, A. and Gil, G. α1-Fetoprotein transcription factor is required for the expression of sterol 12α-hydroxylase, the specific enzyme for cholic acid synthesis. Potential role in the bile acid-mediated regulation of gene transcription. J. Biol. Chem. 275 (2000) 17793-17799. [PMID: 10747975]
7. Yang, Y., Zhang, M., Eggertsen, G. and Chiang, J.Y. On the mechanism of bile acid inhibition of rat sterol 12α-hydroxylase gene (CYP8B1) transcription: roles of α-fetoprotein transcription factor and hepatocyte nuclear factor 4alpha. Biochim. Biophys. Acta 1583 (2002) 63-73. [PMID: 12069850]
8. Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137-174. [PMID: 12543708]
9. Fan, L., Joseph, J.F., Durairaj, P., Parr, M.K. and Bureik, M. Conversion of chenodeoxycholic acid to cholic acid by human CYP8B1. Biol. Chem. 400 (2019) 625-628. [PMID: 30465713]
[EC 1.14.14.140 Transferred entry: licodione synthase. Now included with EC 1.14.14.162, flavanone 2-hydroxylase [EC 1.14.14.139 created 2005 as EC 1.14.13.96, transferred 2018 to EC 1.14.14.139 (EC 1.14.18.8 created 2005 as EC 1.14.13.95, transferred 2015 to EC 1.14.18.8, incorporated 2020), modified 2020]
Accepted name: psoralen synthase
Reaction: (+)-marmesin + [reduced NADPH—hemoprotein reductase] + O2 = psoralen + [oxidized NADPH—hemoprotein reductase] + acetone + 2 H2O
For diagram of reaction click here.
Glossary: (+)-marmesin = (S)-2-(2-hydroxypropan-2-yl)-2,3-dihydro-7H-furo[3,2-g]chromen-7-one
psoralen = 7H-furo[3,2-g]chromen-7-one
Other name(s): CYP71AJ1
Systematic name: (+)-marmesin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: This microsomal cytochrome P-450 (heme-thiolate) enzyme is rather specific for (+)-marmesin, although it can also accept 5-hydroxymarmesin to a much lesser extent. Furanocoumarins protect plants from fungal invasion and herbivore attack. (+)-Columbianetin, the angular furanocoumarin analogue of the linear furanocoumarin (+)-marmesin, acts as a competitive inhibitor even though it is not a substrate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Larbat, R., Kellner, S., Specker, S., Hehn, A., Gontier, E., Hans, J., Bourgaud, F. and Matern, U. Molecular cloning and functional characterization of psoralen synthase, the first committed monooxygenase of furanocoumarin biosynthesis. J. Biol. Chem. 282 (2007) 542-554. [PMID: 17068340]
Accepted name: 8-dimethylallylnaringenin 2'-hydroxylase
Reaction: sophoraflavanone B + [reduced NADPH—hemoprotein reductase] + O2 = leachianone G + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: dimethylallyl = prenyl = 3-methylbut-2-en-1-yl
lavandulyl = 5-methyl-2-(prop-1-en-2-yl)hex-4-en-1-yl
leachianone G = (–)-(2S)-2′-hydroxy-8-prenylnaringenin = (–)-(2S)-2-(2,4-dihydroxyphenyl)-5,7-dihydroxy-8-(3-methylbut-2-en-1-yl)-2,3-dihydro-4H-chromen-4-one
naringenin = 5,7-dihydroxy-2-(4-hydroxyphenyl)-2,3-dihydrochromen-4-one
sophoraflavanone B = (–)-(2S)-8-prenylnaringenin = (–)-(2S)-5,7-dihydroxy-2-(4-hydroxyphenyl)-8-(3-methylbut-2-en-1-yl)-2,3-dihydro-4H-chromen-4-one
Other name(s): 8-DMAN 2'-hydroxylase
Systematic name: sophoraflavanone-B,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2'-hydroxylating)
Comments: A membrane-bound cytochrome P-450 (heme-thiolate) protein that is associated with the endoplasmic reticulum [1,2]. This enzyme is specific for sophoraflavanone B as substrate. Along with EC 2.5.1.70 (naringenin 8-dimethylallyltransferase) and EC 2.5.1.71 (leachianone G 2''-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone G biosynthetic pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yamamoto, H., Yatou, A. and Inoue, K. 8-Dimethylallylnaringenin 2'-hydroxylase, the crucial cytochrome P450 mono-oxygenase for lavandulylated flavanone formation in Sophora flavescens cultured cells. Phytochemistry 58 (2001) 671-676. [PMID: 11672730]
2. Zhao, P., Inoue, K., Kouno, I. and Yamamoto, H. Characterization of leachianone G 2''-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures. Plant Physiol. 133 (2003) 1306-1313. [PMID: 14551337]
Accepted name: (+)-menthofuran synthase
Reaction: (+)-pulegone + [reduced NADPH—hemoprotein reductase] + O2 = (+)-menthofuran + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here or for mechanism click here.
Other name(s): menthofuran synthase; (+)-pulegone 9-hydroxylase; (+)-MFS; cytochrome P450 menthofuran synthase
Systematic name: (+)-pulegone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (9-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The conversion of substrate into product involves the hydroxylation of the syn-methyl (C9), intramolecular cyclization to the hemiketal and dehydration to the furan [1]. This is the second cytochrome P-450-mediated step of monoterpene metabolism in peppermint, with the other step being catalysed by EC 1.14.14.99, (S)-limonene 3-monooxygenase [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Bertea, C.M., Schalk, M., Karp, F., Maffei, M. and Croteau, R. Demonstration that menthofuran synthase of mint (Mentha) is a cytochrome P450 monooxygenase: cloning, functional expression, and characterization of the responsible gene. Arch. Biochem. Biophys. 390 (2001) 279-286. [PMID: 11396930]
2. Mahmoud, S.S. and Croteau, R.B. Menthofuran regulates essential oil biosynthesis in peppermint by controlling a downstream monoterpene reductase. Proc. Natl. Acad. Sci. USA 100 (2003) 14481-14486. [PMID: 14623962]
Accepted name: abieta-7,13-diene hydroxylase
Reaction: abieta-7,13-diene + [reduced NADPH—hemoprotein reductase] + O2 = abieta-7,13-dien-18-ol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: abieta-7,13-diene = (4aS,4bR,10aS)-7-isopropyl-1,1,4a-trimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthrene
abieta-7,13-dien-18-ol = ((1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthren-1-yl)methanol
Other name(s): abietadiene hydroxylase (ambiguous)
Systematic name: abieta-7,13-diene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (18-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses a step in the pathway of abietic acid biosynthesis. The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine). Activity is induced by wounding of the plant tissue [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Funk, C. and Croteau, R. Diterpenoid resin acid biosynthesis in conifers: characterization of two cytochrome P450-dependent monooxygenases and an aldehyde dehydrogenase involved in abietic acid biosynthesis. Arch. Biochem. Biophys. 308 (1994) 258-266. [PMID: 8311462]
2. Funk, C., Lewinsohn, E., Vogel, B.S., Steele, C.L. and Croteau, R. Regulation of oleoresinosis in grand fir (Abies grandis) (coordinate induction of monoterpene and diterpene cyclases and two cytochrome P450-dependent diterpenoid hydroxylases by stem wounding). Plant Physiol. 106 (1994) 999-1005. [PMID: 12232380]
Accepted name: abieta-7,13-dien-18-ol hydroxylase
Reaction: abieta-7,13-dien-18-ol + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = abieta-7,13-dien-18-oate + 2 [oxidized NADPH—hemoprotein reductase] + 3 H2O (overall reaction)
(1a) abieta-7,13-dien-18-ol + [reduced NADPH—hemoprotein reductase] + O2 = abieta-7,13-dien-18,18-diol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) abieta-7,13-dien-18,18-diol = abieta-7,13-dien-18-al + H2O (spontaneous)
(1c) abieta-7,13-dien-18-al + [reduced NADPH—hemoprotein reductase] + O2 = abieta-7,13-dien-18-oate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: abieta-7,13-dien-18-ol = ((1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthren-1-yl)methanol
abieta-7,13-dien-18-al = (1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthrene-1-carbaldehyde
Other name(s): CYP720B1; PtAO; abietadienol hydroxylase (ambiguous)
Systematic name: abieta-7,13-dien-18-ol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (18-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses a step in the pathway of abietic acid biosynthesis. The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine) [1], and the gene encoding the enzyme has been identified in Pinus taeda (loblolly pine) [3]. The recombinant enzyme catalyses the oxidation of multiple diterpene alcohol and aldehydes, including levopimaradienol, isopimara-7,15-dienol, isopimara-7,15-dienal, dehydroabietadienol and dehydroabietadienal. It is not able to oxidize abietadiene.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Funk, C. and Croteau, R. Diterpenoid resin acid biosynthesis in conifers: characterization of two cytochrome P450-dependent monooxygenases and an aldehyde dehydrogenase involved in abietic acid biosynthesis. Arch. Biochem. Biophys. 308 (1994) 258-266. [PMID: 8311462]
2. Funk, C., Lewinsohn, E., Vogel, B.S., Steele, C.L. and Croteau, R. Regulation of oleoresinosis in grand fir (Abies grandis) (coordinate induction of monoterpene and diterpene cyclases and two cytochrome P450-dependent diterpenoid hydroxylases by stem wounding). Plant Physiol. 106 (1994) 999-1005. [PMID: 12232380]
3. Ro, D.K., Arimura, G., Lau, S.Y., Piers, E. and Bohlmann, J. Loblolly pine abietadienol/abietadienal oxidase PtAO (CYP720B1) is a multifunctional, multisubstrate cytochrome P450 monooxygenase. Proc. Natl. Acad. Sci. USA 102 (2005) 8060-8065. [PMID: 15911762]
Accepted name: geranylgeraniol 18-hydroxylase
Reaction: geranylgeraniol + [reduced NADPH—hemoprotein reductase] + O2 = 18-hydroxygeranylgeraniol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: plaunotol = 18-hydroxygeranylgeraniol
Other name(s): GGOH-18-hydroxylase
Systematic name: geranylgeraniol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (18-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Croton sublyratus.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Tansakul, P. and De-Eknamkul, W. Geranylgeraniol-18-hydroxylase: the last enzyme in the plaunotol biosynthetic pathway in Croton sublyratus. Phytochemistry 47 (1998) 1241-1246.
Accepted name: 22α-hydroxysteroid 23-monooxygenase
Reaction: (1) 3-epi-6-deoxocathasterone + [reduced NADPH—hemoprotein reductase] + O2 = 6-deoxotyphasterol + [oxidized NADPH—hemoprotein reductase] + H2O
(2) (22S,24R)-22-hydroxy-5α-ergostan-3-one + [reduced NADPH—hemoprotein reductase] + O2 = 3-dehydro-6-deoxoteasterone + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): cytochrome P450 90C1; CYP90D1; CYP90C1; 3-epi-6-deoxocathasterone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (C-23-hydroxylating); 3-epi-6-deoxocathasterone 23-monooxygenase
Systematic name: 22α-hydroxysteroid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (C-23-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein involved in brassinosteroid biosynthesis in plants. The enzyme has a relaxed substrate specificity, and C-23 hydroxylation can occur at different stages in the pathway. In Arabidopsis thaliana two isozymes, encoded by the CYP90C1 and CYP90D1 genes, have redundant activities.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Kim, G.T., Fujioka, S., Kozuka, T., Tax, F.E., Takatsuto, S., Yoshida, S. and Tsukaya, H. CYP90C1 and CYP90D1 are involved in different steps in the brassinosteroid biosynthesis pathway in Arabidopsis thaliana. Plant J. 41 (2005) 710-721. [PMID: 15703058]
2. Ohnishi, T., Szatmari, A.M., Watanabe, B., Fujita, S., Bancos, S., Koncz, C., Lafos, M., Shibata, K., Yokota, T., Sakata, K., Szekeres, M. and Mizutani, M. C-23 hydroxylation by Arabidopsis CYP90C1 and CYP90D1 reveals a novel shortcut in brassinosteroid biosynthesis. Plant Cell 18 (2006) 3275-3288. [PMID: 17138693]
Accepted name: angelicin synthase
Reaction: (+)-columbianetin + [reduced NADPH—hemoprotein reductase] + O2 = angelicin + [oxidized NADPH—hemoprotein reductase] + acetone + 2 H2O
For diagram of reaction click here.
Other name(s): CYP71AJ4 (gene name)
Systematic name: (+)-columbianetin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: This cytochrome P-450 (heme-thiolate) enzyme from wild parsnip is involved in the formation of angular furanocoumarins. Attacks its substrate by syn-elimination of hydrogen from C-3'.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Larbat, R., Hehn, A., Hans, J., Schneider, S., Jugde, H., Schneider, B., Matern, U. and Bourgaud, F. Isolation and functional characterization of CYP71AJ4 encoding for the first P450 monooxygenase of angular furanocoumarin biosynthesis. J. Biol. Chem. 284 (2009) 4776-4785. [PMID: 19098286]
Accepted name: 5-epiaristolochene 1,3-dihydroxylase
Reaction: 5-epiaristolochene + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = capsidiol + 2 [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of reaction click here.
Other name(s): 5-epi-aristolochene 1,3-dihydroxylase; EAH; CYP71D20
Systematic name: 5-epiaristolochene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (1- and 3-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. Kinetic studies suggest that 1β-hydroxyepiaristolochene is mainly formed first followed by hydroxylation at C-3. However the reverse order via 3α-hydroxyepiaristolochene does occur.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Ralston, L., Kwon, S.T., Schoenbeck, M., Ralston, J., Schenk, D.J., Coates, R.M. and Chappell, J. Cloning, heterologous expression, and functional characterization of 5-epi-aristolochene-1,3-dihydroxylase from tobacco (Nicotiana tabacum). Arch. Biochem. Biophys. 393 (2001) 222-235. [PMID: 11556809]
2. Takahashi, S., Zhao, Y., O'Maille, P.E., Greenhagen, B.T., Noel, J.P., Coates, R.M. and Chappell, J. Kinetic and molecular analysis of 5-epiaristolochene 1,3-dihydroxylase, a cytochrome P450 enzyme catalyzing successive hydroxylations of sesquiterpenes. J. Biol. Chem. 280 (2005) 3686-3696. [PMID: 15522862]
Accepted name: costunolide synthase
Reaction: germacra-1(10),4,11(13)-trien-12-oate + [reduced NADPH—hemoprotein reductase] + O2 = (+)-costunolide + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) germacra-1(10),4,11(13)-trien-12-oate + [reduced NADPH—hemoprotein reductase] + O2 = 6α-hydroxygermacra-1(10),4,11(13)-trien-12-oate + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 6α-hydroxygermacra-1(10),4,11(13)-trien-12-oate = (+)-costunolide + H2O (spontaneous)
For diagram of reaction click here.
Other name(s): CYP71BL2
Systematic name: germacra-1(10),4,11(13)-trien-12-oate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6α-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from chicory plants. The enzyme hydroxylates carbon C-6 of germacra-1(10),4,11(13)-trien-12-oate to give 6α-hydroxygermacra-1(10),4,11(13)-trien-12-oate, which spontaneously cyclises to form the lactone ring.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. de Kraker, J.W., Franssen, M.C., Joerink, M., de Groot, A. and Bouwmeester, H.J. Biosynthesis of costunolide, dihydrocostunolide, and leucodin. Demonstration of cytochrome p450-catalyzed formation of the lactone ring present in sesquiterpene lactones of chicory. Plant Physiol. 129 (2002) 257-268. [PMID: 12011356]
Accepted name: premnaspirodiene oxygenase
Reaction: (–)-vetispiradiene + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = solavetivone + 2 [oxidized NADPH—hemoprotein reductase] + 3 H2O (overall reaction)
(1a) (–)-vetispiradiene + [reduced NADPH—hemoprotein reductase] + O2 = solavetivol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) solavetivol + [reduced NADPH—hemoprotein reductase] + O2 = solavetivone + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of reaction click here.
Glossary: (–)-premnaspirodiene = (–)-vetispiradiene
Other name(s): HPO; Hyoscymus muticus premnaspirodiene oxygenase; CYP71D55
Systematic name: (–)-vetispiradiene,[reduced NADPH—hemoprotein reductase]:oxygen 2α-oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from the plant Hyoscymus muticus also hydroxylates valencene at C-2 to give the α-hydroxy compound, nootkatol, and this is converted into nootkatone. 5-Epiaristolochene and epieremophilene are hydroxylated at C-2 to give a 2β-hydroxy derivatives that are not oxidized further.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Takahashi, S., Yeo, Y.S., Zhao, Y., O'Maille, P.E., Greenhagen, B.T., Noel, J.P., Coates, R.M. and Chappell, J. Functional characterization of premnaspirodiene oxygenase, a cytochrome P450 catalyzing regio- and stereo-specific hydroxylations of diverse sesquiterpene substrates. J. Biol. Chem. 282 (2007) 31744-31754. [PMID: 17715131]
Accepted name: β-amyrin 11-oxidase
Reaction: β-amyrin + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = 11-oxo-β-amyrin + 2 [oxidized NADPH—hemoprotein reductase] + 3 H2O (overall reaction)
(1a) β-amyrin + [reduced NADPH—hemoprotein reductase] + O2 = 11α-hydroxy-β-amyrin + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 11α-hydroxy-β-amyrin + [reduced NADPH—hemoprotein reductase] + O2 = 11-oxo-β-amyrin + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of reaction click here.
Other name(s): CYP88D6
Systematic name: β-amyrin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from the plant Glycyrrhiza uralensis (Chinese licorice) that participates in the glycyrrhizin biosynthesis pathway. The enzyme is also able to oxidize 30-hydroxy-β-amyrin to 11α,30-dihydroxy-β-amyrin but this is not thought to be part of glycyrrhizin biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Seki, H., Ohyama, K., Sawai, S., Mizutani, M., Ohnishi, T., Sudo, H., Akashi, T., Aoki, T., Saito, K. and Muranaka, T. Licorice β-amyrin 11-oxidase, a cytochrome P450 with a key role in the biosynthesis of the triterpene sweetener glycyrrhizin. Proc. Natl. Acad. Sci. USA 105 (2008) 14204-14209. [PMID: 18779566]
Accepted name: indole-2-monooxygenase
Reaction: indole + [reduced NADPH—hemoprotein reductase] + O2 = indolin-2-one + [reduced NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): BX2 (gene name); CYP71C4 (gene name)
Systematic name: indole,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poaceae (grasses).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Frey, M., Chomet, P., Glawischnig, E., Stettner, C., Grün, S., Winklmair, A., Eisenreich, W., Bacher, A., Meeley, R.B., Briggs, S.P., Simcox, K. and Gierl, A. Analysis of a chemical plant defense mechanism in grasses. Science 277 (1997) 696-699. [PMID: 9235894]
2. Glawischnig, E., Grun, S., Frey, M. and Gierl, A. Cytochrome P450 monooxygenases of DIBOA biosynthesis: specificity and conservation among grasses. Phytochemistry 50 (1999) 925-930. [PMID: 10385992]
Accepted name: sterol 14α-demethylase
Reaction: a 14α-methylsteroid + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = a Δ14-steroid + formate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) a 14α-methylsteroid + [reduced NADPH—hemoprotein reductase] + O2 = a 14α-hydroxysteroid + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) a 14α-hydroxysteroid + [reduced NADPH—hemoprotein reductase] + O2 = a 14α-formylsteroid + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) a 14α-formylsteroid + [reduced NADPH—hemoprotein reductase] + O2 = a Δ14-steroid + formate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: obtusifoliol = 4α,14α-dimethyl-5α-ergosta-8,24(28)-dien-3β-ol or 4α,14α-dimethyl-24-methylene-5α-cholesta-8-en-3β-ol
Other name(s): obtusufoliol 14-demethylase; lanosterol 14-demethylase; lanosterol 14α-demethylase; sterol 14-demethylase; CYP51 (gene name); ERG11 (gene name)
Systematic name: sterol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (14-methyl cleaving)
Comments: This cytochrome P-450 (heme-thiolate) enzyme acts on a range of steroids with a 14α-methyl group, such as obtusifoliol and lanosterol. The enzyme catalyses a hydroxylation and a reduction of the 14α-methyl group, followed by a second hydroxylation, resulting in the elimination of formate and formation of a 14(15) double bond.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Alexander, K., Akhtar, M., Boar, R.B., McGhie, J.F. and Barton, D.H.R. The removal of the 32-carbon atom as formic acid in cholesterol biosynthesis. J. Chem. Soc. Chem. Commun. (1972) 383-385.
