3.5.1.105: chitin disaccharide deacetylase
This is an abbreviated version!
For detailed information about chitin disaccharide deacetylase, go to the full flat file.
Word Map on EC 3.5.1.105
-
3.5.1.105
-
pyrococcus
-
vibrio
-
deacetylation
-
chitinase
-
synthesis
-
horikoshii
-
parahaemolyticus
-
deacetylases
-
n-acetyl
-
thermococcus
-
glucosamine
-
n-acetylglucosamine
-
hyperthermophilic
-
chitinolytic
-
furiosus
-
glcnac-glcn
-
rhizobium
-
chitin-degrading
-
kodakaraensis
-
nodabc
-
chitin-binding
-
diagnostics
- 3.5.1.105
- pyrococcus
- vibrio
-
deacetylation
- chitinase
- synthesis
- horikoshii
- parahaemolyticus
- deacetylases
-
n-acetyl
- thermococcus
- glucosamine
- n-acetylglucosamine
-
hyperthermophilic
-
chitinolytic
- furiosus
-
glcnac-glcn
- rhizobium
-
chitin-degrading
- kodakaraensis
-
nodabc
-
chitin-binding
- diagnostics
Reaction
Synonyms
carbohydrate esterase family 4 chitin oligosaccharide deacetylase, CE family 4 COD, CE-14 deacetylase, ChbG, chitin disaccharide deacetylase, chitin oligosaccharide deacetylase, chitooligosaccharide deacetylase, chitooligosaccharide deacetylase homolog, COD, codA, Dac, Dacph, deacetylase DA1, diacetylchitobiose deacetylase, GlcNAc2 deacetylase, N,N'-diacetylchitobiose deacetylase, NodB, NodB homology domain-containing protein, Pa-COD, PF0354, PGTG_04950, Ph-Dac, PH0499, polysaccharide deacetylase, Sb-COD, Sbal_1411, Tk-Dac, TK1764, VC_1280, Vp-COD, VP2638, YdjC, YDJC deacetylase
ECTree
3.5.1.105 chitin disaccharide deacetylaseAdvanced search results
results (
results (Application
Application on EC 3.5.1.105 - chitin disaccharide deacetylase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
diagnostics
the overall survival is high in lung cancer patients having low expression level of YDJC, while progression free survival is decreased in patients having high expression level of YDJC
synthesis
synthesis
biocatalytic production of glucosamine from N-acetylglucosamine by diacetylchitobiose deacetylase. Although both strains are biocatalytically active, the performance of Bacillus subtilis is 2fold more effective. Establishment of an efficient biotransformation process for the biotechnological production of GlcN in Bacillus subtilis that is more environmentally friendly than the traditional multistep chemical synthesis approach. The overall optimal conditions are 18.6 g/l cells at 40°C, pH 7.5 for 3 h in 3-l bioreactor
synthesis
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
synthesis
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
synthesis
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
synthesis
Dac is a key enzyme used in the biodegradation of chitin and chitosan to produce chitosan oligosaccharides and monosaccharides
synthesis
-
enzymatic production of defined chitosan oligomers with a specific pattern of acetylation using a combination of chitin oligosaccharide deacetylases. Production of chitosan oligomers by partial chemical or physical depolymerisation of the respective polymers has severe disadvantages. Not only does the production of the oligomers typically involve harsh thermo-chemical treatments or strong physical forces, which may be environmentally unfriendly and/or partially destructive to the oligosaccharides produced, but also the production is highly difficult to control leading to broad heterogeneous mixtures, and the outcome is strongly dependent on the chemical and physical characteristics of the starting material. Partial enzymatic hydrolysis of chitosan polymers using chitosan hydrolysing enzymes such as chitinases or chitosanases with well-defined cleavage specificities has been proposed as an alternative to chemical or physical depolymerisation. But, this attempt is also strongly dependent on the starting material and it, too, leads to the production of heterogeneous mixtures of chitosan oligomers. Still, due to the cleavage specificities of the enzymes, the resulting mixture will be better defined than the chitosan oligomer mixtures obtained by chemical or physical depolymerisation
synthesis
enzymatic production of defined chitosan oligomers with a specific pattern of acetylation using a combination of chitin oligosaccharide deacetylases. Production of chitosan oligomers by partial chemical or physical depolymerisation of the respective polymers has severe disadvantages. Not only does the production of the oligomers typically involve harsh thermo-chemical treatments or strong physical forces, which may be environmentally unfriendly and/or partially destructive to the oligosaccharides produced, but also the production is highly difficult to control leading to broad heterogeneous mixtures, and the outcome is strongly dependent on the chemical and physical characteristics of the starting material. Partial enzymatic hydrolysis of chitosan polymers using chitosan hydrolysing enzymes such as chitinases or chitosanases with well-defined cleavage specificities has been proposed as an alternative to chemical or physical depolymerisation. But, this attempt is also strongly dependent on the starting material and it, too, leads to the production of heterogeneous mixtures of chitosan oligomers. Still, due to the cleavage specificities of the enzymes, the resulting mixture will be better defined than the chitosan oligomer mixtures obtained by chemical or physical depolymerisation
synthesis
-
Dac is a key enzyme used in the biodegradation of chitin and chitosan to produce chitosan oligosaccharides and monosaccharides
-
synthesis
-
biocatalytic production of glucosamine from N-acetylglucosamine by diacetylchitobiose deacetylase. Although both strains are biocatalytically active, the performance of Bacillus subtilis is 2fold more effective. Establishment of an efficient biotransformation process for the biotechnological production of GlcN in Bacillus subtilis that is more environmentally friendly than the traditional multistep chemical synthesis approach. The overall optimal conditions are 18.6 g/l cells at 40°C, pH 7.5 for 3 h in 3-l bioreactor
-
synthesis
-
Dac is a key enzyme used in the biodegradation of chitin and chitosan to produce chitosan oligosaccharides and monosaccharides
-
synthesis
-
biocatalytic production of glucosamine from N-acetylglucosamine by diacetylchitobiose deacetylase. Although both strains are biocatalytically active, the performance of Bacillus subtilis is 2fold more effective. Establishment of an efficient biotransformation process for the biotechnological production of GlcN in Bacillus subtilis that is more environmentally friendly than the traditional multistep chemical synthesis approach. The overall optimal conditions are 18.6 g/l cells at 40°C, pH 7.5 for 3 h in 3-l bioreactor
-
synthesis
-
Dac is a key enzyme used in the biodegradation of chitin and chitosan to produce chitosan oligosaccharides and monosaccharides
-
synthesis
-
biocatalytic production of glucosamine from N-acetylglucosamine by diacetylchitobiose deacetylase. Although both strains are biocatalytically active, the performance of Bacillus subtilis is 2fold more effective. Establishment of an efficient biotransformation process for the biotechnological production of GlcN in Bacillus subtilis that is more environmentally friendly than the traditional multistep chemical synthesis approach. The overall optimal conditions are 18.6 g/l cells at 40°C, pH 7.5 for 3 h in 3-l bioreactor
-
synthesis
-
enzymatic production of defined chitosan oligomers with a specific pattern of acetylation using a combination of chitin oligosaccharide deacetylases. Production of chitosan oligomers by partial chemical or physical depolymerisation of the respective polymers has severe disadvantages. Not only does the production of the oligomers typically involve harsh thermo-chemical treatments or strong physical forces, which may be environmentally unfriendly and/or partially destructive to the oligosaccharides produced, but also the production is highly difficult to control leading to broad heterogeneous mixtures, and the outcome is strongly dependent on the chemical and physical characteristics of the starting material. Partial enzymatic hydrolysis of chitosan polymers using chitosan hydrolysing enzymes such as chitinases or chitosanases with well-defined cleavage specificities has been proposed as an alternative to chemical or physical depolymerisation. But, this attempt is also strongly dependent on the starting material and it, too, leads to the production of heterogeneous mixtures of chitosan oligomers. Still, due to the cleavage specificities of the enzymes, the resulting mixture will be better defined than the chitosan oligomer mixtures obtained by chemical or physical depolymerisation
-
synthesis
-
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
-
synthesis
Puccinia graminis f. sp. tritici race SCCL
-
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
-
synthesis
-
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
-
synthesis
-
Dac is a key enzyme used in the biodegradation of chitin and chitosan to produce chitosan oligosaccharides and monosaccharides
-
synthesis
-
biocatalytic production of glucosamine from N-acetylglucosamine by diacetylchitobiose deacetylase. Although both strains are biocatalytically active, the performance of Bacillus subtilis is 2fold more effective. Establishment of an efficient biotransformation process for the biotechnological production of GlcN in Bacillus subtilis that is more environmentally friendly than the traditional multistep chemical synthesis approach. The overall optimal conditions are 18.6 g/l cells at 40°C, pH 7.5 for 3 h in 3-l bioreactor
-
synthesis
-
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
-
synthesis
-
Dac is a key enzyme used in the biodegradation of chitin and chitosan to produce chitosan oligosaccharides and monosaccharides
-
synthesis
-
biocatalytic production of glucosamine from N-acetylglucosamine by diacetylchitobiose deacetylase. Although both strains are biocatalytically active, the performance of Bacillus subtilis is 2fold more effective. Establishment of an efficient biotransformation process for the biotechnological production of GlcN in Bacillus subtilis that is more environmentally friendly than the traditional multistep chemical synthesis approach. The overall optimal conditions are 18.6 g/l cells at 40°C, pH 7.5 for 3 h in 3-l bioreactor
-
synthesis
Shewanella baltica ATCC BAA-1091
-
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
-
synthesis
-
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
-
