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Information on EC 3.5.1.105 - chitin disaccharide deacetylase
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3.5.1.105 chitin disaccharide deacetylaseIUBMB Comments
Chitin oligosaccharide deacetylase is a key enzyme in the chitin catabolic cascade of chitinolytic Vibrio strains. Besides being a nutrient, the heterodisaccharide product 4-O-(N-acetyl-beta-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio parahemolyticus . In contrast to EC 3.5.1.41 (chitin deacetylase) this enzyme is specific for the chitin disaccharide [1,3]. It also deacetylates the chitin trisaccharide with lower efficiency . No activity with higher polymers of GlcNAc [1,3].
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Word Map
- 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
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
diacetylchitobiose deacetylase, chitin oligosaccharide deacetylase, vp-cod, n,n'-diacetylchitobiose deacetylase, chitooligosaccharide deacetylase, pa-cod, deacetylase da1, ydjc deacetylase, chitooligosaccharide deacetylase homolog, ce family 4 cod, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carbohydrate esterase family 4 chitin oligosaccharide deacetylase
CE family 4 COD
CE-14 deacetylase
ChbG
chitin oligosaccharide deacetylase
chitooligosaccharide deacetylase
COD
codA
Dac
Dacph
deacetylase DA1
diacetylchitobiose deacetylase
N,N'-diacetylchitobiose deacetylase
NodB
NodB homology domain-containing protein
Pa-COD
PGTG_04950
Ph-Dac
PH0499
polysaccharide deacetylase
Sb-COD
Sbal_1411
VC_1280
Vp-COD
carbohydrate esterase family 4 chitin oligosaccharide deacetylase
-
-
carbohydrate esterase family 4 chitin oligosaccharide deacetylase
-
-
-
carbohydrate esterase family 4 chitin oligosaccharide deacetylase
-
-
-
CE family 4 COD
Vibrio cholerae serotype O1 RIMD2203102
-
-
-
chitin oligosaccharide deacetylase
Vibrio cholerae serotype O1 RIMD2203102
-
-
-
chitin oligosaccharide deacetylase
-
-
COD
Vibrio cholerae serotype O1 RIMD2203102
-
-
-
NodB homology domain-containing protein
UniProt
-
NodB homology domain-containing protein
UniProt
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N,N'-diacetylchitobiose + H2O = N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-D-glucopyranose acetylhydrolase
Chitin oligosaccharide deacetylase is a key enzyme in the chitin catabolic cascade of chitinolytic Vibrio strains. Besides being a nutrient, the heterodisaccharide product 4-O-(N-acetyl-beta-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio parahemolyticus [2]. In contrast to EC 3.5.1.41 (chitin deacetylase) this enzyme is specific for the chitin disaccharide [1,3]. It also deacetylates the chitin trisaccharide with lower efficiency [3]. No activity with higher polymers of GlcNAc [1,3].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
specific deacetylation at the nonreducing GlcNAc residue
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
specific deacetylation at the nonreducing GlcNAc residue
-
-
?
N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
i.e. N,N'-diacetylchitobiose, the enzyme is involved in chitin catabolic pathway
-
-
?
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
-
i.e. N,N'-diacetylchitobiose, the enzyme is involved in chitin catabolic pathway
-
-
?
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
i.e. N,N'-diacetylchitobiose, the deacetylation site is specific to the nonreducing end residue of (GlcNAc)(2). The enzyme can also deacetylate N-acetyl-D-glucosamine (cf. EC 3.5.1.33)
-
-
?
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
-
i.e. N,N'-diacetylchitobiose, the deacetylation site is specific to the nonreducing end residue of (GlcNAc)(2). The enzyme can also deacetylate N-acetyl-D-glucosamine (cf. EC 3.5.1.33)
-
-
?
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
i.e. N,N'-diacetylchitobiose, the enzyme is involved in chitin catabolic pathway
-
-
?
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
i.e. N,N'-diacetylchitobiose, the deacetylation site is specific to the nonreducing end residue of (GlcNAc)(2). The enzyme can also deacetylate N-acetyl-D-glucosamine (cf. EC 3.5.1.33)
-
-
?
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
i.e. N,N'-diacetylchitobiose, the enzyme is involved in chitin catabolic pathway
-
-
?
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
i.e. N,N'-diacetylchitobiose, the deacetylation site is specific to the nonreducing end residue of (GlcNAc)(2). The enzyme can also deacetylate N-acetyl-D-glucosamine (cf. EC 3.5.1.33)
-
-
?
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
i.e. N,N'-diacetylchitobiose, the enzyme is probably involved in archaeal chitin catabolic pathway
-
-
?
