Biflaviolin synthase

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
Biflaviolin synthase
Identifiers
EC no.1.14.21.7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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 FP, Bellamine A, Lamb DC, Izumikawa M, Lei L, Podust LM, Sundaramoorthy M, Kalaitzis JA, Reddy LM, Kelly SL, Moore BS, Stec D, Voehler M, Falck JR, Shimada T, Waterman MR (March 2005). "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. doi:10.1074/jbc.M410933200. PMID 15659395.
  2. Zhao B, Guengerich FP, Voehler M, Waterman MR (December 2005). "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. doi:10.1074/jbc.M509220200. PMID 16239228.
  3. Zhao B, Lamb DC, Lei L, Kelly SL, Yuan H, Hachey DL, Waterman MR (July 2007). "Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2". Biochemistry. 46 (30): 8725–33. doi:10.1021/bi7006959. PMID 17614370.
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