| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1374810 | Bioorganic & Medicinal Chemistry Letters | 2008 | 5 Pages |
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.
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Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Arkadius Pichota, 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,