期刊
FEBS LETTERS
卷 589, 期 1, 页码 145-151出版社
WILEY
DOI: 10.1016/j.febslet.2014.11.039
关键词
Chitin oligosaccharide deacetylase; Protein structure; Domain function; Enzyme mutation; Binding assay; Kinetics
资金
- College of Bioresource Sciences, Nihon University
The X-ray crystal structure of chitin oligosaccharide deacetylase from Vibrio parahaemolyticus (Vp-COD) was determined at an 1.35 angstrom resolution. The amino acid sequence and structure of Vp-COD show that the enzyme comprises one polysaccharide deacetylase domain (PDD) and two carbohydrate-binding domains (CBDs). On the basis of a chitin-binding assay with Vp-COD and its CBDs-deleted mutant, it was confirmed that CBDs can adhere to chitin. The catalytic activity of the CBDs-deleted mutant was only mildly depressed compared with that of Vp-COD, indicating that CBDs are unlikely to affect the configuration of the active center residues in active site of PDD. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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