The effects of the surface-exposed residues on the binding and hydrolytic activities of Vibrio carchariae chitinase A.

ABSTRACT:

Background

Vibrio carchariae chitinase A (EC3.2.1.14) is a family-18 glycosyl hydrolase and comprises three distinct structural domains: i) the amino terminal chitin binding domain (ChBD); ii) the (alpha/beta)8 TIM barrel catalytic domain (CatD); and iii) the alpha + beta insertion domain. The predicted tertiary structure of V. carchariae chitinase A has located the residues Ser33 & Trp70 at the end of ChBD and Trp231 & Tyr245 at the exterior of the catalytic cleft. These residues are surface-exposed and presumably play an important role in chitin hydrolysis.

Results

Point mutations of the target residues of V. carchariae chitinase A were generated by site-directed mutagenesis. With respect to their binding activity towards crystalline alpha-chitin and colloidal chitin, chit

SUBMITTER: Pantoom S 

PROVIDER: S-EPMC2265269 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature