4.5 Article

A-102395, a new inhibitor of bacterial translocase I, produced by Amycolatopsis sp SANK 60206

Journal

JOURNAL OF ANTIBIOTICS
Volume 60, Issue 11, Pages 690-695

Publisher

SPRINGERNATURE
DOI: 10.1038/ja.2007.88

Keywords

translocase I; peptidoglycan; nucleoside inhibitor; capuramycin; Amycolatopsis sp.; antimicrobial activity

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Bacterial phospho-N-acetylmuramyl-pentapeptide translocase (translocase I: EC 2.7.8.13) is a key enzyme in peptidoglycan biosynthesis, and a known target of antibiotics. Here we report a new nucleoside inhibitor for translocase I, A-102395, isolated from the culture broth of the strain Amycolatopsis sp. SANK 60206. A-102395 is a new derivative of capuramycin that has the benzene with a uniquely substituted chain instead of an aminocaprolactam. A-102395 is a potent inhibitor of bacterial translocase I with IC50 value of 11 nM, but possesses no antimicrobial activity against various strains tested.

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