IUBMB Enzyme Nomenclature

EC 1.14.13.188

Accepted name: 6-deoxyerythronolide B hydroxylase

Reaction: 6-deoxyerythronolide B + NADPH + H+ + O2 = erythronolide B + NADP+ + H2O

For diagram of reaction click here.

Other name(s): DEB hydroxylase; eryF (gene name); P450(eryF); CYP107A1

Systematic name: 6-deoxyerythronolide-B,NADPH:oxygen oxidoreductase

Comments: A heme-thiolate protein (P-450). Isolated from the bacterium Saccharopolyspora erythraea. The enzyme is involved in the biosynthesis of the antibiotic erythromycin.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Weber, J.M., Leung, J.O., Swanson, S.J., Idler, K.B. and McAlpine, J.B. An erythromycin derivative produced by targeted gene disruption in Saccharopolyspora erythraea. Science 252 (1991) 114-117. [PMID: 2011746]

2. Shafiee, A. and Hutchinson, C.R. Macrolide antibiotic biosynthesis: isolation and properties of two forms of 6-deoxyerythronolide B hydroxylase from Saccharopolyspora erythraea (Streptomyces erythreus). Biochemistry 26 (1987) 6204-6210. [PMID: 2446657]

3. Cupp-Vickery, J.R., Li, H. and Poulos, T.L. Preliminary crystallographic analysis of an enzyme involved in erythromycin biosynthesis: cytochrome P450eryF. Proteins: Struct., Funct., Bioinf. 20 (1994) 197-201. [PMID: 7846029]

4. Nagano, S., Cupp-Vickery, J.R. and Poulos, T.L. Crystal structures of the ferrous dioxygen complex of wild-type cytochrome P450eryF and its mutants, A245S and A245T: investigation of the proton transfer system in P450eryF. J. Biol. Chem. 280 (2005) 22102-22107. [PMID: 15824115]

[EC 1.14.13.188 created 2014]


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