Probing impact of active site residue mutations on stability and activity of Neisseria polysaccharea amylosucrase.

ABSTRACT: The amylosucrase from Neisseria polysaccharea is a transglucosidase from the GH13 family of glycoside-hydrolases that naturally catalyzes the synthesis of α-glucans from the widely available donor sucrose. Interestingly, natural molecular evolution has modeled a dense hydrogen bond network at subsite -1 responsible for the specific recognition of sucrose and conversely, it has loosened interactions at the subsite +1 creating a highly promiscuous subsite +1. The residues forming these subsites are considered to be likely involved in the activity as well as the overall stability of the enzyme. To assess their role, a structure-based approach was followed to reshape the subsite -1. A strategy based on stability change predictions, using the FoldX algorithm, was considered to identify the best

SUBMITTER: Daude D 

PROVIDER: S-EPMC3843629 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature