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Isopenicillin N synthase mediates thiolate oxidation to sulfenate in a depsipeptide substrate analogue: implications for oxygen binding and a link to nitrile hydratase?

…, RM Adlington, JE Baldwin, PJ Rutledge

文献索引:Elkins, Jonathan M.; Rutledge, Peter J.; Burzlaff, Nicolai I.; Clifton, Ian J.; Adlington, Robert M.; Roach, Peter L.; Baldwin, Jack E. Organic and Biomolecular Chemistry, 2003 , vol. 1, # 9 p. 1455 - 1460

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被引用次数: 23

摘要

Isopenicillin N synthase (IPNS) is a nonheme iron oxidase that catalyzes the central step in the biosynthesis of β-lactam antibiotics: oxidative cyclization of the linear tripeptide δ-l-α- aminoadipoyl-l-cysteinyl-d-valine (ACV) to isopenicillin N (IPN). The ACV analogue δ-l-α-