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
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3.5.1.105
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pyrococcus
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vibrio
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deacetylation
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chitinase
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synthesis
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horikoshii
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parahaemolyticus
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deacetylases
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n-acetyl
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thermococcus
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glucosamine
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n-acetylglucosamine
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hyperthermophilic
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chitinolytic
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furiosus
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glcnac-glcn
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rhizobium
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chitin-degrading
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kodakaraensis
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nodabc
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chitin-binding
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diagnostics
- 3.5.1.105
- pyrococcus
- vibrio
-
deacetylation
- chitinase
- synthesis
- horikoshii
- parahaemolyticus
- deacetylases
-
n-acetyl
- thermococcus
- glucosamine
- n-acetylglucosamine
-
hyperthermophilic
-
chitinolytic
- furiosus
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glcnac-glcn
- rhizobium
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chitin-degrading
- kodakaraensis
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nodabc
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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
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results (Engineering
Engineering on EC 3.5.1.105 - chitin disaccharide deacetylase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D13A
site-directed mutagenesis, the enzyme mutant lost its activity to induce sphingosylphosphorylcholine (SPC)-induced phosphorylation and reorganization of keratin 8. Overexpression of YDJCD13A cannot induce K8 phosphorylation, and YDJCD13A overexpression suppresses SPC-induced migration and invasion of A549 lung cancer cells. For gene silencing of YDJC, the A-549, H-1703, and H-23 cells are transfected with YDJC siRNA or control siRNA and stimulated with or without SPC
R157H
site-directed mutagenesis, the mutant exhibits increased specific activity compared to the wild-type
R157T
site-directed mutagenesis, the mutant R157T exhibits much higher specific activity than the wild-type. Achievement of efficient secretory production and improvement of the catalytic efficiency of diacetylchitobiose deacetylase in Bacillus subtilis
R157W
site-directed mutagenesis, the mutant exhibits increased specific activity compared to the wild-type
R157H
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site-directed mutagenesis, the mutant exhibits increased specific activity compared to the wild-type
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R157T
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site-directed mutagenesis, the mutant R157T exhibits much higher specific activity than the wild-type. Achievement of efficient secretory production and improvement of the catalytic efficiency of diacetylchitobiose deacetylase in Bacillus subtilis
-
R157W
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site-directed mutagenesis, the mutant exhibits increased specific activity compared to the wild-type
-
R157H
-
site-directed mutagenesis, the mutant exhibits increased specific activity compared to the wild-type
-
R157T
-
site-directed mutagenesis, the mutant R157T exhibits much higher specific activity than the wild-type. Achievement of efficient secretory production and improvement of the catalytic efficiency of diacetylchitobiose deacetylase in Bacillus subtilis
-
R157W
-
site-directed mutagenesis, the mutant exhibits increased specific activity compared to the wild-type
-
R157H
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site-directed mutagenesis, the mutant exhibits increased specific activity compared to the wild-type
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R157T
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site-directed mutagenesis, the mutant R157T exhibits much higher specific activity than the wild-type. Achievement of efficient secretory production and improvement of the catalytic efficiency of diacetylchitobiose deacetylase in Bacillus subtilis
-
R157W
-
site-directed mutagenesis, the mutant exhibits increased specific activity compared to the wild-type
-
R157H
-
site-directed mutagenesis, the mutant exhibits increased specific activity compared to the wild-type
-
R157T
-
site-directed mutagenesis, the mutant R157T exhibits much higher specific activity than the wild-type. Achievement of efficient secretory production and improvement of the catalytic efficiency of diacetylchitobiose deacetylase in Bacillus subtilis
-
R157W
-
site-directed mutagenesis, the mutant exhibits increased specific activity compared to the wild-type
-
R157H
-
site-directed mutagenesis, the mutant exhibits increased specific activity compared to the wild-type
-
R157T
-
site-directed mutagenesis, the mutant R157T exhibits much higher specific activity than the wild-type. Achievement of efficient secretory production and improvement of the catalytic efficiency of diacetylchitobiose deacetylase in Bacillus subtilis
-
R157W
-
site-directed mutagenesis, the mutant exhibits increased specific activity compared to the wild-type
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additional information
additional information
growth of different mutant strains on various beta-glucosides as the sole carbon source. Effect of chbG deletion on transcriptional activation of the chb promoter in Cel+ mutants carrying a deletion of nagC and different activating mutations in chbR, overview. The Vibrio cholerae homologue of chbG can rescue the effect of the Escherichia coli chbG mutation
additional information
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growth of different mutant strains on various beta-glucosides as the sole carbon source. Effect of chbG deletion on transcriptional activation of the chb promoter in Cel+ mutants carrying a deletion of nagC and different activating mutations in chbR, overview. The Vibrio cholerae homologue of chbG can rescue the effect of the Escherichia coli chbG mutation
additional information
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growth of different mutant strains on various beta-glucosides as the sole carbon source. Effect of chbG deletion on transcriptional activation of the chb promoter in Cel+ mutants carrying a deletion of nagC and different activating mutations in chbR, overview. The Vibrio cholerae homologue of chbG can rescue the effect of the Escherichia coli chbG mutation
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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
additional information
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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
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additional information
Puccinia graminis f. sp. tritici race SCCL
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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
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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
additional information
Shewanella baltica ATCC BAA-1091
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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
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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
-
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
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
-
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
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additional information
removal of the carbohydrate-binding domains is unlikely to affect the configuration of the active center residues in the polysaccharide deacetylase domain, although that of amino acid residues interacting with (GlcNAc)2 changes slightly
additional information
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removal of the carbohydrate-binding domains is unlikely to affect the configuration of the active center residues in the polysaccharide deacetylase domain, although that of amino acid residues interacting with (GlcNAc)2 changes slightly
additional information
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removal of the carbohydrate-binding domains is unlikely to affect the configuration of the active center residues in the polysaccharide deacetylase domain, although that of amino acid residues interacting with (GlcNAc)2 changes slightly
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