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

FEBS Lett. 2015 Jan 2;589(1):145-51. doi: 10.1016/j.febslet.2014.11.039. Epub 2014 Dec 3.

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.

Keywords: Binding assay; Chitin oligosaccharide deacetylase; Domain function; Enzyme mutation; Kinetics; Protein structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amidohydrolases / chemistry*
  • Amidohydrolases / genetics
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Chitin / chemistry*
  • Crystallography, X-Ray
  • Protein Structure, Tertiary
  • Sequence Deletion
  • Vibrio parahaemolyticus / enzymology*
  • Vibrio parahaemolyticus / genetics

Substances

  • Bacterial Proteins
  • Chitin
  • Amidohydrolases