Abstract
Cytochrome P450eryF catalyzes the 6S-hydroxylation of 6-deoxyerythronolide B, the initial reaction in a multistep pathway to convert 6-deoxyerythronolide B into the antibiotic, erythromycin. The overall structure of P450eryF is similar to that of P450cam but differs in the exact positioning of several α-helices. The largest difference occurs in the B′ helix and results in the enlargement of the substrate-binding pocket of P450eryF. The substrate is positioned with the macrolide ring perpendicular to the haem plane and contacts seven hydrophobic residues and three solvent molecules. The substrate participates in a network of hydrogen bonds that may provide a proton shuttle pathway in the oxygen cleavage reaction.
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Cupp-Vickery, J., Poulos, T. Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Nat Struct Mol Biol 2, 144–153 (1995). https://doi.org/10.1038/nsb0295-144
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DOI: https://doi.org/10.1038/nsb0295-144
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