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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

Author:
Li, Qiang, Wang, Fengping, Zhou, Ying, Xiao, Xiang
Source:
Applied and environmental microbiology 2005 v.71 no.11 pp. 7559-7561
ISSN:
0099-2240
Subject:
Aeromonas punctata, binding sites, chitin, chitinase, hydrolysis, site-directed mutagenesis
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.
Agid:
577629