| Literature DB >> 22942282 |
Kristin E Burns1, Fiona E McAllister, Carsten Schwerdtfeger, Julian Mintseris, Francisca Cerda-Maira, Elke E Noens, Matthias Wilmanns, Stevan R Hubbard, Francesco Melandri, Huib Ovaa, Steven P Gygi, K Heran Darwin.
Abstract
Deamidase of Pup (Dop), the prokaryotic ubiquitin-like protein (Pup)-deconjugating enzyme, is critical for the full virulence of Mycobacterium tuberculosis and is unique to bacteria, providing an ideal target for the development of selective chemotherapies. We used a combination of genetics and chemical biology to characterize the mechanism of depupylation. We identified an aspartate as a potential nucleophile in the active site of Dop, suggesting a novel protease activity to target for inhibitor development.Entities:
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Year: 2012 PMID: 22942282 PMCID: PMC3481346 DOI: 10.1074/jbc.M112.384784
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157