Putative Exposed Aromatic and Hydroxyl Residues on the Surface of the N-Terminal Domains of Chi1 from Aeromonas caviae CB101 Are Essential for Chitin Binding and Hydrolysis
Open Access
- 1 November 2005
- journal article
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 71 (11) , 7559-7561
- https://doi.org/10.1128/aem.71.11.7559-7561.2005
Abstract
Chitinase Chi1 of Aeromonas caviae CB101 possesses chitin binding sites at both its N and C termini. Four putative exposed residues aligned in a line on the surface of the N-terminal domains of Chi1 were found to contribute to the enzyme-chitin binding and hydrolysis via site-directed mutagenesis. Also, it was found that Chi1 requires the cooperation of the N- and C-terminal domains to bind fully with crystalline and colloidal chitin.Keywords
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