Ryan_2014_FEMS.Microbiol.Lett_350_42

Reference

Title : Mechanism-based inhibition of HsaD: a C-C bond hydrolase essential for survival of Mycobacterium tuberculosis in macrophage - Ryan_2014_FEMS.Microbiol.Lett_350_42
Author(s) : Ryan A , Keany S , Eleftheriadou O , Ballet R , Cheng HY , Sim E
Ref : FEMS Microbiology Letters , 350 :42 , 2014
Abstract :

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.

PubMedSearch : Ryan_2014_FEMS.Microbiol.Lett_350_42
PubMedID: 24164668

Related information

Substrate HOPDA

Citations formats

Ryan A, Keany S, Eleftheriadou O, Ballet R, Cheng HY, Sim E (2014)
Mechanism-based inhibition of HsaD: a C-C bond hydrolase essential for survival of Mycobacterium tuberculosis in macrophage
FEMS Microbiology Letters 350 :42

Ryan A, Keany S, Eleftheriadou O, Ballet R, Cheng HY, Sim E (2014)
FEMS Microbiology Letters 350 :42