Structure and function of a broad-specificity chitin deacetylase from Aspergillus nidulans FGSC A4.

ABSTRACT: Enzymatic conversion of chitin, a β-1,4 linked polymer of N-acetylglucosamine, is of major interest in areas varying from the biorefining of chitin-rich waste streams to understanding how medically relevant fungi remodel their chitin-containing cell walls. Although numerous chitinolytic enzymes have been studied in detail, relatively little is known about enzymes capable of deacetylating chitin. We describe the structural and functional characterization of a 237 residue deacetylase (AnCDA) from Aspergillus nidulans FGSC A4. AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and acetylxylan, but not on peptidoglycan. The K _m and k _cat of AnCDA for the first deacetylation of penta-N-acetyl-chitopentaose are 72 µM and 1.4 s^-1, respectively. Combining

SUBMITTER: Liu Z 

PROVIDER: S-EPMC5431758 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature