Biflaviolin synthase
| Biflaviolin synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.21.7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Biflaviolin synthase (EC 1.14.21.7, CYP158A2, CYP 158A2, cytochrome P450 158A2) is an enzyme with systematic name flaviolin,NADPH:oxygen oxidoreductase.[1][2][3] This enzyme catalyses the following chemical reaction
- (1) 2 flaviolin + NADPH + H+ + O2 3,3'-biflaviolin + NADP+ + 2 H2O
- (2) 2 flaviolin + NADPH + H+ + O2 3,8'-biflaviolin + NADP+ + 2 H2O
This cytochrome P450 enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyses a phenol oxidation C-C coupling reaction.
References
- ↑ Zhao, B.; Guengerich, F.P.; Bellamine, A.; Lamb, D.C.; Izumikawa, M.; Lei, L.; Podust, L.M.; Sundaramoorthy, M.; Kalaitzis, J.A.; Reddy, L.M.; Kelly, S.L.; Moore, B.S.; Stec, D.; Voehler, M.; Falck, J.R.; Shimada, T.; Waterman, M.R. (2005). "Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2". J. Biol. Chem. 280 (12): 11599–11607. doi:10.1074/jbc.M410933200. PMID 15659395.
- ↑ Zhao, B.; Guengerich, F.P.; Voehler, M.; Waterman, M.R. (2005). "Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer". J. Biol. Chem. 280 (51): 42188–42197. doi:10.1074/jbc.M509220200. PMID 16239228.
- ↑ Zhao, B.; Lamb, D.C.; Lei, L.; Kelly, S.L.; Yuan, H.; Hachey, D.L.; Waterman, M.R. (2007). "Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2". Biochemistry. 46 (30): 8725–8733. doi:10.1021/bi7006959. PMID 17614370.
External links
- Biflaviolin synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
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