2. Aoyama, Y. and Yoshida, Y. Different substrate specificities of lanosterol 14α-demethylase (P-45014DM) of Saccharomyces cerevisiae and rat liver of 24-methylene-24,25-dihydrolanosterol and 24,25-dihydrolanosterol. Biochem. Biophys. Res. Commun. 178 (1991) 1064-1071. [PMID: 1872829]
3. Aoyama, Y. and Yoshida, Y. The 4β-methyl group of substrate does not affect the activity of lanosterol 14α-demethylase (P45014DM) of yeast: differences between the substrate recognition by yeast and plant sterol 14α-demethylases. Biochem. Biophys. Res. Commun. 183 (1992) 1266-1272. [PMID: 1567403]
4. Bak, S., Kahn, R.A., Olsen, C.E. and Halkier, B.A. Cloning and expression in Escherichia coli of the obtusifoliol 14α-demethylase of Sorghum bicolor (L.) Moench, a cytochrome P450 orthologous to the sterol 14α-demethylases (CYP51) from fungi and mammals. Plant J. 11 (1997) 191-201. [PMID: 9076987]
5. Aoyama, Y. and Yoshida, Y. The 4β-methyl group of substrate does not affect the activity of lanosterol 14α-demethylase (P45014DM) of yeast: differences between the substrate recognition by yeast and plant sterol 14α-demethylases. Biochem. Biophys. Res. Commun. 183 (1992) 1266-1272. [PMID: 1567403]
6. Bak, S., Kahn, R.A., Olsen, C.E. and Halkier, B.A. Cloning and expression in Escherichia coli of the obtusifoliol 14α-demethylase of Sorghum bicolor (L.) Moench, a cytochrome P450 orthologous to the sterol 14α-demethylases (CYP51) from fungi and mammals. Plant J. 11 (1997) 191-201. [PMID: 9076987]
Accepted name: 3,6-diketocamphane 1,2-monooxygenase
Reaction: (–)-bornane-2,5-dione + O2 + FMNH2 = (–)-5-oxo-1,2-campholide + FMN + H2O
Glossary: (–)-bornane-2,5-dione = 3,6-diketocamphane
Other name(s): 3,6-diketocamphane lactonizing enzyme; 3,6-DKCMO
Systematic name: (–)-bornane-2,5-dione,FMNH2:oxygen oxidoreductase (1,2-lactonizing)
Comments: A Baeyer-Villiger monooxygenase isolated from camphor-grown strains of Pseudomonas putida and encoded on the cam plasmid. Involved in the degradation of (–)-camphor. Requires a dedicated NADH-FMN reductase [cf. EC 1.5.1.42, FMN reductase (NADH)] [1-2]. The product spontaneously converts to [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Iwaki, H., Grosse, S., Bergeron, H., Leisch, H., Morley, K., Hasegawa, Y. and Lau, P.C. Camphor pathway redux: functional recombinant expression of 2,5- and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions. Appl. Environ. Microbiol. 79 (2013) 3282-3293. [PMID: 23524667]
2. Isupov, M.N., Schroder, E., Gibson, R.P., Beecher, J., Donadio, G., Saneei, V., Dcunha, S.A., McGhie, E.J., Sayer, C., Davenport, C.F., Lau, P.C., Hasegawa, Y., Iwaki, H., Kadow, M., Balke, K., Bornscheuer, U.T., Bourenkov, G. and Littlechild, J.A. The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida: the first crystal structure of a type II Baeyer-Villiger monooxygenase. Acta Crystallogr. D Biol. Crystallogr. 71 (2015) 2344-2353. [PMID: 26527149]
Accepted name: tryptophan N-monooxygenase
Reaction: L-tryptophan + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = (E)-indol-3-ylacetaldoxime + 2 [oxidized NADPH—hemoprotein reductase] + CO2 + 3 H2O (overall reaction)
(1a) L-tryptophan + [reduced NADPH—hemoprotein reductase] + O2 = N-hydroxy-L-tryptophan + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) N-hydroxy-L-tryptophan + [reduced NADPH—hemoprotein reductase] + O2 = N,N-dihydroxy-L-tryptophan + [oxidized NADPH—hemoprotein reductase] + H2O
(1c) N,N-dihydroxy-L-tryptophan = (E)-indol-3-ylacetaldoxime + CO2 + H2O
Other name(s): tryptophan N-hydroxylase; CYP79B1; CYP79B2; CYP79B3
Systematic name: L-tryptophan,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from the plant Arabidopsis thaliana. This enzyme catalyses two successive N-hydroxylations of L-tryptophan, the first steps in the biosynthesis of both auxin and the indole alkaloid phytoalexin camalexin. The product of the two hydroxylations, N,N-dihydroxy-L-tryptophan, is extremely labile and dehydrates spontaneously. The dehydrated product is then subject to a decarboxylation that produces an oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Mikkelsen, M.D., Hansen, C.H., Wittstock, U. and Halkier, B.A. Cytochrome P450 CYP79B2 from Arabidopsis catalyzes the conversion of tryptophan to indole-3-acetaldoxime, a precursor of indole glucosinolates and indole-3-acetic acid. J. Biol. Chem. 275 (2000) 33712-33717. [PMID: 10922360]
2. Hull, A.K., Vij, R. and Celenza, J.L. Arabidopsis cytochrome P450s that catalyze the first step of tryptophan-dependent indole-3-acetic acid biosynthesis. Proc. Natl. Acad. Sci. USA 97 (2000) 2379-2384. [PMID: 10681464]
3. Zhao, Y., Hull, A.K., Gupta, N.R., Goss, K.A., Alonso, J., Ecker, J.R., Normanly, J., Chory, J. and Celenza, J.L. Trp-dependent auxin biosynthesis in Arabidopsis: involvement of cytochrome P450s CYP79B2 and CYP79B3. Genes Dev. 16 (2002) 3100-3112. [PMID: 12464638]
4. Naur, P., Hansen, C.H., Bak, S., Hansen, B.G., Jensen, N.B., Nielsen, H.L. and Halkier, B.A. CYP79B1 from Sinapis alba converts tryptophan to indole-3-acetaldoxime. Arch. Biochem. Biophys. 409 (2003) 235-241. [PMID: 12464264]
Accepted name: indolin-2-one monooxygenase
Reaction: indolin-2-one + [reduced NADPH—hemoprotein reductase] + O2 = 3-hydroxyindolin-2-one + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here
Other name(s): BX3 (gene name); CYP71C2 (gene name)
Systematic name: indolin-2-one,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poaceae (grasses).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Frey, M., Chomet, P., Glawischnig, E., Stettner, C., Grün, S., Winklmair, A., Eisenreich, W., Bacher, A., Meeley, R.B., Briggs, S.P., Simcox, K. and Gierl, A. Analysis of a chemical plant defense mechanism in grasses. Science 277 (1997) 696-699. [PMID: 9235894]
2. Glawischnig, E., Grun, S., Frey, M. and Gierl, A. Cytochrome P450 monooxygenases of DIBOA biosynthesis: specificity and conservation among grasses. Phytochemistry 50 (1999) 925-930. [PMID: 10385992]
Accepted name: carotenoid ε hydroxylase
Reaction: (1) α-carotene + [reduced NADPH-hemoprotein reductase] + O2 = α-cryptoxanthin + [oxidized NADPH-hemoprotein reductase] + H2O
(2) zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2 = lutein + [oxidized NADPH-hemoprotein reductase] + H2O
For diagram of reaction click here
Other name(s): CYP97C1; LUT1; CYP97C; carotene ε-monooxygenase
Systematic name: α-carotene,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating)
Comments: A P-450 (heme-thiolate) protein.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Pogson, B., McDonald, K.A., Truong, M., Britton, G. and DellaPenna, D. Arabidopsis carotenoid mutants demonstrate that lutein is not essential for photosynthesis in higher plants. Plant Cell 8 (1996) 1627-1639. [PMID: 8837513]
2. Tian, L., Musetti, V., Kim, J., Magallanes-Lundback, M. and DellaPenna, D. The Arabidopsis LUT1 locus encodes a member of the cytochrome P450 family that is required for carotenoid ε-ring hydroxylation activity. Proc. Natl. Acad. Sci. USA 101 (2004) 402-407. [PMID: 14709673]
3. Stigliani, A.L., Giorio, G. and D'Ambrosio, C. Characterization of P450 carotenoid β- and ε-hydroxylases of tomato and transcriptional regulation of xanthophyll biosynthesis in root, leaf, petal and fruit. Plant Cell Physiol 52 (2011) 851-865. [PMID: 21450689]
4. Chang, S., Berman, J., Sheng, Y., Wang, Y., Capell, T., Shi, L., Ni, X., Sandmann, G., Christou, P. and Zhu, C. Cloning and functional characterization of the maize (Zea mays L.) Carotenoid Epsilon Hydroxylase Gene. PLoS One 10 (2015) e0128758. [PMID: 26030746]
5. Reddy, C.S., Lee, S.H., Yoon, J.S., Kim, J.K., Lee, S.W., Hur, M., Koo, S.C., Meilan, J., Lee, W.M., Jang, J.K., Hur, Y., Park, S.U. and Kim, A.YB. Molecular cloning and characterization of carotenoid pathway genes and carotenoid content in Ixeris dentata var. albiflora. Molecules 22 (2017) . [PMID: 28858245]
Accepted name: dolabradiene monooxygenase
Reaction: (1) dolabradiene + O2 + [reduced NADPH—hemoprotein reductase] = 15,16-epoxydolabrene + H2O + [oxidized NADPH—hemoprotein reductase]
(2) 15,16-epoxydolabrene + O2 + [reduced NADPH—hemoprotein reductase] = 3β-hydroxy-15,16-epoxydolabrene + H2O + [oxidized NADPH—hemoprotein reductase]
For diagram of reaction click here.
Glossary: dolabradiene = (4aS,4bR,7S,8aR,10aS)-7-ethenyl-4b,7,10a-trimethyl-1-methylidenetetradecahydrophenanthrene
Other name(s): CYP71Z16 (gene name)
Systematic name: dolabradiene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3β-hydroxy-15,16-epoxydolabrene-forming)
Comments: A cytochrome P-450 (heme thiolate) enzyme characterized from maize. The enzyme catalyses the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Mafu, S., Ding, Y., Murphy, K.M., Yaacoobi, O., Addison, J.B., Wang, Q., Shen, Z., Briggs, S.P., Bohlmann, J., Castro-Falcon, G., Hughes, C.C., Betsiashvili, M., Huffaker, A., Schmelz, E.A. and Zerbe, P. Discovery, biosynthesis and stress-related accumulation of dolabradiene-derived defenses in maize. Plant Physiol. 176 (2018) 2677-2690. [PMID: 29475898]
Accepted name: zealexin A1 synthase
Reaction: (S)-β-macrocarpene + 3 O2 + 3 [reduced NADPH—hemoprotein reductase] = zealexin A1 + 4 H2O + 3 [oxidized NADPH—hemoprotein reductase] (overall reaction)
(1a) (S)-β-macrocarpene + O2 + [reduced NADPH—hemoprotein reductase] = [(4S)-4-(5,5-dimethylcyclohex-1-en-1-yl)-cyclohex-1-en-1-yl]methanol + H2O + [oxidized NADPH—hemoprotein reductase]
(1b) [(4S)-4-(5,5-dimethylcyclohex-1-en-1-yl)-cyclohex-1-en-1-yl] methanol + O2 + [reduced NADPH—hemoprotein reductase] = (4S)-4-(5,5-dimethylcyclohex-1-en-1-yl)cyclohex-1-ene-1-carbaldehyde + 2 H2O + [oxidized NADPH—hemoprotein reductase]
(1c) (4S)-4-(5,5-dimethylcyclohex-1-en-1-yl)cyclohex-1-ene-1-carbaldehyde + O2 + [reduced NADPH—hemoprotein reductase] = zealexin A1 + H2O + [oxidized NADPH—hemoprotein reductase]
For diagram of reaction click here
Glossary: (S)-β-macrocarpene = (1'S)-4',5,5-trimethyl-1,1'-bi(cyclohexane)-1,3'-diene
zealexin A1 = (4S)-4-(5,5-dimethylcyclohex-1-en-1-yl)cyclohex-1-ene-1-carboxylate
Other name(s): CYP71Z18 (gene name)
Systematic name: (S)-β-macrocarpene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (zealexin A1-forming)
Comments: A cytochrome P-450 (heme thiolate) enzyme characterized from maize. The enzyme sequentially oxidizes(S)-β-macrocarpene via alcohol and aldehyde intermediates to form zealexin A1, a maize phytoalexin that provides biochemical protection against fungal infection.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Mao, H., Liu, J., Ren, F., Peters, R.J. and Wang, Q. Characterization of CYP71Z18 indicates a role in maize zealexin biosynthesis. Phytochemistry 121 (2016) 4-10. [PMID: 26471326]
Accepted name: nepetalactol monooxygenase
Reaction: (+)-cis,trans-nepetalactol + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = 7-deoxyloganetate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) (+)-cis,trans-nepetalactol + [reduced NADPH—hemoprotein reductase] + O2 = 7-deoxyloganetic alcohol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 7-deoxyloganetic alcohol + [reduced NADPH—hemoprotein reductase] + O2 = iridotrial + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) iridotrial + [reduced NADPH—hemoprotein reductase] + O2 = 7-deoxyloganetate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here
Glossary: (+)-cis,trans-nepetalactol = (4aS,7S,7aR)-4,7-dimethyl-1,4a,5,6,7,7a-hexahydrocyclopenta[c]pyran-1-ol
7-deoxyloganetate = (1S,4aS,7S,7aR)-1-hydroxy-7-methyl-1,4a,5,6,7,7a-hexahydrocyclopenta[c]pyran-4-carboxylate
Other name(s): CYP76A26 (gene name); iridoid oxidase (misleading)
Systematic name: (+)-cis,trans-nepetalactol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (hydroxylating)
Comments: The enzyme, characterized from the plant Catharanthus roseus, is a cytochrome P-450 (heme thiolate) protein. It catalyses three successive reactions in the pathway leading to biosynthesis of monoterpenoid indole alkaloids.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. 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]
Accepted name: flavanone 2-hydroxylase
Reaction: a flavanone + [reduced NADPH—hemoprotein reductase] + O2 = a 2-hydroxyflavanone + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here or click here
Other name(s): CYP93G2 (gene name); CYP93B1 (gene name); (2S)-flavanone 2-hydroxylase; ; licodione synthase
Systematic name: flavanone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2-hydroxylating)
Comments: A cytochrome P-450 (heme thiolate) plant enzyme that catalyses the 2-hydroxylation of multiple flavanones such as (2S)-naringenin, (2S)-eriodictyol, (2S)-pinocembrin, and (2S)-liquiritigenin. The products are meta-stable and exist in an equilibrium with open forms such as 1-(4-hydroxyphenyl)-3-(2,4,6-trihydroxyphenyl)propane-1,3-dione.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Otani, K., Takahashi, T., Furuya, T. and Ayabe, S. Licodione synthase, a cytochrome P450 monooxygenase catalyzing 2-hydroxylation of 5-deoxyflavanone, in cultured Glycyrrhiza echinata L. cells. Plant Physiol. 105 (1994) 1427-1432. [PMID: 12232298]
2. Akashi, T., Aoki, T. and Ayabe, S. Identification of a cytochrome P450 cDNA encoding (2S)-flavanone 2-hydroxylase of licorice (Glycyrrhiza echinata L.; Fabaceae) which represents licodione synthase and flavone synthase II. FEBS Lett. 431 (1998) 287-290. [PMID: 9708921]
3. Du, Y., Chu, H., Chu, I.K. and Lo, C. CYP93G2 is a flavanone 2-hydroxylase required for C-glycosylflavone biosynthesis in rice. Plant Physiol. 154 (2010) 324-333. [PMID: 20647377]
Accepted name: (S)-1-hydroxy-N-methylcanadine 13-hydroxylase
Reaction: (S)-1-hydroxy-N-methylcanadine + [reduced NADPH—hemoprotein reductase] + O2 = (13S,14R)-1,13-dihydroxy-N-methylcanadine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): CYP82X2 (gene name)
Systematic name: (S)-1-hydroxy-N-methylcanadine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (13-hydroxylating)
Comments: The enzyme, characterized from the plant Papaver somniferum (opium poppy), participates in the biosynthesis of the isoquinoline alkaloid noscapine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Dang, T.T., Chen, X. and Facchini, P.J. Acetylation serves as a protective group in noscapine biosynthesis in opium poppy. Nat. Chem. Biol. 11 (2015) 104-106. [PMID: 25485687]
2. Li, Y. and Smolke, C.D. Engineering biosynthesis of the anticancer alkaloid noscapine in yeast. Nat Commun 7 (2016) 12137. [PMID: 27378283]
3. Li, Y., Li, S., Thodey, K., Trenchard, I., Cravens, A. and Smolke, C.D. Complete biosynthesis of noscapine and halogenated alkaloids in yeast. Proc. Natl Acad. Sci. USA 115 (2018) E3922-E3931. [PMID: 29610307]
Accepted name: fraxetin 5-hydroxylase
Reaction: fraxetin + [reduced NADPH—hemoprotein reductase] + O2 = sideretin (reduced form) + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: fraxetin = 7,8-dihydroxy-6-methoxy-2H-chromen-2-one
sideretin (reduced form) = 5,7,8-trihydroxy-6-methoxy-2H-chromen-2-one
Other name(s): CYP82C4; fraxetin 5-monooxygenase
Systematic name: fraxetin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (5-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein involved in biosynthesis of iron(III)-chelating coumarins in higher plants.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Rajniak, J., Giehl, R.FH., Chang, E., Murgia, I., von Wiren, N. and Sattely, E.S. Biosynthesis of redox-active metabolites in response to iron deficiency in plants. Nat. Chem. Biol. 14 (2018) 442-450. [PMID: 29581584]
Accepted name: indole-3-carbonyl nitrile 4-hydroxylase
Reaction: indole-3-carbonyl nitrile + [reduced NADPH—hemoprotein reductase] + O2 = 4-hydroxyindole-3-carbonyl nitrile + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: indole-3-carbonyl nitrile = 2-(1H-indole-3-yl)-2-oxoacetonitrile
4-hydroxyindole-3-carbonyl nitrile = 2-(4-hydroxy-1H-indole-3-yl)-2-oxoacetonitrile
Other name(s): CYP82C2
