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	evolution	the enzyme belongs to carbohydrate esterase (CE) family 14	-, 745652	
3.5.1.105	evolution	the enzyme belongs to the carbohydrate esterase family 14	-, 752555	
3.5.1.105	evolution	the enzyme belongs to the carbohydrate esterase family 4. Amino acid residues that officiate as the metal ion-binding triad and general acid–base catalysts are generally conserved in other Zn-dependent deacetylases	-, 733875	
3.5.1.105	evolution	the enzyme is an evolutionarily conserved protein that belongs to the the YdjC family of proteins	-, 734074	
3.5.1.105	evolution	YDJC belongs to the YDJC superfamily and exerts deacetylase activity	754966	
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	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	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	additional information	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	additional information	enzyme structure analysis and modelling, molecular dynamics simulation	-, 745652	
3.5.1.105	additional information	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	additional information	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	additional information	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	additional information	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	
3.5.1.105	physiological function	role and molecular mechanisms of YdjC chitooligosaccharide deacetylase homologue YDJC in sphingosylphosphorylcholine (SPC)-induced phosphorylation and reorganization of keratin 8 (K8), and migration and invasion (SPC-induced events), overview	754966	
3.5.1.105	physiological function	the diacetylchitobiose deacetylase (Dac) plays an important role in a unique chitin degradation pathway in Archaea	-, 752555	
3.5.1.105	physiological function	the enzyme generates beta-N-acetyl-D-glucosaminyl-(1,4)-D-glucosamine from (GlcNAc)2, in strain KN1699, GlcNAc-GlcN is an end product of chitin degradation outside the cell	-, 733875	
3.5.1.105	physiological function	the enzyme hydrolyzes the N-acetyl group at the reducing-end GlcNAc residue of (GlcNAc)2 to generate the heterodisaccharide beta-N-acetyl-D-glucosaminyl-(1,4)-D-glucosamine (GlcNAc-GlcN)	754021	
3.5.1.105	physiological function	the monodeacetylase that is essential for growth on the acetylated chitooligosaccharides chitobiose and chitotriose but is dispensable for growth on cellobiose and chitosan dimer, the deacetylated form of chitobiose. Activation of the chb promoter by the regulatory protein ChbR is dependent on ChbG, deacetylation of chitobiose-6-phosphate and chitotriose-6-phosphate is necessary for their recognition by ChbR as inducers. ChbR-independent expression of the permease and phospho-beta-glucosidase from a heterologous promoter did not support growth on both chitobiose and chitotriose in the absence of chbG, suggesting an additional role of chbG in the hydrolysis of chitooligosaccharides	-, 734074