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
i.e. N,N'-diacetylchitobiose, the deacetylation site is specific to the nonreducing end residue of (GlcNAc)(2). The enzyme can also deacetylate N-acetyl-D-glucosamine (cf. EC 3.5.1.33)
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
i.e. N,N-diacetylchitobiose
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
i.e. N,N-diacetylchitobiose
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
i.e. 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-D-glucopyranose. Besides being a nutrient, the heterodisaccharide product 4-O-(N-acetyl-beta-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio bacteria that have the chitin oligosaccharide deacetylase producing ability. Chitin oligosaccharide deacetylase involved in the synthesis of this signal compound is one of the key enzymes in the chitin catabolic cascade of chitinolytic Vibrio strains
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
i.e. 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-D-glucopyranose
i.e. 4-O-(N-acetyl-beta-D-glucosaminyl)-D-glucosamine
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
i.e. N,N-diacetylchitobiose
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
i.e. N,N-diacetylchitobiose
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
i.e. 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-D-glucopyranose. Besides being a nutrient, the heterodisaccharide product 4-O-(N-acetyl-beta-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio bacteria that have the chitin oligosaccharide deacetylase producing ability. Chitin oligosaccharide deacetylase involved in the synthesis of this signal compound is one of the key enzymes in the chitin catabolic cascade of chitinolytic Vibrio strains
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
i.e. 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-D-glucopyranose
i.e. 4-O-(N-acetyl-beta-D-glucosaminyl)-D-glucosamine
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
i.e. N,N-diacetylchitobiose
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
i.e. 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-D-glucopyranose. Besides being a nutrient, the heterodisaccharide product 4-O-(N-acetyl-beta-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio bacteria that have the chitin oligosaccharide deacetylase producing ability. Chitin oligosaccharide deacetylase involved in the synthesis of this signal compound is one of the key enzymes in the chitin catabolic cascade of chitinolytic Vibrio strains
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
i.e. 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-D-glucopyranose
i.e. 4-O-(N-acetyl-beta-D-glucosaminyl)-D-glucosamine
-
?
GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcNAc-beta-(1-4)-GlcN + acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcNAc-beta-(1-4)-GlcN + acetate
i.e. 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-D-glucopyranose. No activity with chitotriose, chitotetraose, chitopentaose and chitohexaose. The 2-acetamido group is completely hydrolyzed within 3 h, no hydrolysis of 2'-acetamide group occurs
i.e. 4-O-(N-acetyl-beta-D-glucosaminyl)-D-glucosamine
-
?
GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcNAc-beta-(1-4)-GlcN + acetate
i.e. 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-D-glucopyranose. No activity with chitotriose, chitotetraose, chitopentaose and chitohexaose. The 2-acetamido group is completely hydrolyzed within 3 h, no hydrolysis of 2'-acetamide group occurs
i.e. 4-O-(N-acetyl-beta-D-glucosaminyl)-D-glucosamine
-
?
GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcNAc-beta-(1-4)-GlcN + acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcNAc-beta-(1-4)-GlcN + acetate
Vibrio cholerae serotype O1 RIMD2203102
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcNAc-beta-(1-4)-GlcN + acetate
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcNAc-beta-(1-4)-GlcN + acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcNAc-beta-(1-4)-GlcN + acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcNAc-beta-(1-4)-GlcN + acetate
-
-
-
-
?
GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcN + acetate
-
-
-
-
?
GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcN + acetate
-
GlcNAc-beta-1,4-GlcN is produced from chitin by the cooperative hydrolytic reactions of both chitinase and chitin oligosaccharide deacetylase
-
-
?
GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcN + acetate
-
-
-
-
?
GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcN + acetate
-
GlcNAc-beta-1,4-GlcN is produced from chitin by the cooperative hydrolytic reactions of both chitinase and chitin oligosaccharide deacetylase
-
-
?
GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcN + acetate
-
-
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
?
-
20% of the activity with GlcNAc-beta-1,4-GlcNAc
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
?
-
30% of the activity with GlcNAc-beta-1,4-GlcNAc
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
?
-
20% of the activity with GlcNAc-beta-1,4-GlcNAc
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
?
-
30% of the activity with GlcNAc-beta-1,4-GlcNAc
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
-
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
-
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
specific deacetylation at the nonreducing GlcNAc residue
-
-
?
N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O
?
-
-
-
?
N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O
?
-
-
-
?
N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O
?
Puccinia graminis f. sp. tritici race SCCL
-
-
-
?
N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O
?
-
-
-
?
N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
-
-
-
?
N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
-
-
-
?
N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
-
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
?
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
?
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
?
Puccinia graminis f. sp. tritici race SCCL
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
?
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
?
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
?
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
?
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
?
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
?
Puccinia graminis f. sp. tritici race SCCL
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
?
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
?
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
?
-
-
-
?
N,N',N''-triacetylchitotriose + H2O
?
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
preferred substrate
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
Shewanella baltica ATCC BAA-1091
preferred substrate
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
preferred substrate
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
preferred substrate
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
preferred substrate
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
preferred substrate
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate
-
-
-
?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
-
-
-
?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
-
-
-
?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
-
-
-
?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
-
-
-
?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
-
-
-
?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
-
-
-
?
additional information
?
-
activity increases with increasing DP
-
-
?
additional information
?
-
activity increases with increasing DP
-
-
?
additional information
?
-
Puccinia graminis f. sp. tritici race SCCL
activity increases with increasing DP
-
-
?
additional information
?
-
enzymatic production of defined chitosan oligomers with a specific pattern of acetylation using a combination of chitin oligosaccharide deacetylases, method evaluation and optimization, overview. Production of specific chitosan oligomers which are deacetylated at the first two units starting from the non-reducing end by the combined use of two different chitin deacetylases, namely NodB from Rhizobium sp. GRH2 that deacetylates the first unit and COD from Vibrio cholerae that deacetylates the second unit starting from the non-reducing end. Both chitin deacetylases accept the product of each other resulting in production of chitosan oligomers with a novel and defined PA. NodB deacetylates exclusively the GlcNAc unit at the non-reducing end. The chitin deacetylase activity of NodB is tested against GlcNAc1-6. NodB is not active towards GlcNAc1, but converts GlcNAc2-6 completely into mono-deacetylated chitosan oligomers
-
-
?
additional information
?
-
enzymatic production of defined chitosan oligomers with a specific pattern of acetylation using a combination of chitin oligosaccharide deacetylases, method evaluation and optimization, overview. Production of specific chitosan oligomers which are deacetylated at the first two units starting from the non-reducing end by the combined use of two different chitin deacetylases, namely NodB from Rhizobium sp. GRH2 that deacetylates the first unit and COD from Vibrio cholerae that deacetylates the second unit starting from the non-reducing end. Both chitin deacetylases accept the product of each other resulting in production of chitosan oligomers with a novel and defined PA. NodB deacetylates exclusively the GlcNAc unit at the non-reducing end. The chitin deacetylase activity of NodB is tested against GlcNAc1-6. NodB is not active towards GlcNAc1, but converts GlcNAc2-6 completely into mono-deacetylated chitosan oligomers
-
-
?
additional information
?
-
chitin oligosaccharide deacetylase (COD) is an enzyme that catalyzes the hydrolysis of the acetamide bond of the second N-acetyl-D-glucosamine (GlcNAc) residue from the non-reducing end of chitin oligosaccharides and shows the highest activity against N,N'-diacetylchitobiose (GlcNAc)2
-
-
?
additional information
?
-
-
chitin oligosaccharide deacetylase (COD) is an enzyme that catalyzes the hydrolysis of the acetamide bond of the second N-acetyl-D-glucosamine (GlcNAc) residue from the non-reducing end of chitin oligosaccharides and shows the highest activity against N,N'-diacetylchitobiose (GlcNAc)2
-
-
?
additional information
?
-
increase in activity DP2 > DP4 > DP3, product analysis
-
-
?
additional information
?
-
product determination by reaction with beta-N-acetylhexisosaminidase (NAGase), an exo-type glycosidase that liberates GlcNAc from non-reducing end of N-acetyl-beta-D-hexosaminides, detected by TLC. No activity of the recombinant enzyme with N-acetyl-D-glucosamine
-
-
?
additional information
?
-
-
product determination by reaction with beta-N-acetylhexisosaminidase (NAGase), an exo-type glycosidase that liberates GlcNAc from non-reducing end of N-acetyl-beta-D-hexosaminides, detected by TLC. No activity of the recombinant enzyme with N-acetyl-D-glucosamine
-
-
?
additional information
?
-
Shewanella baltica ATCC BAA-1091
chitin oligosaccharide deacetylase (COD) is an enzyme that catalyzes the hydrolysis of the acetamide bond of the second N-acetyl-D-glucosamine (GlcNAc) residue from the non-reducing end of chitin oligosaccharides and shows the highest activity against N,N'-diacetylchitobiose (GlcNAc)2
-
-
?
additional information
?
-
Shewanella baltica ATCC BAA-1091
product determination by reaction with beta-N-acetylhexisosaminidase (NAGase), an exo-type glycosidase that liberates GlcNAc from non-reducing end of N-acetyl-beta-D-hexosaminides, detected by TLC. No activity of the recombinant enzyme with N-acetyl-D-glucosamine
-
-
?
additional information
?
-
Shewanella baltica ATCC BAA-1091
increase in activity DP2 > DP4 > DP3, product analysis
-
-
?
additional information
?
-
chitin oligosaccharide deacetylase (COD) is an enzyme that catalyzes the hydrolysis of the acetamide bond of the second N-acetyl-D-glucosamine (GlcNAc) residue from the non-reducing end of chitin oligosaccharides and shows the highest activity against N,N'-diacetylchitobiose (GlcNAc)2
-
-
?
additional information
?
-
product determination by reaction with beta-N-acetylhexisosaminidase (NAGase), an exo-type glycosidase that liberates GlcNAc from non-reducing end of N-acetyl-beta-D-hexosaminides, detected by TLC. No activity of the recombinant enzyme with N-acetyl-D-glucosamine
-
-
?
additional information
?
-
increase in activity DP2 > DP4 > DP3, product analysis
-
-
?
additional information
?
-
-
enzymatic production of defined chitosan oligomers with a specific pattern of acetylation using a combination of chitin oligosaccharide deacetylases, method evaluation and optiization, overview. Production of specific chitosan oligomers which are deacetylated at the first two units starting from the non-reducing end by the combined use of two different chitin deacetylases, namely NodB from Rhizobium sp. GRH2 that deacetylates the first unit and chitin oligosaccharide deacetylase (COD) from Vibrio cholerae that deacetylates the second unit starting from the non-reducing end. Both chitin deacetylases accept the product of each other resulting in production of chitosan oligomers with a novel and defined PA. COD deacetylates the second unit from the non-reducing end. COD is active on short chitin oligosaccharides
-
-
?
additional information
?
-
activity increases with decreasing DP
-
-
?
additional information
?
-
activity increases with decreasing DP
-
-
?
additional information
?
-
activity increases with decreasing DP
-
-
?
additional information
?
-
-
no activity with: GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc, GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc or GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc
-
-
?
additional information
?
-
-
no activity with: GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc, GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc or GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc
-
-
?
additional information
?
-
-
no activity with: GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc, GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc or GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc
-
-
?
additional information
?
-
-
no activity with: GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc, GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc or GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
i.e. N,N'-diacetylchitobiose, the enzyme is involved in chitin catabolic pathway
-
-
?
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
-
i.e. N,N'-diacetylchitobiose, the enzyme is involved in chitin catabolic pathway
-
-
?
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
i.e. N,N'-diacetylchitobiose, the enzyme is involved in chitin catabolic pathway
-
-
?
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
i.e. N,N'-diacetylchitobiose, the enzyme is probably involved in archaeal chitin catabolic pathway
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
i.e. N,N-diacetylchitobiose
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
i.e. N,N-diacetylchitobiose
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
i.e. 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-D-glucopyranose. Besides being a nutrient, the heterodisaccharide product 4-O-(N-acetyl-beta-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio bacteria that have the chitin oligosaccharide deacetylase producing ability. Chitin oligosaccharide deacetylase involved in the synthesis of this signal compound is one of the key enzymes in the chitin catabolic cascade of chitinolytic Vibrio strains
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
i.e. N,N-diacetylchitobiose
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
i.e. N,N-diacetylchitobiose
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
i.e. 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-D-glucopyranose. Besides being a nutrient, the heterodisaccharide product 4-O-(N-acetyl-beta-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio bacteria that have the chitin oligosaccharide deacetylase producing ability. Chitin oligosaccharide deacetylase involved in the synthesis of this signal compound is one of the key enzymes in the chitin catabolic cascade of chitinolytic Vibrio strains
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
i.e. N,N-diacetylchitobiose
-
-
?
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
-
i.e. 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-D-glucopyranose. Besides being a nutrient, the heterodisaccharide product 4-O-(N-acetyl-beta-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio bacteria that have the chitin oligosaccharide deacetylase producing ability. Chitin oligosaccharide deacetylase involved in the synthesis of this signal compound is one of the key enzymes in the chitin catabolic cascade of chitinolytic Vibrio strains
-
-
?
GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcN + acetate
-
GlcNAc-beta-1,4-GlcN is produced from chitin by the cooperative hydrolytic reactions of both chitinase and chitin oligosaccharide deacetylase
-
-
?
GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcN + acetate
-
GlcNAc-beta-1,4-GlcN is produced from chitin by the cooperative hydrolytic reactions of both chitinase and chitin oligosaccharide deacetylase
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
-
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate
-
-
-
?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
-
-
-
?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
-
-
-
?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
-
-
-
?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
-
-
-
?
N-acetyl-D-glucosamine + H2O
D-glucosamine + acetate
-
-
-
?
additional information
?
-
chitin oligosaccharide deacetylase (COD) is an enzyme that catalyzes the hydrolysis of the acetamide bond of the second N-acetyl-D-glucosamine (GlcNAc) residue from the non-reducing end of chitin oligosaccharides and shows the highest activity against N,N'-diacetylchitobiose (GlcNAc)2
-
-
?
additional information
?
-
-
chitin oligosaccharide deacetylase (COD) is an enzyme that catalyzes the hydrolysis of the acetamide bond of the second N-acetyl-D-glucosamine (GlcNAc) residue from the non-reducing end of chitin oligosaccharides and shows the highest activity against N,N'-diacetylchitobiose (GlcNAc)2
-
-
?
additional information
?
-
Shewanella baltica ATCC BAA-1091
chitin oligosaccharide deacetylase (COD) is an enzyme that catalyzes the hydrolysis of the acetamide bond of the second N-acetyl-D-glucosamine (GlcNAc) residue from the non-reducing end of chitin oligosaccharides and shows the highest activity against N,N'-diacetylchitobiose (GlcNAc)2
-
-
?
additional information
?
-
chitin oligosaccharide deacetylase (COD) is an enzyme that catalyzes the hydrolysis of the acetamide bond of the second N-acetyl-D-glucosamine (GlcNAc) residue from the non-reducing end of chitin oligosaccharides and shows the highest activity against N,N'-diacetylchitobiose (GlcNAc)2
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+
the Ph-Dac crystal structure contains a phosphate ion bound to the metal ion, catalytic Zn2+
Zn2+
one Zn2+ ion is bound in the active site pocket. The zinc ion is coordinated by the triad consisting of an aspartic acid residue (Asp36) and two histidine residues (His93 and His97), which are located near the zinc ion
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CDC16
binds to the enzyme and inhibits sphingosylphosphorylcholine (SPC)-induced phosphorylation and reorganization of keratin 8 (K8) induced by YdjC
-
Zinc
the catalytic zinc that is situated at the end of the intermolecular cleft is coordinated by three side chain ligands from His44, Asp47, and His155, and by a phosphate ion derived from the crystallization reservoir solution
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Lung Neoplasms
YdjC chitooligosaccharide deacetylase homolog induces keratin reorganization in lung cancer cells: involvement of interaction between YDJC and CDC16.
