In silico and in vitro analysis of an Aspergillus niger chitin deacetylase to decipher its subsite sugar preferences.

ABSTRACT: Chitin deacetylases (CDAs) are found in many different organisms ranging from marine bacteria to fungi and insects. These enzymes catalyze the removal of acetyl groups from chitinous substrates generating various chitosans, linear copolymers consisting of N-acetylglucosamine (GlcNAc) and glucosamine. CDAs influence the degree of acetylation of chitosans as well as their pattern of acetylation, a parameter that was recently shown to influence the physicochemical properties and biological activities of chitosans. The binding site of CDAs typically consists of around four subsites, each accommodating a single sugar unit of the substrate. It has been hypothesized that the subsite preferences for GlcNAc or glucosamine units play a crucial role in the acetylation pattern they generate, but so fa

SUBMITTER: Bonin M 

PROVIDER: S-EPMC8488497 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature