Structure‐based analysis of domain function of chitin oligosaccharide deacetylase from  Vibrio parahaemolyticus | Zendy

Hirano Takako | Zendy; Sugiyama Kanako | Zendy; Sakaki Yuta | Zendy; Hakamata Wataru | Zendy; Park Sam-Yong | Zendy; Nishio Toshiyuki | Zendy

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Structure‐based analysis of domain function of chitin oligosaccharide deacetylase from Vibrio parahaemolyticus

Author(s) -

Hirano Takako,

Sugiyama Kanako,

Sakaki Yuta,

Hakamata Wataru,

Park Sam-Yong,

Nishio Toshiyuki

Publication year - 2015

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2014.11.039

Subject(s) - vibrio parahaemolyticus , chitin , chemistry , oligosaccharide , biochemistry , mutant , microbiology and biotechnology , active site , enzyme , biology , bacteria , gene , chitosan , genetics

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.

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