Lung Neoplasms
YDJC Induces Epithelial-Mesenchymal Transition via Escaping from Interaction with CDC16 through Ubiquitination of PP2A.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
31.8
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose
pH 8.5, 75°C
0.24
GlcNAc-beta-(1,4)-GlcNAc
pH 7.0, 37°C, recombinant enzyme
1.93
GlcNAc-beta-(1,4)-GlcNAc
pH 7.0, 37°C, recombinant mutant enzyme lacking the carbohydrate-binding domains
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
21.6
GlcNAc-beta-(1,4)-GlcNAc
pH 7.0, 37°C, recombinant mutant enzyme lacking the carbohydrate-binding domains
29.5
GlcNAc-beta-(1,4)-GlcNAc
pH 7.0, 37°C, recombinant enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.77
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose
pH 8.5, 75°C
11.2
GlcNAc-beta-(1,4)-GlcNAc
pH 7.0, 37°C, recombinant mutant enzyme lacking the carbohydrate-binding domains
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.029
purified recombinant enzyme, pH 8.0, 37°C, substrate N,N',N''-triacetylchitotriose
0.22
purified recombinant enzyme, pH 8.0, 37°C, substrate N,N',N'',N'''-tetraacetylchitotetraose
9.4
purified recombinant enzyme, pH 8.0, 37°C, substrate N,N'-diacetylchitobiose
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5 - 9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 11
pH 6.5: about 45% of maximal activity, pH 11: about 55% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
45
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 90
high activity at 40-90°C, 50% of maximal activity at 30°C
37 - 100
activity levels at 37°C and 100°C are about 20% of that observed at the optimal temperature (75°C)
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene chbG or ydjC; gene chbG or ydjC, encoded in the chb operon
UniProt
brenda
gene chbG or ydjC; gene chbG or ydjC, encoded in the chb operon
UniProt
brenda
no activity in Vibrio furnissii
no activity in Vibrio nereis
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
YDJC expression is increased in patient lung adenocarcinoma
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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
metabolism
physiological function
additional information
evolution
the enzyme belongs to the carbohydrate esterase family 4. Amino acid residues that officiate as the metal ion-binding triad and general acidbase catalysts are generally conserved in other Zn-dependent deacetylases
evolution
the enzyme is an evolutionarily conserved protein that belongs to the the YdjC family of proteins
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
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
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
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
evolution
the enzyme belongs to carbohydrate esterase (CE) family 14
evolution
the enzyme belongs to the carbohydrate esterase family 14
evolution
YDJC belongs to the YDJC superfamily and exerts deacetylase activity
evolution
-
the enzyme belongs to carbohydrate esterase (CE) family 14
-
evolution
-
the enzyme belongs to the carbohydrate esterase family 14
-
evolution
-
the enzyme belongs to carbohydrate esterase (CE) family 14
-
evolution
-
the enzyme belongs to the carbohydrate esterase family 14
-
evolution
-
the enzyme belongs to carbohydrate esterase (CE) family 14
-
evolution
-
the enzyme belongs to the carbohydrate esterase family 14
-
evolution
-
the enzyme is an evolutionarily conserved protein that belongs to the the YdjC family of proteins
-
evolution
-
the enzyme belongs to the carbohydrate esterase family 4. Amino acid residues that officiate as the metal ion-binding triad and general acidbase catalysts are generally conserved in other Zn-dependent deacetylases
-
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
-
evolution
Puccinia graminis f. sp. tritici race SCCL
-
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
-
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
-
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
-
evolution
-
the enzyme belongs to carbohydrate esterase (CE) family 14
-
evolution
-
the enzyme belongs to the carbohydrate esterase family 14
-
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
-
evolution
Shewanella baltica ATCC BAA-1091
-
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
-
evolution
Shewanella baltica ATCC BAA-1091
-
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
-
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
-
metabolism
deacetylated chitobiose and chitotriose provide the induction signal necessary for the activation of the ChbR regulator
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
metabolism
involvement of the deacetylase activity of YDJC in keratin reorganization
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
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
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
-
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
-
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
-
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
-
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
-
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
-
metabolism
-
deacetylated chitobiose and chitotriose provide the induction signal necessary for the activation of the ChbR regulator
-
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
-
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
-
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
-
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
-
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
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
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
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
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
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
physiological function
the diacetylchitobiose deacetylase (Dac) plays an important role in a unique chitin degradation pathway in Archaea
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)
physiological function
-
the diacetylchitobiose deacetylase (Dac) plays an important role in a unique chitin degradation pathway in Archaea
-
physiological function
-
the diacetylchitobiose deacetylase (Dac) plays an important role in a unique chitin degradation pathway in Archaea
-
physiological function
-
the diacetylchitobiose deacetylase (Dac) plays an important role in a unique chitin degradation pathway in Archaea
-
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
-
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
-
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
-
physiological function
Puccinia graminis f. sp. tritici race SCCL
-
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
-
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
-
physiological function
-
the diacetylchitobiose deacetylase (Dac) plays an important role in a unique chitin degradation pathway in Archaea
-
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
-
physiological function
-
the diacetylchitobiose deacetylase (Dac) plays an important role in a unique chitin degradation pathway in Archaea
-
physiological function
Shewanella baltica ATCC BAA-1091
-
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
-
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
-
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
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
additional information
three conserved residues Asp11, His61, and His125 form the catalytic triad
additional information
-
three conserved residues Asp11, His61, and His125 form the catalytic triad
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
enzyme structure analysis and modelling, molecular dynamics simulation
additional information
-
enzyme structure analysis and modelling, molecular dynamics simulation
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
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
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
additional information
-
enzyme structure analysis and modelling, molecular dynamics simulation
-
additional information
-
enzyme structure analysis and modelling, molecular dynamics simulation
-
additional information
-
enzyme structure analysis and modelling, molecular dynamics simulation
-
additional information
-
three conserved residues Asp11, His61, and His125 form the catalytic triad
-
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
-
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
-
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
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
-
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
-
enzyme structure analysis and modelling, molecular dynamics simulation
-
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
-
enzyme structure analysis and modelling, molecular dynamics simulation
-
additional information
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
-
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
-
Show AA Sequence and Transmembrane Helices (1471 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
homohexamer
additional information
hexamer
comprised of two trimers. An intermolecular cleft is formed by two polypeptides in the trimeric assembly
hexamer
comprised of two trimers. An intermolecular cleft is formed by two polypeptides in the trimeric assembly
additional information
the Pyrococcus Dac enzyme forms a homohexamer composed of two trimers. A deep cleft exists between two polypeptides in each trimeric assembly, with the central Zn being chelated at the bottom by two His residues and one Asp residue. Determination, analysis and modelling of tertiary structure of Ph-Dac
additional information
-
the Pyrococcus Dac enzyme forms a homohexamer composed of two trimers. A deep cleft exists between two polypeptides in each trimeric assembly, with the central Zn being chelated at the bottom by two His residues and one Asp residue. Determination, analysis and modelling of tertiary structure of Ph-Dac
additional information
-
the Pyrococcus Dac enzyme forms a homohexamer composed of two trimers. A deep cleft exists between two polypeptides in each trimeric assembly, with the central Zn being chelated at the bottom by two His residues and one Asp residue. Determination, analysis and modelling of tertiary structure of Ph-Dac
-
additional information
-
the Pyrococcus Dac enzyme forms a homohexamer composed of two trimers. A deep cleft exists between two polypeptides in each trimeric assembly, with the central Zn being chelated at the bottom by two His residues and one Asp residue. Determination, analysis and modelling of tertiary structure of Ph-Dac
-
additional information
-
the Pyrococcus Dac enzyme forms a homohexamer composed of two trimers. A deep cleft exists between two polypeptides in each trimeric assembly, with the central Zn being chelated at the bottom by two His residues and one Asp residue. Determination, analysis and modelling of tertiary structure of Ph-Dac
-
additional information
-
the Pyrococcus Dac enzyme forms a homohexamer composed of two trimers. A deep cleft exists between two polypeptides in each trimeric assembly, with the central Zn being chelated at the bottom by two His residues and one Asp residue. Determination, analysis and modelling of tertiary structure of Ph-Dac
-
additional information
-
the Pyrococcus Dac enzyme forms a homohexamer composed of two trimers. A deep cleft exists between two polypeptides in each trimeric assembly, with the central Zn being chelated at the bottom by two His residues and one Asp residue. Determination, analysis and modelling of tertiary structure of Ph-Dac
-
additional information
the enzyme comprises one polysaccharide deacetylase domain and two carbohydrate-binding domains
additional information
-
the enzyme comprises one polysaccharide deacetylase domain and two carbohydrate-binding domains
additional information
-
the enzyme comprises one polysaccharide deacetylase domain and two carbohydrate-binding domains
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the native enzyme and its selenomethionine derivative are crystallized and analyzed in the presence and absence of cadmium ion
hanging drop vapor-diffusion method, the crystal structure of the enzyme in complex with 2-deoxy-2-methylphosphoramido-D-glucose demonstrates that Arg92, Asp115, and His152 side chains interact with hydroxyl groups of the glucose moiety of the non-reducing-end GlcNAc residue
purified enzyme in complex with 2-deoxy-2-methylphosphoramido-D-glucose, hanging drop vapor diffusion method, mixing of 0.001 ml of 20 mg/ml protein in 10 mM MPG, 20 mM Tris-HCl, pH 8.1, and 150 mM NaCl, with 0.001 ml of reservoir solution containing either 0.4 M ammonium phosphate (reservoir 1) or 100 mM sodium acetate, pH 4.6, 10 mM CoCl2, and 1 M 1,6-hexanediol (reservoir 2), equilibration against 0.4 ml of reservoir solution, 20°C, X-ray diffraction structure determiantion and analysis at 1.8-1.9 A resolution, modelling
purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 20 mg/ml protein in 20 mM sodium phosphate, pH 7.0, with an equal volume of reservoir solution containing 0.1 M Tris-HCl, pH 7.0, 10% w/v PEG 8000, and 0.2 M MgCl2, 4 weeks, 20°C, X-ray diffraction structure determination and analysis at 1.35 A resolution
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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
-
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
-
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
-
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
-
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
-
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
-
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
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
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
-
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
-
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
-
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
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
-
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
-
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant engineered extracellular enzyme mutant enzymes from Bacillus subtilis by anion exchange chromatography
recombinant enzyme from Escherichia coli strain HMS174(DE3) by ammonium sulfate fractionation, anion exchange and hydrophic interaction chromatography, ultrafiltration, and gel filtration
recombinant StrepII-tagged enzyme from Escherichia coli strain BL21(DE3) by streptactin affinity chromatography
recombinant StrepII-tagged enzyme from Escherichia coli strain Rosetta 2 (DE3) by streptactin affinity chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, anion exchange chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of the soluble recombinant protein in Escherichia coli
gene chbG or ydjC, encoded in the chb operon, DNA and amino acid sequence determination and analysis
gene cod, recombinant expression of StrepII-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3)
-
gene nodB, recombinant expression of StrepII-tagged enzyme in Escherichia coli strain BL21(DE3)
gene PH0499, recombinant expression of the enzyme in Escherichia coli strain BL21(DE3) and in Bacillus subtilis strain WB600, subcloning in Escherichia coli strain JM109, method optimization, overview
gene PH0499, recombinant expression of wild-type and mutants in Bacillus subtilis strain WB600 under control of the HpaII promoter and secreteion as extracellular enzymes, screening of signal peptides from Bacillus subtilis for optimal expression. The signal peptide YncM achieves the highest extracellular diacetylchitobiose deacetylase activity of 13.5 U/ml. Subcloning in Escherichia coli. Quantitative real-time PCR expression analysis. Method optimization, overview
gene Sbal_1411, cloning in Escherichia coli strain DH5alpha and recombinant expression in Escherichia coli strain HMS174(DE3), the recombinant protein is secreted to the culture medium
gene VP2638, quantitative real-time PCR expression analysis
overexpressed as inclusion bodies in Escherichia coli Rosetta (DE3) pLys. The insoluble inclusion body is solubilized and reactivated through a refolding procedure
production of a recombinant chitin oligosaccharide deacetylase from Vibrio parahaemolyticus in the culture medium of Escherichia coli cells. The concentration of the recombinant enzyme in the Escherichia coli culture medium is 150times higher than that of wild-type enzyme produced in the culture medium by Vibrio parahaemolyticus KN1699
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
expression of the soluble recombinant protein in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
COD, encoded by gene VP2638, is detected at a high coverage in the culture supernatant, and its expression appears to be induced by disaccharides over 50fold
sphingosylphosphorylcholine induced expression of YDJC in a dose- and time-dependent manner
the COD activity in the culture fluid to which GlcNAc-GlcN is added is higher than that to which (GlcNAc)2 is added
the transcription is specifically induced by GlcNAc2, suggesting the function of this gene in chitin catabolism in vivo. GlcNAc can not act as an inducer
the COD activity in the culture fluid to which GlcNAc-GlcN is added is higher than that to which (GlcNAc)2 is added
the COD activity in the culture fluid to which GlcNAc-GlcN is added is higher than that to which (GlcNAc)2 is added
-
the COD activity in the culture fluid to which GlcNAc-GlcN is added is higher than that to which (GlcNAc)2 is added
-
the COD activity in the culture fluid to which GlcNAc-GlcN is added is higher than that to which (GlcNAc)2 is added
-
the COD activity in the culture fluid to which GlcNAc-GlcN is added is higher than that to which (GlcNAc)2 is added
-
the COD activity in the culture fluid to which GlcNAc-GlcN is added is higher than that to which (GlcNAc)2 is added
-
-
the COD activity in the culture fluid to which GlcNAc-GlcN is added is higher than that to which (GlcNAc)2 is added
Vibrio cholerae serotype O1 RIMD2203102
-
-
the COD activity in the culture fluid to which GlcNAc-GlcN is added is higher than that to which (GlcNAc)2 is added
-
-
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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
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kadokura, K.; Rokutani, A.; Yamamoto, M.; Ikegami, T.; Sugita, H.; Itoi, S.; Hakamata, W.; Oku, T.; Nishio, T.
Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin
Appl. Microbiol. Biotechnol.
75
357-365
2007
Vibrio parahaemolyticus, Vibrio parahaemolyticus KN1699
brenda
Kadokura, K.; Sakamoto, Y.; Saito, K.; Ikegami, T.; Hirano, T.; Hakamata, W.; Oku, T.; Nishio, T.
Production of a recombinant chitin oligosaccharide deacetylase from Vibrio parahaemolyticus in the culture medium of Escherichia coli cells
Biotechnol. Lett.
29
1209-1215
2007
Vibrio parahaemolyticus, Vibrio parahaemolyticus KN1699
brenda
Kadokura, K.; Sakamoto, Y.; Rokutani, A.; Ikegami, T.; Hirano, T.; Yamamoto, M.; Saito, K.; Hakamata, W.; Itoi, S.; Sugita, H.; Oku, T.; Nishio, T.
Purification, characterization and cloning of Vibrio parahaemolyticus chitinolytic enzymes and application to oligosaccharide production
J. Appl. Glycosci.
55
157-164
2008
Vibrio parahaemolyticus, Vibrio parahaemolyticus KN1699
-
brenda
Ohishi, K.; Yamagishi, M.; Ohta, T.; Motosugi, M.; Izumida, H.; Sano, H.; Adachi, K.; Miwa, T.
Purification and properties of two deacetylases produced by Vibrio alginolyticus H-8
Biosci. Biotechnol. Biochem.
61
1113-1117
1997
Vibrio alginolyticus (Q99PX1), Vibrio alginolyticus H-8 (Q99PX1)
-
brenda
Hirano, T.; Kadokura, K.; Ikegami, T.; Shigeta, Y.; Kumaki, Y.; Hakamata, W.; Oku, T.; Nishio, T.
Heterodisaccharide 4-O-(N-acetyl-beta-D-glucosaminyl)-D-glucosamine is a specific inducer of chitinolytic enzyme production in Vibrios harboring chitin oligosaccharide deacetylase genes
Glycobiology
19
1046-1053
2009
Vibrio proteolyticus, Vibrio alginolyticus, Vibrio parahaemolyticus, Vibrio parahaemolyticus (A6P4T5), Vibrio campbellii, no activity in Vibrio orientalis, no activity in Vibrio furnissii, no activity in Vibrio nereis, Vibrio cholerae serotype O1, Vibrio parahaemolyticus RIMD2210633, Vibrio cholerae serotype O1 RIMD2203102, Vibrio parahaemolyticus KN1699
brenda
Ohishi, K.; Murase, K.; Ohta, T.; Etoh, H.