Systematic name: indole-3-carbonyl nitrile,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (4-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein characterized from the plant Arabidopsis thaliana. Involved in biosynthesis of small cyanogenic compounds that take part in pathogen defense. The enzyme also catalyses the 5-hydroxylation of xanthotoxin [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kruse, T., Ho, K., Yoo, H.D., Johnson, T., Hippely, M., Park, J.H., Flavell, R. and Bobzin, S. In planta biocatalysis screen of P450s identifies 8-methoxypsoralen as a substrate for the CYP82C subfamily, yielding original chemical structures. Chem. Biol. 15 (2008) 149-156. [PMID: 18291319]
2. Rajniak, J., Barco, B., Clay, N.K. and Sattely, E.S. A new cyanogenic metabolite in Arabidopsis required for inducible pathogen defence. Nature 525 (2015) 376-379. [PMID: 26352477]
Accepted name: (S)-N-methylcanadine 1-hydroxylase
Reaction: (S)-cis-N-methylcanadine + [reduced NADPH—hemoprotein reductase] + O2 = (S)-1-hydroxy-cis-N-methylcanadine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): CYP82Y1 (gene name)
Systematic name: (S)-cis-N-methylcanadine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (1-hydroxylating)
Comments: This cytochrome P-450 (heme-thiolate) enzyme, characterized from the plant Papaver somniferum (opium poppy), participates in the biosynthesis of the isoquinoline alkaloid noscapine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Dang, T.T. and Facchini, P.J. CYP82Y1 is N-methylcanadine 1-hydroxylase, a key noscapine biosynthetic enzyme in opium poppy. J. Biol. Chem 289 (2014) 2013-2026. [PMID: 24324259]
2. Li, Y., Li, S., Thodey, K., Trenchard, I., Cravens, A. and Smolke, C.D. Complete biosynthesis of noscapine and halogenated alkaloids in yeast. Proc. Natl Acad. Sci. USA 115 (2018) E3922-E3931. [PMID: 29610307]
Accepted name: (13S,14R)-13-O-acetyl-1-hydroxy-N-methylcanadine 8-hydroxylase
Reaction: (13S,14R)-13-O-acetyl-1-hydroxy-N-methylcanadine + [reduced NADPH—hemoprotein reductase] + O2 = (13S,14R)-13-O-acetyl-1,8-dihydroxy-N-methylcanadine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Other name(s): CYP82X1 (gene name)
Systematic name: (13S,14R)-13-O-acetyl-1-hydroxy-N-methylcanadine 8-hydroxylase,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (8-hydroxylating)
Comments: This cytochrome P-450 (heme-thiolate) enzyme, characterized from the plant Papaver somniferum (opium poppy), participates in the biosynthesis of the isoquinoline alkaloid noscapine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Dang, T.T., Chen, X. and Facchini, P.J. Acetylation serves as a protective group in noscapine biosynthesis in opium poppy. Nat. Chem. Biol. 11 (2015) 104-106. [PMID: 25485687]
2. Li, Y. and Smolke, C.D. Engineering biosynthesis of the anticancer alkaloid noscapine in yeast. Nat Commun 7 (2016) 12137. [PMID: 27378283]
3. Li, Y., Li, S., Thodey, K., Trenchard, I., Cravens, A. and Smolke, C.D. Complete biosynthesis of noscapine and halogenated alkaloids in yeast. Proc. Natl Acad. Sci. USA 115 (2018) E3922-E3931. [PMID: 29610307]
Accepted name: germacrene A acid 8β-hydroxylase
Reaction: germacra-1(10),4,11(13)-trien-12-oate + [reduced NADPH—hemoprotein reductase] + O2 = 8β-hydroxygermacra-1(10),4,11(13)-trien-12-oate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here.
Glossary: germacra-1(10),4,11(13)-trien-12-oate = germacrene A acid
8β-hydroxygermacra-1(10),4,11(13)-triene-12-oate = 8β-hydroxygermacrene A acid
inunolide = germacra-1(10),4,11(13)-trien-12,8β-lactone
8-epi-inunolide = germacra-1(10),4,11(13)-trien-12,8α-lactone
Other name(s): HaG8H; CYP71BL1; CYP71BL6
Systematic name: germacra-1(10),4,11(13)-trien-12-oate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (8β-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from the plant Helianthus annuus (common sunflower). The cyclisation of 8β-hydroxygermacra-1(10),4,11(13)-triene-12-oate to inunolide (12,8β) does not seem to occur spontaneously. The enzyme from Inula hupehensis also forms some 8α-hydroxygermacra-1(10),4,11(13)-triene-12-oate, which spontaneously cyclises to 8-epi-inunolide (12,8α) (cf. EC 1.14.14.170 8-epi-inunolide synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Frey, M., Schmauder, K., Pateraki, I. and Spring, O. Biosynthesis of eupatolide-A metabolic route for sesquiterpene lactone formation involving the P450 enzyme CYP71DD6. ACS Chem. Biol. 13 (2018) 1536-1543. [PMID: 29758164]
2. Gou, J., Hao, F., Huang, C., Kwon, M., Chen, F., Li, C., Liu, C., Ro, D.K., Tang, H. and Zhang, Y. Discovery of a non-stereoselective cytochrome P450 catalyzing either 8α- or 8β-hydroxylation of germacrene A acid from the Chinese medicinal plant, Inula hupehensis. Plant J. 93 (2018) 92-106. [PMID: 29086444]
Accepted name: eupatolide synthase
Reaction: 8β-hydroxygermacra-1(10),4,11(13)-trien-12-oate + [reduced NADPH—hemoprotein reductase] + O2 = eupatolide + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) 8β-hydroxygermacra-1(10),4,11(13)-trien-12-oate + [reduced NADPH—hemoprotein reductase] + O2 = 6α,8β-dihydroxygermacra-1(10),4,11(13)-trien-12-oate + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 6α,8β-dihydroxygermacra-1(10),4,11(13)-trien-12-oate = eupatolide + H2O (spontaneous)
For diagram of reaction click here.
Glossary: 8β-hydroxygermacra-1(10),4,11(13)-triene-12-oate = 8β-hydroxygermacrene A acid
eupatolide = 8β-hydroxygermacra-1(10),4,11(13)-trien-12,6α-lactone
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
Other name(s): CYP71DD6; HaES
Systematic name: 8β-hydroxygermacra-1(10),4,11(13)-trien-12-oate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6α-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from the plant Helianthus annuus (common sunflower).
References:
1. Frey, M., Schmauder, K., Pateraki, I. and Spring, O. Biosynthesis of eupatolide-A metabolic route for sesquiterpene lactone formation involving the P450 enzyme CYP71DD6. ACS Chem. Biol. 13 (2018) 1536-1543. [PMID: 29758164]
Accepted name: 8-epi-inunolide synthase
Reaction: germacra-1(10),4,11(13)-trien-12-oate + [reduced NADPH—hemoprotein reductase] + O2 = 8-epi-inunolide + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) germacra-1(10),4,11(13)-trien-12-oate + [reduced NADPH—hemoprotein reductase] + O2 = 8α-hydroxygermacra-1(10),4,11(13)-trien-12-oate + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 8α-hydroxygermacra-1(10),4,11(13)-trien-12-oate = 8-epi-inunolide + H2O (spontaneous)
Glossary: 8-epi-inunolide = germacra-1(10),4,11(13)-trien-12,8α-lactone
Other name(s): CYP71BL1
Systematic name: germacra-1(10),4,11(13)-trien-12-oate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (8α-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from the plant Inula hupehensis. The enzyme also produces 8β-hydroxygermacra-1(10),4,11(13)-triene-12-oate (EC 1.14.14.168, germacrene A acid 8β-hydroxylase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Gou, J., Hao, F., Huang, C., Kwon, M., Chen, F., Li, C., Liu, C., Ro, D.K., Tang, H. and Zhang, Y. Discovery of a non-stereoselective cytochrome P450 catalyzing either 8α- or 8β-hydroxylation of germacrene A acid from the Chinese medicinal plant, Inula hupehensis. Plant J. 93 (2018) 92-106. [PMID: 29086444]
Accepted name: β-amyrin 16α-hydroxylase
Reaction: β-amyrin + [reduced NADPH—hemoprotein reductase] + O2 = 16α-hydroxy-β-amyrin + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here
Glossary: 16α-hydroxy-β-amyrin = olean-12-ene-3β,16α-diol
Other name(s): CYP87D16
Systematic name: β-amyrin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (16α-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Maesa lanceolata (false assegai). Involved in the biosynthesis of maesasaponins. It also acts on some derivatives of β-amyrin such as erythrodiol or oleanolic acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Moses, T., Pollier, J., Almagro, L., Buyst, D., Van Montagu, M., Pedreño, M.A., Martins, J.C., Thevelein, J.M. and Goossens, A. Combinatorial biosynthesis of sapogenins and saponins in Saccharomyces cerevisiae using a C-16α hydroxylase from Bupleurum falcatum. Proc. Natl Acad. Sci. USA 111 (2014) 1634-1639. [PMID: 24434554]
2. Moses, T., Pollier, J., Faizal, A., Apers, S., Pieters, L., Thevelein, J.M., Geelen, D. and Goossens, A. Unraveling the triterpenoid saponin biosynthesis of the African shrub Maesa lanceolata. Mol. Plant 8 (2015) 122-135. [PMID: 25578277]
Accepted name: 3,5,6-trichloropyridin-2-ol monooxygenase
Reaction: (1) 3,5,6-trichloropyridin-2-ol + FADH2 + O2 = 3,6-dichloropyridine-2,5-dione + Cl- + FAD + H2O
(2) 3,6-dichloropyridine-2,5-diol + FADH2 + O2 = 6-chloro-3-hydroxypyridine-2,5-dione + Cl- + FAD + H2O
(3) 6-chloropyridine-2,3,5-triol + FADH2 + O2 = 3,6-dihydroxypyridine-2,5-dione + Cl- + FAD + H2O
Other name(s): tcpA (gene name)
Systematic name: 3,5,6-trichloropyridin-2-ol,FADH2:oxygen oxidoreductase (dechlorinating)
Comments: The enzyme, characterized from a number of bacterial species, participates in the degradation of 3,5,6-trichloropyridin-2-ol (TCP), a metabolite of the common organophosphorus insecticide chlorpyrifos. The enzyme is a multifunctional flavin-dependent monooxygenase that displaces three chlorine atoms by attacking three different positions in the substrate. Each reaction catalysed by the enzyme displaces a single chlorine and results in formation of a dione, which must be reduced by FADH2 before the monooxygenase could catalyse the next step. The large amount of FADH2 that is required is generated by a dedicated flavin reductase (TcpX). cf. EC 1.14.14.173, 2,4,6-trichlorophenol monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Li, J., Huang, Y., Hou, Y., Li, X., Cao, H. and Cui, Z. Novel gene clusters and metabolic pathway involved in 3,5,6-trichloro-2-pyridinol degradation by Ralstonia sp. strain T6. Appl. Environ. Microbiol. 79 (2013) 7445-7453. [PMID: 24056464]
2. Fang, L., Shi, T., Chen, Y., Wu, X., Zhang, C., Tang, X., Li, Q.X. and Hua, R. Kinetics and catabolic pathways of the insecticide chlorpyrifos, annotation of the degradation genes, and characterization of enzymes TcpA and Fre in Cupriavidus nantongensis X1(T). J. Agric. Food Chem. 67 (2019) 2245-2254. [PMID: 30721044]
Accepted name: 2,4,6-trichlorophenol monooxygenase
Reaction: 2,4,6-trichlorophenol + FADH2 + O2 = 6-chloro-2-hydroxy-1,4-benzoquinone + 2 Cl- + FAD (overall reaction)
(1a) 2,4,6-trichlorophenol + FADH2 + O2 = 2,6-dichloro-1,4-benzoquinone + Cl- + FAD + H2O
(1b) 2,6-dichloro-1,4-benzoquinone + H2O = 6-chloro-2-hydroxy-1,4-benzoquinone + Cl-
Other name(s): tcpA (gene name)
Systematic name: 2,4,6-trichlorophenol,FADH2:oxygen oxidoreductase (dechlorinating)
Comments: The enzyme, characterized from Cupriavidus pinatubonensis, participates in the degradation of 2,4,6-trichlorophenol, a compound that has been used for decades as a wood preservative. The enzyme is a multifunctional flavin-dependent monooxygenase that catalyses two different reactions to displace two chlorine atoms, a monooxygenase reaction followed by a hydrolysis reaction that takes advantage of the reactivity of the product of the first reaction, 2,6-dichloro-1,4-benzoquinone [2]. The large amount of FADH2 that is required is generated by a dedicated flavin reductase (TcpB). cf. EC 1.14.14.172, 3,5,6-trichloropyridin-2-ol monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Louie, T.M., Webster, C.M. and Xun, L. Genetic and biochemical characterization of a 2,4,6-trichlorophenol degradation pathway in Ralstonia eutropha JMP134. J. Bacteriol. 184 (2002) 3492-3500. [PMID: 12057943]
2. Xun, L. and Webster, C.M. A monooxygenase catalyzes sequential dechlorinations of 2,4,6-trichlorophenol by oxidative and hydrolytic reactions. J. Biol. Chem. 279 (2004) 6696-6700. [PMID: 14662756]
3. Hayes, R.P., Webb, B.N., Subramanian, A.K., Nissen, M., Popchock, A., Xun, L. and Kang, C. Structural and catalytic differences between two FADH2-dependent monooxygenases: 2,4,5-TCP 4-monooxygenase (TftD) from Burkholderia cepacia AC1100 and 2,4,6-TCP 4-monooxygenase (TcpA) from Cupriavidus necator JMP134. Int. J. Mol. Sci. 13 (2012) 9769-9784. [PMID: 22949829]
Accepted name: geranylhydroquinone 3''-hydroxylase
Reaction: geranylhydroquinone + [reduced NADPH—hemoprotein reductase] + O2 = 3''-hydroxygeranylhydroquinone + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: 3''-hydroxygeranylhydroquinone = 2-[(2Z)-3-(hydroxymethyl)-7-methylocta-2,6-dien-1-yl]benzene-1,4-diol
Other name(s): GHQ 3''-hydroxylase; CYP76B74 (gene name); geranylhydroquinone,NADPH:oxygen oxidoreductase (3''-hydroxylating)
Systematic name: geranylhydroquinone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3''-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants, where it is part of the biosynthesis pathway of the red naphthoquinone pigment shikonin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Yamamoto, H., Inoue, K., Li, S.M. and Heide, L. Geranylhydroquinone 3''-hydroxylase, a cytochrome P-450 monooxygenase from Lithospermum erythrorhizon cell suspension cultures. Planta 210 (2000) 312-317. [PMID: 10664138]
2. Wang, S., Wang, R., Liu, T., Lv, C., Liang, J., Kang, C., Zhou, L., Guo, J., Cui, G., Zhang, Y., Werck-Reichhart, D., Guo, L. and Huang, L. CYP76B74 catalyzes the 3''-hydroxylation of geranylhydroquinone in shikonin biosynthesis. Plant Physiol. 179 (2019) 402-414. [PMID: 30498024]
Accepted name: ferruginol synthase
Reaction: abieta-8,11,13-triene + [reduced NADPH—hemoprotein reductase] + O2 = ferruginol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of abietane diterpenoids biosynthesis, click here
Glossary: ferruginol = abieta-8,11,13-trien-12-ol
Other name(s): miltiradiene oxidase (incorrect); CYP76AH1; miltiradiene,NADPH:oxygen oxidoreductase (ferruginol forming) (incorrect)
Systematic name: abieta-8,11,13-triene,[NADPH–hemoprotein reductase]:oxygen 12-oxidoreductase (ferruginol-forming)
Comments: A cytochrome P-450 (heme thiolate) enzyme found in some members of the Lamiaceae (mint family). The enzyme from Rosmarinus officinalis (rosemary) is involved in biosynthesis of carnosic acid, while the enzyme from the Chinese medicinal herb Salvia miltiorrhiza is involved in the biosynthesis of the tanshinones, abietane-type norditerpenoid naphthoquinones that are the main lipophilic bioactive components found in the plant.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Guo, J., Zhou, Y.J., Hillwig, M.L., Shen, Y., Yang, L., Wang, Y., Zhang, X., Liu, W., Peters, R.J., Chen, X., Zhao, Z.K. and Huang, L. CYP76AH1 catalyzes turnover of miltiradiene in tanshinones biosynthesis and enables heterologous production of ferruginol in yeasts. Proc. Natl. Acad. Sci. USA 110 (2013) 12108-12113. [PMID: 23812755]
2. Zi, J. and Peters, R.J. Characterization of CYP76AH4 clarifies phenolic diterpenoid biosynthesis in the Lamiaceae. Org. Biomol. Chem. 11 (2013) 7650-7652. [PMID: 24108414]
3. Bozic, D., Papaefthimiou, D., Bruckner, K., de Vos, R.C., Tsoleridis, C.A., Katsarou, D., Papanikolaou, A., Pateraki, I., Chatzopoulou, F.M., Dimitriadou, E., Kostas, S., Manzano, D., Scheler, U., Ferrer, A., Tissier, A., Makris, A.M., Kampranis, S.C. and Kanellis, A.K. Towards elucidating carnosic acid biosynthesis in Lamiaceae: functional characterization of the three first steps of the pathway in Salvia fruticosa and Rosmarinus officinalis. PLoS One 10 (2015) e0124106. [PMID: 26020634]
Accepted name: taxadiene 5α-hydroxylase
Reaction: taxa-4,11-diene + [reduced NADPH–hemoprotein reductase] + O2 = taxa-4(20),11-dien-5α-ol + [oxidized NADPH–hemoprotein reductase] + H2O
For diagram of taxadiene hydroxylation, click here
Systematic name: taxa-4,11-diene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (5α-hydroxylating)
Comments: This microsomal cytochrome-P-450 enzyme is involved in the biosynthesis of the diterpenoid antineoplastic drug taxol (paclitaxel). The reaction includes rearrangement of the 4(5)-double bond to a 4(20)-double bond, possibly through allylic oxidation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Hefner, J., Rubenstein, S.M., Ketchum, R.E., Gibson, D.M., Williams, R.M. and Croteau, R. Cytochrome P450-catalyzed hydroxylation of taxa-4(5),11(12)-diene to taxa-4(20),11(12)-dien-5α-ol: the first oxygenation step in taxol biosynthesis. Chem. Biol. 3 (1996) 479-489. [PMID: 8807878]
