Structural and Biochemical Basis of a Marine Bacterial Glycoside Hydrolase Family 2 β-Glycosidase with Broad Substrate Specificity.

ABSTRACT: Uronic acids are commonly found in marine polysaccharides and increase structural complexity and intrinsic recalcitrance to enzymatic attack. Glycoside hydrolase family 2 (GH2) includes proteins that target sugar conjugates with hexuronates and are involved in the catabolism and cycling of marine polysaccharides. Here, we report a novel GH2, AqGalA from a marine alga-associated Bacteroidetes organism with broad substrate specificity. Biochemical analyses revealed that AqGalA exhibits hydrolyzing activities against β-galacturonide, β-glucuronide, and β-galactopyranoside via retaining mechanisms. We solved the AqGalA crystal structure in complex with galacturonic acid (GalA) and determined (via mutagenesis) that charge characteristics at uronate-binding subsites c

SUBMITTER: Yang J 

PROVIDER: S-EPMC8788668 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature