| Literature DB >> 18057698 |
Ryo Murakami1, Yoko Fujita, Masaaki Kizuka, Tomoka Kagawa, Yasunori Muramatsu, Shunichi Miyakoshi, Toshio Takatsu, Masatoshi Inukai.
Abstract
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.Entities:
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Year: 2007 PMID: 18057698 DOI: 10.1038/ja.2007.88
Source DB: PubMed Journal: J Antibiot (Tokyo) ISSN: 0021-8820 Impact factor: 2.649