Biflaviolin synthase

Biflaviolin synthase
Identifiers
EC no.	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${\displaystyle \rightleftharpoons }$ 3,3'-biflaviolin + NADP⁺ + 2 H₂O

(2) 2 flaviolin + NADPH + H⁺ + O₂${\displaystyle \rightleftharpoons }$ 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 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.

External links

• Biflaviolin+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)