The effects of the surface-exposed residues on the binding and hydrolytic activities of Vibrio carchariae chitinase A
Open Access
- 21 January 2008
- journal article
- Published by Springer Nature in BMC Biochemistry
- Vol. 9 (1) , 2
- https://doi.org/10.1186/1471-2091-9-2
Abstract
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 (α/β)8 TIM barrel catalytic domain (CatD); and iii) the α + β 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.Keywords
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