title: Structure-based analysis of domain function of chitin oligosaccharide deacetylase from Vibrio parahaemolyticus.
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.
authors.affiliation: Department of Chemistry and Life Science, College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa, Kanagawa 252-0880, Japan.
authors.forename: Takako
authors.initials: T
authors.lastname: Hirano
authors.affiliation: Drug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Tsurumi, Yokohama, Kanagawa 230-0045, Japan.
authors.forename: Kanako
authors.initials: K
authors.lastname: Sugiyama
authors.affiliation: Department of Chemistry and Life Science, College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa, Kanagawa 252-0880, Japan.
authors.forename: Yuta
authors.initials: Y
authors.lastname: Sakaki
authors.affiliation: Department of Chemistry and Life Science, College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa, Kanagawa 252-0880, Japan.
authors.forename: Wataru
authors.initials: W
authors.lastname: Hakamata
authors.affiliation: Drug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Tsurumi, Yokohama, Kanagawa 230-0045, Japan.
authors.forename: Sam-Yong
authors.initials: SY
authors.lastname: Park
authors.affiliation: Department of Chemistry and Life Science, College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa, Kanagawa 252-0880, Japan. Electronic address: nishio.toshiyuki@nihon-u.ac.jp.
authors.forename: Toshiyuki
authors.initials: T
authors.lastname: Nishio
mesh_terms: D000581:Amidohydrolases / Q000737:chemistry* / Q000235:genetics; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D002686:Chitin / Q000737:chemistry*; D018360:Crystallography, X-Ray; D017434:Protein Structure, Tertiary; D017384:Sequence Deletion; D014736:Vibrio parahaemolyticus / Q000201:enzymology* / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D002686:Chitin; D000581:Amidohydrolases
keywords: Binding assay; Chitin oligosaccharide deacetylase; Domain function; Enzyme mutation; Kinetics; Protein structure