Accepted name: ultra-long-chain fatty acid ω-hydroxylase
Reaction: an ultra-long-chain fatty acid + [reduced NADPH—hemoprotein reductase] + O2 = an ultra-long-chain ω-hydroxy fatty acid + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): CYP4F22 (gene name)
Systematic name: ultra-long-chain fatty acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ω-hydroxylating)
Comments: The enzyme, which is expressed in the epidermis of mammals, catalyses the ω-hydroxylation of ultra-long-chain fatty acids (C28 to C36). The products are incorporated into acylceramides, epidermis-specific ceramide species that are very important for skin barrier formation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Ohno, Y., Nakamichi, S., Ohkuni, A., Kamiyama, N., Naoe, A., Tsujimura, H., Yokose, U., Sugiura, K., Ishikawa, J., Akiyama, M. and Kihara, A. Essential role of the cytochrome P450 CYP4F22 in the production of acylceramide, the key lipid for skin permeability barrier formation. Proc. Natl. Acad. Sci. USA 112 (2015) 7707-7712. [PMID: 26056268]
Accepted name: steroid 22S-hydroxylase
Reaction: (1) a C27-steroid + O2 + [reduced NADPH—hemoprotein reductase] = a (22S)-22-hydroxy-C27-steroid + 2 H2O + [oxidized NADPH—hemoprotein reductase]
(2) a C28-steroid + O2 + [reduced NADPH—hemoprotein reductase] = a (22S)-22-hydroxy-C28-steroid + 2 H2O + [oxidized NADPH—hemoprotein reductase]
(3) a C29-steroid + O2 + [reduced NADPH—hemoprotein reductase] = a (22S)-22-hydroxy-C29-steroid + 2 H2O + [oxidized NADPH—hemoprotein reductase]
Other name(s): CYP90B1 (gene name); DWF4 (gene name); steroid C-22 hydroxylase
Systematic name: steroid,NADPH—hemoprotein reductase:oxygen 22S-oxidoreductase (hydroxylating)
Comments: This plant cytochrome P-450 (heme thiolate) enzyme participates in the biosynthesis of brassinosteroids. While in vivo substrates include C28-steroids such as campestanol, campesterol, and 6-oxocampestanol, the enzyme is able to catalyse the C-22 hydroxylation of a variety of C27, C28 and C29 steroids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Asami, T., Mizutani, M., Fujioka, S., Goda, H., Min, Y.K., Shimada, Y., Nakano, T., Takatsuto, S., Matsuyama, T., Nagata, N., Sakata, K. and Yoshida, S. Selective interaction of triazole derivatives with DWF4, a cytochrome P450 monooxygenase of the brassinosteroid biosynthetic pathway, correlates with brassinosteroid deficiency in planta. J. Biol. Chem. 276 (2001) 25687-25691. [PMID: 11319239]
2. Choe, S., Fujioka, S., Noguchi, T., Takatsuto, S., Yoshida, S. and Feldmann, K.A. Overexpression of DWARF4 in the brassinosteroid biosynthetic pathway results in increased vegetative growth and seed yield in Arabidopsis. Plant J. 26 (2001) 573-582. [PMID: 11489171]
3. Asami, T., Mizutani, M., Shimada, Y., Goda, H., Kitahata, N., Sekimata, K., Han, S.Y., Fujioka, S., Takatsuto, S., Sakata, K. and Yoshida, S. Triadimefon, a fungicidal triazole-type P450 inhibitor, induces brassinosteroid deficiency-like phenotypes in plants and binds to DWF4 protein in the brassinosteroid biosynthesis pathway. Biochem. J. 369 (2003) 71-76. [PMID: 12350224]
4. Fujita, S., Ohnishi, T., Watanabe, B., Yokota, T., Takatsuto, S., Fujioka, S., Yoshida, S., Sakata, K. and Mizutani, M. Arabidopsis CYP90B1 catalyses the early C-22 hydroxylation of C27, C28 and C29 sterols. Plant J. 45 (2006) 765-774. [PMID: 16460510]
5. Ohnishi, T., Watanabe, B., Sakata, K. and Mizutani, M. CYP724B2 and CYP90B3 function in the early C-22 hydroxylation steps of brassinosteroid biosynthetic pathway in tomato. Biosci. Biotechnol. Biochem. 70 (2006) 2071-2080. [PMID: 16960392]
Accepted name: brassinosteroid 6-oxygenase
Reaction: 6-deoxocastasterone + 2 O2 + 2 [reduced NADPH—hemoprotein reductase] = castasterone + 3 H2O + 2 [oxidized NADPH—hemoprotein reductase] (overall reaction)
(1a) 6-deoxocastasterone + O2 + [reduced NADPH—hemoprotein reductase] = 6α-hydroxy-6-deoxocastasterone + H2O + [oxidized NADPH—hemoprotein reductase]
(1b) 6α-hydroxy-6-deoxocastasterone + O2 + [reduced NADPH—hemoprotein reductase] = castasterone + 2 H2O + [oxidized NADPH—hemoprotein reductase]
For diagram of reaction, click here
Other name(s): CYP85A1 (gene name); CYP85A2 (gene name); brassinosteroid 6-oxidase
Systematic name: 6-deoxocastasterone,NADPH—hemoprotein reductase:oxygen 6-oxidoreductase (castasteron-forming)
Comments: This cytochrome P-450 (heme thiolate) plant enzyme catalyses the C-6 hydoxylation of several brassinosteroid biosynthesis intermediates, and the further oxidation of the hydroxyl group to an oxo group. Substrates include 6-deoxocastasterone, 6-deoxotyphasterol, 3-dehydro-6-deoxoteasterone, and 6-deoxoteasterone. The CYP85A2 isozyme of Arabidopsis thaliana (but not the CYP85A1 isozyme) also catalyses the activity of EC 1.14.14.180, brassinolide synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Shimada, Y., Fujioka, S., Miyauchi, N., Kushiro, M., Takatsuto, S., Nomura, T., Yokota, T., Kamiya, Y., Bishop, G.J. and Yoshida, S. Brassinosteroid-6-oxidases from Arabidopsis and tomato catalyze multiple C-6 oxidations in brassinosteroid biosynthesis. Plant Physiol. 126 (2001) 770-779. [PMID: 11402205]
2. Perez-Espana, V.H., Sanchez-Leon, N. and Vielle-Calzada, J.P. CYP85A1 is required for the initiation of female gametogenesis in Arabidopsis thaliana. Plant Signal Behav. 6 (2011) 321-326. [PMID: 21364326]
Accepted name: brassinolide synthase
Reaction: castasterone + O2 + [reduced NADPH—hemoprotein reductase] = brassinolide + 2 H2O + [oxidized NADPH—hemoprotein reductase]
For diagram of reaction, click here
Other name(s): CYP85A2 (gene name); CYP85A3 (gene name)
Systematic name: castasterone,NADPH—hemoprotein reductase:oxygen oxidoreductase (lactonizing, brassinolide-forming)
Comments: This cytochrome P-450 (heme thiolate) plant enzyme catalyses the latonization of several brassinosteroids, including castasterone, teasterone, and typhasterol. The CYP85A2 enzyme of Arabidopsis thaliana also catalyses the activity of EC 1.14.14.179, brassinosteroid 6-oxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Nomura, T., Kushiro, T., Yokota, T., Kamiya, Y., Bishop, G.J. and Yamaguchi, S. The last reaction producing brassinolide is catalyzed by cytochrome P-450s, CYP85A3 in tomato and CYP85A2 in Arabidopsis. J. Biol. Chem. 280 (2005) 17873-17879. [PMID: 15710611]
2. Kim, T.W., Hwang, J.Y., Kim, Y.S., Joo, S.H., Chang, S.C., Lee, J.S., Takatsuto, S. and Kim, S.K. Arabidopsis CYP85A2, a cytochrome P450, mediates the Baeyer-Villiger oxidation of castasterone to brassinolide in brassinosteroid biosynthesis. Plant Cell 17 (2005) 2397-2412. [PMID: 16024588]
3. Katsumata, T., Hasegawa, A., Fujiwara, T., Komatsu, T., Notomi, M., Abe, H., Natsume, M. and Kawaide, H. Arabidopsis CYP85A2 catalyzes lactonization reactions in the biosynthesis of 2-deoxy-7-oxalactone brassinosteroids. Biosci. Biotechnol. Biochem. 72 (2008) 2110-2117. [PMID: 18685225]
Accepted name: sulfoquinovose monooxygenase
Reaction: 6-sulfo-D-quinovose + FMNH2 + O2 = 6-dehydro-D-glucose + FMN + sulfite + H2O
Glossary: D-quinovose = 6-deoxy-D-glucopyranose
6-dehydro-D-glucose = 6-oxo-D-quinovose
Other name(s): 6-deoxy-6-sulfo-D-glucose monooxygenase; smoC (gene name); squD (gene name)
Systematic name: 6-sulfo-D-quinovose,FMNH2:oxygen oxidoreductase
Comments: The enzyme, characterized from the bacteria Agrobacterium fabrum and Rhizobium oryzae, is involved in a D-sulfoquinovose degradation pathway. FMNH2 is provided by an associated FMN reductase [SmoA, EC 1.5.1.42, FMN reductase (NADH)]..
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Liu, J., Wei, Y., Ma, K., An, J., Liu, X., Liu, Y., Ang, E.L., Zhao, H. and Zhang, Y. Mechanistically diverse pathways for sulfoquinovose degradation in bacteria. ACS Catal. 11 (2021) 14740-14750.
