Biology:Biflaviolin synthase
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Short description: Class of enzymes
| 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 3,3'-biflaviolin + NADP+ + 2 H2O
- (2) 2 flaviolin + NADPH + H+ + O2 [math]\displaystyle{ \rightleftharpoons }[/math] 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
- ↑ "Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2". The Journal of Biological Chemistry 280 (12): 11599–607. March 2005. doi:10.1074/jbc.M410933200. PMID 15659395.
- ↑ "Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer". The Journal of Biological Chemistry 280 (51): 42188–97. December 2005. doi:10.1074/jbc.M509220200. PMID 16239228.
- ↑ "Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2". Biochemistry 46 (30): 8725–33. July 2007. 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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