The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: biflaviolin synthase
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
For diagram of flaviolin metabolism, click here
Glossary: flaviolin = 4,5,7-trihydroxynaphthalene-1,2-dione
3,3′-biflaviolin = 3,3′,6,6′,8,8′-hexahydroxy-2,2′-binaphthalene-1,1′,4,4′-tetraone
3,8′-biflaviolin = 2,3′,4,6′,7,8′-hexahydroxy-1,2′-binaphthalene-1′,4′,5,8-tetraone
Other name(s): CYP158A2; CYP 158A2; cytochrome P450 158A2
Systematic name: flaviolin,NADPH:oxygen oxidoreductase
Comments: This cytochrome-P-450 enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyses a phenol oxidation C-C coupling reaction, which results in the polymerization of flaviolin to form biflaviolin or triflaviolin without the incorporation of oxygen into the product [1,3]. The products are highly conjugated pigments that protect the bacterium from the deleterious effects of UV irradiation [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2. J. Biol. Chem. 280 (2005) 11599–11607. [PMID: 15659395]
2.  Zhao, B., Guengerich, F.P., Voehler, M. and Waterman, M.R. 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 (2005) 42188–42197. [PMID: 16239228]
3.  Zhao, B., Lamb, D.C., Lei, L., Kelly, S.L., Yuan, H., Hachey, D.L. and Waterman, M.R. Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2. Biochemistry 46 (2007) 8725–8733. [PMID: 17614370]
[EC created 2008]

Data © 2001–2018 IUBMB
Web site © 2005–2018 Andrew McDonald