Interaction of carbohydrate binding module 20 with starch substrates.

ABSTRACT: CBM20s are starch-binding domains found in many amylolytic enzymes, including glucoamylase, alpha-amylase, beta-amylases, and a new family of starch-active polysaccharide monooxygenases (AA13 PMOs). Previous studies of CBM20-substrate interaction only concerned relatively small or soluble amylose molecules, while amylolytic enzymes often work on extended chains of insoluble starch molecules. In this study, we utilized molecular simulation techniques to gain further insights into the interaction of CBM20 with substrates of various sizes via its two separate binding sites, termed as BdS1 and BdS2. Results show that substrate binding at BdS1 involving two conserved tryptophan residues is about 2-4 kcal mol^-1 stronger than that at BdS2. CBM20 exhibits about two-fold higher af

SUBMITTER: Ngo ST 

PROVIDER: S-EPMC9069913 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature