EC Number   |
General Information |
Reference |
|---|
   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 | evolution |
chitin deacetylases and chitooligosaccharides deacetylases [EC 3.5.1.105 (CODa)]. ChDas and CODa are a group of enzymes catalyzing the hydrolysis of acetamido groups of N-acetyl-D-glucosamine residues in chitin, chitosan and chitooligosaccharides, respectively. Both of these groups of enzymes are classified in the carbohydrate esterase family 4 (CE4) in the CAZY database |
-, 753650 |
| 3.5.1.105 | evolution |
chitin oligosaccharide deacetylase (COD) typically comprise two carbohydrate-binding domains (CBDs) and one polysaccharide deacetylase domain. In contrast, Shewanella baltica ATCC BAA-1091 COD (Sb-COD) has only one CBD, yet exhibits chitin-binding properties and substrate specificities similar to those of other CODs |
-, 753032 |
| 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 |
| 3.5.1.105 | metabolism |
deacetylated chitobiose and chitotriose provide the induction signal necessary for the activation of the ChbR regulator |
-, 734074 |
| 3.5.1.105 | metabolism |
diacetylchitobiose deacetylase works in the chitin degradation pathway in combination with glucosaminidase to hydrolyze diacetylchitobiose (GlcNAc2) to glucosamine (GlcN). First, the N-acetyl group of GlcNAc2 is catalyzed by Dac from the nonreducing end residue N-acetylglucosamine (GlcNAc) of GlcNAc2 and generates the product GlcN-GlcNAc, the product (GlcNGlcNAc) is then hydrolyzed by glucosaminidase following degradation into GlcN and GlcNAc. Finally, the resulting monomer GlcNAc is catalyzed by Dac to generate GlcN |
-, 752555 |
| 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 | malfunction |
gene silencing of YDJC suppresses sphingosylphosphorylcholine (SPC)-induced events. YdjC overexpression induces the SPC-induced events. YdjC deacetylase dominant negative mutant (YDJCD13A) does not induce SPC-induced events. YDJC siRNA reduces ERK activation and overexpression of YDJC induces ERK activation. The siRNA of ERK1 or ERK2 suppresses YDJC-induced phosphorylation and reorganization of keratin 8 (K8), and migration and invasion |
754966 |
| 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 |
