Journal
FEMS MICROBIOLOGY LETTERS
Volume 350, Issue 1, Pages 42-47Publisher
OXFORD UNIV PRESS
DOI: 10.1111/1574-6968.12302
Keywords
HsaD; Mycobacterium tuberculosis; inhibitors; mechanism; MCP hydrolase; cholesterol
Categories
Ask authors/readers for more resources
Mycobacterium tuberculosis remains the leading cause of death by a bacterial pathogen worldwide. Increasing prevalence of multidrug-resistant organisms means prioritizing identification of targets for antituberculars. 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase (HsaD), part of the cholesterol metabolism operon, is vital for survival within macrophage. The C-C bond hydrolase, HsaD, has a serine protease-like catalytic triad. We tested a range of serine protease and esterase inhibitors for their effects on HsaD activity. As well as providing a potential starting point for drug development, the data provides evidence for the mechanism of C-C bond hydrolysis. This screen also provides a route to initiate development of fragment-based inhibitors.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available