EC Number   |
General Information |
Reference |
|---|
   3.5.1.105 | metabolism |
involvement of the deacetylase activity of YDJC in keratin reorganization |
754966 |
| 3.5.1.105 | metabolism |
N,N'-diacetylchitobiose deacetylase (Dac) belongs to the CE-14 family and plays a role in the chitinolytic pathway in archaea by deacetylating N,N'-diacetylchitobiose (GlcNAc2), which is the end product of chitinase |
-, 745652 |
| 3.5.1.105 | metabolism |
Vibrio parahaemolyticus strain RIMD 2210633 secretes both chitinase and chitin oligosaccharide deacetylase (COD) and produces beta-N-acetyl-D-glucosaminyl-(1,4)-D-glucosamine (GlcNAc-GlcN) from chitin. GlcNAc-GlcN induces chitinase production by several strains of Vibrio harboring chitin oligosaccharide deacetylase genes. Enzyme chitin oligosaccharide deacetylase is involved in the Vibrio chitin degradation system degrading N,N'-diacetylchitobiose, a homodisaccharide produced from chitin, which is known to induce the expression of genes encoding several proteins involved in chitin metabolism in Vibrio strains. (GlcNAc)2 is deacetylated to GlcNAc-GlcN by COD |
754021 |
| 3.5.1.105 | more |
biotransformation of chitin into chitosan through enzymatic deacetylation can be achieved with chitin deacetylases (EC 3.5.1.41, ChDa). Other enzymes involved in chitin and chitosan conversion are chitinases (EC 3.2.1.14) and chitosanases (EC 3.2.1.132). Both of them catalyze the hydrolysis of glycosidic bonds but differ in substrate specificity, hydrolysing bonds of chitin and chitosan, respectively. Obtained chitooligosaccharides can be further enzymatically modified by chitooligosaccharides deacetylases (EC 3.5.1.105, CODa) to obtain products with desired chain arrangement |
-, 753650 |
| 3.5.1.105 | more |
enzyme structure analysis and modelling, molecular dynamics simulation |
-, 745652 |
| 3.5.1.105 | more |
examination of the induction of protein expression by several sugars released from chitin using peptide mass fingerprinting and confirming the expression of genes encoding enzymes involved in chitin metabolism using real-time quantitative PCR analysis, detailed overview |
754021 |
| 3.5.1.105 | more |
His291 and Asp35, which are in the vicinity of the zinc ion-binding triad, act as the catalytic base and acid, respectively. The enzyme comprises one polysaccharide deacetylase domain and two carbohydrate-binding domains. The carbohydrate-binding domains are unlikely to affect the configuration of the active center residues in active site of polysaccharide deacetylase domain, overview |
-, 733875 |
| 3.5.1.105 | more |
pattern of acetylation of GlcNAc5 after hydrolysis with NodB from Rhizobium sp. strain GRH2 by enzymatic sequencing in combination with UHPLC-ELSD-ESI-MS analysis, overview |
-, 755414 |
| 3.5.1.105 | more |
three conserved residues Asp11, His61, and His125 form the catalytic triad |
-, 734074 |
| 3.5.1.105 | physiological function |
CODa isolated from different sources exhibit different catalytic mechanisms, indicating that a variety of well-defined chitooligosaccharides can be produced during a single enzymatic reaction |
-, 753650 |
