Structural and functional determination of homologs of the <i>Mycobacterium tuberculosis N</i>-acetylglucosamine-6-phosphate deacetylase (NagA).

ABSTRACT: The Mycobacterium tuberculosis (Mtb) pathogen encodes a GlcNAc-6-phosphate deacetylase enzyme, NagA (Rv3332), that belongs to the amidohydrolase superfamily. NagA enzymes catalyze the deacetylation of GlcNAc-6-phosphate (GlcNAc6P) to glucosamine-6-phosphate (GlcN6P). NagA is a potential antitubercular drug target because it represents the key enzymatic step in the generation of essential amino-sugar precursors required for Mtb cell wall biosynthesis and also influences recycling of cell wall peptidoglycan fragments. Here, we report the structural and functional characterization of NagA from Mycobacterium smegmatis (MSNagA) and Mycobacterium marinum (MMNagA), close relatives of Mtb Using a combination of X-ray crystallography, site-directed mutagene

SUBMITTER: Ahangar MS 

PROVIDER: S-EPMC6016474 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature