| Literature DB >> 19008098 |
Arkadius Pichota1, Jeyaraj Duraiswamy, Zheng Yin, Thomas H Keller, Jenefer Alam, Sarah Liung, Gladys Lee, Mei Ding, Gang Wang, Wai Ling Chan, Mark Schreiber, Ida Ma, David Beer, Xinyi Ngew, Kakoli Mukherjee, Mahesh Nanjundappa, Jeanette W P Teo, Pamela Thayalan, Amelia Yap, Thomas Dick, Wuyi Meng, Mei Xu, James Koehn, Shi-Hao Pan, Kirk Clark, Xiaoling Xie, Carolyn Shoen, Michael Cynamon.
Abstract
Bacterial peptide deformylase (PDF) belongs to a subfamily of metalloproteases catalyzing the removal of the N-terminal formyl group from newly synthesized proteins. We report the synthesis and biological activity of highly potent inhibitors of Mycobacterium tuberculosis (Mtb) PDF enzyme as well as the first X-ray crystal structure of Mtb PDF. Structure-activity relationship and crystallographic data clarified the structural requirements for high enzyme potency and cell based potency. Activities against single and multi-drug-resistant Mtb strains are also reported.Entities:
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Year: 2008 PMID： 19008098 DOI： 10.1016/j.bmcl.2008.10.040
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN： 0960-894X Impact factor: 2.823