Structural highlights
Function
A6P4T5_VIBPH
Publication Abstract from PubMed
The X-ray crystal structure of chitin oligosaccharide deacetylase from Vibrio parahaemolyticus (Vp-COD) was determined at an 1.35 A 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.
Structure-based analysis of domain function of chitin oligosaccharide deacetylase from Vibrio parahaemolyticus.,Hirano T, Sugiyama K, Sakaki Y, Hakamata W, Park SY, Nishio T FEBS Lett. 2015 Jan 2;589(1):145-51. doi: 10.1016/j.febslet.2014.11.039. Epub, 2014 Dec 3. PMID:25479092[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hirano T, Sugiyama K, Sakaki Y, Hakamata W, Park SY, Nishio T. 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. PMID:25479092 doi:http://dx.doi.org/10.1016/j.febslet.2014.11.039
