Article
Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation.
Bioscience, biotechnology, and biochemistry - 1 Jan 2006
Aronson Nathan N, Halloran Brian A, Alexeyev Mikhail F, Zhou Xiaoyin E, Wang Yujun, Meehan Edward J, Chen Liqing
Abstract excerpt
Family 18 chitinases have the signature peptide DGXDXDXE forming the fourth beta-strand in the (beta/alpha)8-barrel of their catalytic domain. The carboxyl-end glutamic acid, E315 in Serratia marcescens chitinase A, serves as the acid/base during chitin hydrolysis, and the side-chain of the preceding aspartic acid, D313, helps to position correctly the N-acetyl moiety of the glycosyl sugar undergoing hydrolysis....
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.