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© Institut Pasteur
Cristaux de cellulase, enzyme purifiée de Clostridium thermocellum permettant la digestion de la cellulose. Image colorisée.
Publication : Current topics in medicinal chemistry

Drug design and identification of potent leads against mycobacterium tuberculosis thymidine monophosphate kinase

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Current topics in medicinal chemistry - 01 Jan 2012

Van Calenbergh S, Pochet S, Munier-Lehmann H

Link to Pubmed [PMID] – 22283813

Curr Top Med Chem 2012;12(7):694-705

Antiviral chemotherapy often relies on nucleoside analogues, which, once phophorylated by intracellular kinases, target viral polymerases impeding DNA synthesis. In contrast, nucleoside analogues are much less explored as antibacterial drugs. Thymidine monophosphate kinase from Mycobacterium tuberculosis (TMPKmt), which is essential to DNA replication, was selected as a promising target for the design of new inhibitors. This review describes stepwise modifications of the TMPKmt substrate, guided by the feedback of enzyme assays and crystallographic analysis to afford potent enzyme inhibitors some of which also exhibited antitubercular activity. More importantly, several of the reported thymidine analogues provided a deeper understanding of the structure and catalytic mechanism of this intriguing enzyme.

http://www.ncbi.nlm.nih.gov/pubmed/22283813

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