Structure-based analysis of domain function of chitin oligosaccharide deacetylase from Vibrio parahaemolyticus
| Autor: | Sam-Yong Park, Takako Hirano, Wataru Hakamata, Toshiyuki Nishio, Kanako Sugiyama, Yuta Sakaki |
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| Rok vydání: | 2014 |
| Předmět: |
Biophysics
Enzyme mutation Chitin Crystallography X-Ray Biochemistry Chitin oligosaccharide deacetylase Amidohydrolases chemistry.chemical_compound Protein structure Bacterial Proteins Structural Biology Hydrolase Genetics Amino Acid Sequence Molecular Biology Peptide sequence Domain function Sequence Deletion chemistry.chemical_classification Binding assay biology Vibrio parahaemolyticus Active site Cell Biology Oligosaccharide biology.organism_classification Chitin deacetylase Protein Structure Tertiary Kinetics chemistry biology.protein |
| Zdroj: | FEBS letters. 589(1) |
| ISSN: | 1873-3468 |
| Popis: | The X-ray crystal structure of chitin oligosaccharide deacetylase from Vibrio parahaemolyticus (Vp-COD) was determined at an 1.35Å 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. |
| Databáze: | OpenAIRE |
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