| Literature DB >> 25479092 |
Takako Hirano1, Kanako Sugiyama2, Yuta Sakaki1, Wataru Hakamata1, Sam-Yong Park2, Toshiyuki Nishio3.
Abstract
The X-ray crystal structure of chitin oligosaccharide deacetylase from Vibrio parahaemolyticus (Vp-COD) was determined at an 1.35 Å 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.Entities:
Keywords: Binding assay; Chitin oligosaccharide deacetylase; Domain function; Enzyme mutation; Kinetics; Protein structure
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Year: 2014 PMID: 25479092 DOI: 10.1016/j.febslet.2014.11.039
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124