Back to Search
Start Over
Structure-based analysis of domain function of chitin oligosaccharide deacetylase from Vibrio parahaemolyticus.
- Source :
-
FEBS Letters . Jan2015, Vol. 589 Issue 1, p145-151. 7p. - Publication Year :
- 2015
-
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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00145793
- Volume :
- 589
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- FEBS Letters
- Publication Type :
- Academic Journal
- Accession number :
- 100080376
- Full Text :
- https://doi.org/10.1016/j.febslet.2014.11.039