2. Sharma, M., Lingford, J.P., Petricevic, M., Snow, A.JD., Zhang, Y., Jarva, M.A., Mui, J.W., Scott, N.E., Saunders, E.C., Mao, R., Epa, R., da Silva, B.M., Pires, D.EV., Ascher, D.B., McConville, M.J., Davies, G.J., Williams, S.J. and Goddard-Borger, E.D. Oxidative desulfurization pathway for complete catabolism of sulfoquinovose by bacteria. Proc. Natl. Acad. Sci. USA 119 (2022) . [PMID: 35074914]
Accepted name: taxoid 7β-hydroxylase
Reaction: (1) taxusin + [reduced NADPH—hemoprotein reductase] + O2 = 7β-hydroxytaxusin + [oxidized NADPH—hemoprotein reductase] + H2O
(2) 2α-hydroxytaxusin + [reduced NADPH—hemoprotein reductase] + O2 = 2α,7β-dihydroxytaxusin + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: taxusin = taxa-4(20),11-diene-5α,9α,10β,13α-tetrayl tetraacetate
Systematic name: taxusin, [reduced NADPH—hemoprotein reductase]:oxygen 7-oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein from the yew tree Taxus cuspidata. Does not act on earlier intermediates in taxol biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Chau, M., Jennewein, S., Walker, K. and Croteau, R. Taxol biosynthesis: Molecular cloning and characterization of a cytochrome P450 taxoid 7β-hydroxylase. Chem. Biol. 11 (2004) 663-672. [PMID: 15157877]
2. Chau, M. and Croteau, R. Molecular cloning and characterization of a cytochrome P450 taxoid 2α-hydroxylase involved in taxol biosynthesis. Arch. Biochem. Biophys. 427 (2004) 48-57. [PMID: 15178487]
Accepted name: taxoid 2α-hydroxylase
Reaction: (1) taxusin + [reduced NADPH—hemoprotein reductase] + O2 = 2α-hydroxytaxusin + [oxidized NADPH—hemoprotein reductase] + H2O
(2) 7β-hydroxytaxusin + [reduced NADPH—hemoprotein reductase] + O2 = 2α,7β-dihydroxytaxusin + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: taxusin = taxa-4(20),11-diene-5α,9α,10β,13α-tetrayl tetraacetate
Systematic name: taxusin, [reduced NADPH—hemoprotein reductase]:oxygen 2-oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein from the yew tree Taxus cuspidata. Does not act on earlier intermediates in taxol biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Chau, M., Jennewein, S., Walker, K. and Croteau, R. Taxol biosynthesis: Molecular cloning and characterization of a cytochrome P450 taxoid 7β-hydroxylase. Chem. Biol. 11 (2004) 663-672. [PMID: 15157877]
2. Chau, M. and Croteau, R. Molecular cloning and characterization of a cytochrome P450 taxoid 2α-hydroxylase involved in taxol biosynthesis. Arch. Biochem. Biophys. 427 (2004) 48-57. [PMID: 15178487]
Accepted name: 5-dehydro-6-demethoxyfumagillol synthase
Reaction: (+)-exo-β-bergamotene + 2 [reduced NADPH—hemoprotein reductase] + 3 O2 = 5-dehydro-6-demethoxyfumagillol + 2 [oxidized NADPH—hemoprotein reductase] + 3 H2O (overall reaction)
(1a) (+)-exo-β-bergamotene + [reduced NADPH—hemoprotein reductase] + O2 = (5R)-hydroxy-(+)-exo-β-bergamotene + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) (5R)-hydroxy-(+)-exo-β-bergamotene + O2 = (3S)-3-[2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-4-methylidenecyclohexan-1-one + H2O
(1c) (3S)-3-[2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-4-methylidenecyclohexan-1-one + [reduced NADPH—hemoprotein reductase] + O2 = 5-dehydro-6-demethoxyfumagillol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here and mechanism click here
For diagram of reaction click here
Glossary: (+)-exo-β-bergamotene = β-trans-bergamotene = (1S,5S,6R)-6-methyl-2-methylidene-6-(4-methylpent-3-enyl)bicyclo[3.1.1]heptane
fumagillol = (3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-1-oxaspiro[2.5]octan-6-ol
fumagillin = (2E,4E,6E,8E)-10-({(3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-1-oxaspiro[2.5]oct-6-yl}oxy)-10-oxodeca-2,4,6,8-tetraenoate
Other name(s): fumagillin multifunctional cytochrome P450 monooxygenase; Fma-P450; fmaG (gene name)
Systematic name: (+)-exo-β-bergamotene,[reduced NADPH—hemoprotein reductase] oxidoreductase (5-dehydro-6-demethoxyfumagillol-producing)
Comments: The enzyme, characterized from the mold Aspergillus fumigatus, catalyses a complex transformation comprising hydroxylation, bicyclic ring-opening, and two epoxidations, generating the sesquiterpenoid core skeleton of fumagillin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Lin, H.C., Tsunematsu, Y., Dhingra, S., Xu, W., Fukutomi, M., Chooi, Y.H., Cane, D.E., Calvo, A.M., Watanabe, K. and Tang, Y. Generation of complexity in fungal terpene biosynthesis: discovery of a multifunctional cytochrome P450 in the fumagillin pathway. J. Am. Chem. Soc. 136 (2014) 4426-4436. [PMID: 24568283]
Accepted name: taxane 9α-hydroxylase
Reaction: 5,20-epoxytax-11-en-4α-ol + [reduced NADPH—hemoprotein reductase] + O2 = 5,20-epoxytax-11-ene-4α,9α-diol + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): taxoid 9α hydroxylase; CYP725A22; T9αOH
Systematic name: 5,20-epoxytax-11-en-4α-ol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (9α-hydroxylating)
Comments: The enzyme is active in the biosynthetic pathway of paclitaxel (Taxol) in Taxus species (yew)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Zhang, Y., Wiese, L., Fang, H., Alseekh, S., Perez de Souza, L., Scossa, F., Molloy, J., Christmann, M. and Fernie, A.R. Synthetic biology identifies the minimal gene set required for paclitaxel biosynthesis in a plant chassis. Mol. Plant 16 (2023) 1951-1961. [PMID: 37897038]
Accepted name: tryptamine 5-hydroxylase
Reaction: tryptamine + O2 + [reduced NADPH—hemoprotein reductase] = serotonin + H2O + [oxidized NADPH—hemoprotein reductase]
Glossary: serotonin = 5-hydroxytryptamine
Other name(s): CYP71P1 (gene name)
Systematic name: tryptamine,NADPH—hemoprotein reductase:oxygen oxidoreductase (5-hydroxylating)
Comments: A cytochrome P-450. The enzyme has been characterized from rice (Oryza sativa) and walnut (Juglans regia).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Schroder, P., Abele, C., Gohr, P., Stuhlfauth-Roisch, U. and Grosse, W. Latest on enzymology of serotonin biosynthesis in walnut seeds. Adv. Exp. Med. Biol. 467 (1999) 637-644. [PMID: 10721112]
2. Fujiwara, T., Maisonneuve, S., Isshiki, M., Mizutani, M., Chen, L., Wong, H.L., Kawasaki, T. and Shimamoto, K. Sekiguchi lesion gene encodes a cytochrome P450 monooxygenase that catalyzes conversion of tryptamine to serotonin in rice. J. Biol. Chem. 285 (2010) 11308-11313. [PMID: 20150424]
3. Park, S., Kang, K., Lee, S.W., Ahn, M.J., Bae, J.M. and Back, K. Production of serotonin by dual expression of tryptophan decarboxylase and tryptamine 5-hydroxylase in Escherichia coli. Appl. Microbiol. Biotechnol. 89 (2011) 1387-1394. [PMID: 21080162]
4. Park, S., Byeon, Y. and Back, K. Transcriptional suppression of tryptamine 5-hydroxylase, a terminal serotonin biosynthetic gene, induces melatonin biosynthesis in rice (Oryza sativa L.). J Pineal Res 55 (2013) 131-137. [PMID: 23521226]
Accepted name: rhazimal synthase
Reaction: geissoschizine + [reduced NADPH—hemoprotein reductase] + O2 = rhazimal + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of reaction click here and mechanism click here
Other name(s): RHS (gene name)
Systematic name: geissoschizine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (rhazimal forming)
Comments: A heme-thiolate protein (P-450) isolated from the plant Alstonia scholaris (blackboard tree).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wang, Z., Xiao, Y., Wu, S., Chen, J., Li, A. and Tatsis, E.C. Deciphering and reprogramming the cyclization regioselectivity in bifurcation of indole alkaloid biosynthesis. Chem. Sci. 13 (2022) 12389-12395. [PMID: 36349266]
Accepted name: norfluorocurarine 18-hydroxylase
Reaction: norfluorocurarine + [reduced NADPH—hemoprotein reductase] + O2 = 18-hydroxynorfluorocurarine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here
Glossary: norfluorocurarine = (19E)-cura-2(16),19-dien-17-al
Other name(s): norfluorocurarine oxidase; CYP71A144
Systematic name: (19E)-cura-2(16),19-dien-17-al,[NADPH—hemoprotein reductase]:oxygen oxidoreductase (18-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme, isolated from the tree Strychnos nux-vomica, participates in the biosynthesis of strychnine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Hong, B., Grzech, D., Caputi, L., Sonawane, P., Lopez, C.ER., Kamileen, M.O., Hernandez Lozada, N.J., Grabe, V. and O'Connor, S.E. Biosynthesis of strychnine. Nature 607 (2022) 617-622. [PMID: 35794473]
Accepted name: strychnine 10-hydroxylase
Reaction: strychnine + [reduced NADPH—hemoprotein reductase] + O2 = 10-hydroxystrychnine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here or click here
Glossary: strychnine = strychnidin-10-one
10-hydroxystrychnine (ref 1)| = 2-hydroxystrychnidin-10-one
Other name(s): CYP82D36
Systematic name: strychnine,[NADPH—hemoprotein reductase]:oxygen oxidoreductase (10-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme, isolated from the tree Strychnos nux-vomica, participates in the biosynthesis of brucine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Hong, B., Grzech, D., Caputi, L., Sonawane, P., Lopez, C.ER., Kamileen, M.O., Hernandez Lozada, N.J., Grabe, V. and O'Connor, S.E. Biosynthesis of strychnine. Nature 607 (2022) 617-622. [PMID: 35794473]
Accepted name: β-colubrine 11-hydroxylase
Reaction: β-colubrine + [reduced NADPH—hemoprotein reductase] + O2 = 11-demethylbrucine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction click here
Glossary: β-colubrine = 2-methoxystrychnidine (IUPAC) = 10-methoxystrychnidine (ref 1)
11-demethylbrucine (ref 1) = 3-hydroxy-2-methoxystrichnidine (IUPAC)
Other name(s): CYP71AH44
Systematic name: β-colubrine,[NADPH—hemoprotein reductase]:oxygen oxidoreductase (11-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme, isolated from the tree Strychnos nux-vomica, participates in the biosynthesis of brucine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Hong, B., Grzech, D., Caputi, L., Sonawane, P., Lopez, C.ER., Kamileen, M.O., Hernandez Lozada, N.J., Grabe, V. and O'Connor, S.E. Biosynthesis of strychnine. Nature 607 (2022) 617-622. [PMID: 35794473]