Crystal structure of a raw-starch-degrading bacterial α-amylase belonging to subfamily 37 of the glycoside hydrolase family GH13.

ABSTRACT: Subfamily 37 of the glycoside hydrolase family GH13 was recently established on the basis of the discovery of a novel α-amylase, designated AmyP, from a marine metagenomic library. AmyP exhibits raw-starch-degrading activity and consists of an N-terminal catalytic domain and a C-terminal starch-binding domain. To understand this newest subfamily, we determined the crystal structure of the catalytic domain of AmyP, named AmyP_ΔSBD, complexed with maltose, and the crystal structure of the E221Q mutant AmyP_ΔSBD complexed with maltotriose. Glu221 is one of the three conserved catalytic residues, and AmyP is inactivated by the E221Q mutation. Domain B of AmyP_ΔSBD forms a loop that protrudes from domain A, stabilizes the conformation of the active site and increas

SUBMITTER: Liu Y 

PROVIDER: S-EPMC5355875 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature