| EC |
1.14.15.35 |
| Accepted name: |
6-deoxyerythronolide B hydroxylase |
| Reaction: |
6-deoxyerythronolide B + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = erythronolide B + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O |
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For diagram of erythromycin biosynthesis, click here |
| Other name(s): |
DEB hydroxylase; eryF (gene name); P450(eryF); CYP107A1 |
| Systematic name: |
6-deoxyerythronolide-B,reduced ferredoxin:oxygen oxidoreductase |
| Comments: |
A cytochrome P-450 (heme-thiolate) protein 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, PDB |
| 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. [DOI] [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 20 (1994) 197–201. [DOI] [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. [DOI] [PMID: 15824115] |
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| [EC 1.14.15.35 created 2014 as EC 1.14.13.188, transferred 2018 to EC 1.14.15.35] |
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