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
Search PMC articles PubMed articles NCBI proteins

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 $\rightleftharpoons$ 3,3'-biflaviolin + NADP⁺ + 2 H₂O

(2) 2 flaviolin + NADPH + H⁺ + O₂ $\rightleftharpoons$ 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

1. Zhao, B., Guengerich, F.P., Bellamine, A., Lamb, D.C., Izumikawa, M., Lei, L., Podust, L.M., Sundaramoorthy, M., Kalaitzis, J.A., Reddy, L.M., Kelly, S.L., Moore, B.S., Stec, D., Voehler, M., Falck, J.R., Shimada, T. and Waterman, M.R. (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.
2. Zhao, B., Guengerich, F.P., Voehler, M. and 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.
3. Zhao, B., Lamb, D.C., Lei, L., Kelly, S.L., Yuan, H., Hachey, D.L. and 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)