Cloning and sequencing of the deacetylase gene from Vibrio alginolyticus H-8
J. Biosci. Bioeng.
90
561-563
2000
Vibrio alginolyticus (Q99PX1), Vibrio alginolyticus H-8 (Q99PX1), Vibrio alginolyticus H-8
brenda
Hirano, T.; Aoki, M.; Kadokura, K.; Kumaki, Y.; Hakamata, W.; Oku, T.; Nishio, T.
Heterodisaccharide 4-O-(N-acetyl-beta-D-glucosaminyl)-D-glucosamine is an effective chemotactic attractant for Vibrio bacteria that produce chitin oligosaccharide deacetylase
Lett. Appl. Microbiol.
53
161-166
2011
Vibrio alginolyticus, Vibrio parahaemolyticus, no activity in Vibrio furnissii, no activity in Vibrio nereis, Vibrio parahaemolyticus RIMD2210633, no activity in Vibrio nereis NBRC15637, Vibrio parahaemolyticus KN1699, no activity in Vibrio furnissii RIMD2223001, Vibrio alginolyticus NBRC15630
brenda
Tanaka, T.; Fukui, T.; Fujiwara, S.; Atomi, H.; Imanaka, T.
Concerted action of diacetylchitobiose deacetylase and exo-beta-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
J. Biol. Chem.
279
30021-30027
2004
Thermococcus kodakarensis (Q6F4N1)
brenda
Mine, S.; Ikegami, T.; Kawasaki, K.; Nakamura, T.; Uegaki, K.
Expression, refolding, and purification of active diacetylchitobiose deacetylase from Pyrococcus horikoshii
Protein Expr. Purif.
84
265-269
2012
Pyrococcus horikoshii (O58235), Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428 (O58235)
brenda
Liu, B.; Ni, J.F.; Shen, Y.L.
Cloning, expression and biochemical characterization of a novel diacetylchitobiose deacetylase from the hyperthermophilic archaeon Pyrococcus horikoshii
Wei Sheng Wu Xue Bao
46
255-258
2006
Pyrococcus horikoshii (O58235), Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428 (O58235)
brenda
Mine, S.; Niiyama, M.; Hashimoto, W.; Ikegami, T.; Koma, D.; Ohmoto, T.; Fukuda, Y.; Inoue, T.; Abe, Y.; Ueda, T.; Morita, J.; Uegaki, K.; Nakamura, T.
Expression from engineered Escherichia coli chromosome and crystallographic study of archaeal N,N'-diacetylchitobiose deacetylase
FEBS J.
281
2584-2596
2014
Pyrococcus horikoshii (O58235), Pyrococcus horikoshii, Pyrococcus furiosus (Q8U3V1)
brenda
Nakamura, T.; Niiyama, M.; Hashimoto, W.; Ida, K.; Abe, M.; Morita, J.; Uegaki, K.
Multiple crystal forms of N,N'-diacetylchitobiose deacetylase from Pyrococcus furiosus
Acta Crystallogr. Sect. F
71
657-662
2015
Pyrococcus furiosus (Q8U3V1), Pyrococcus furiosus
brenda
Hirano, T.; Sugiyama, K.; Sakaki, Y.; Hakamata, W.; Park, S.Y.; Nishio, T.
Structure-based analysis of domain function of chitin oligosaccharide deacetylase from Vibrio parahaemolyticus
FEBS Lett.
589
145-151
2015
Vibrio parahaemolyticus (A6P4T5), Vibrio parahaemolyticus, Vibrio parahaemolyticus KN1699 (A6P4T5)
brenda
Verma, S.; Mahadevan, S.
The ChbG gene of the chitobiose (chb) operon of Escherichia coli encodes a chitooligosaccharide deacetylase
J. Bacteriol.
194
4959-4971
2012
Escherichia coli (P37794), Escherichia coli, Escherichia coli BW25113 (P37794)
brenda
Nakamura, T.; Yonezawa, Y.; Tsuchiya, Y.; Niiyama, M.; Ida, K.; Oshima, M.; Morita, J.; Uegaki, K.
Substrate recognition of N,N'-diacetylchitobiose deacetylase from Pyrococcus horikoshii
J. Struct. Biol.
195
286-293
2016
Pyrococcus horikoshii (O58235), Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428 (O58235), Pyrococcus horikoshii NBRC 100139 (O58235), Pyrococcus horikoshii JCM 9974 (O58235), Pyrococcus horikoshii ATCC 700860 (O58235), Pyrococcus horikoshii OT-3 (O58235)
brenda
Jiang, Z.; Niu, T.; Lv, X.; Liu, Y.; Li, J.; Lu, W.; Du, G.; Chen, J.; Liu, L.
Secretory expression fine-tuning and directed evolution of diacetylchitobiose deacetylase by Bacillus subtilis
Appl. Environ. Microbiol.
85
e01076-19
2019
Pyrococcus horikoshii (O58235), Pyrococcus horikoshii ATCC 700860 (O58235), Pyrococcus horikoshii DSM 12428 (O58235), Pyrococcus horikoshii JCM 9974 (O58235), Pyrococcus horikoshii NBRC 100139 (O58235), Pyrococcus horikoshii OT-3 (O58235)
brenda
Hirano, T.; Shiraishi, H.; Ikejima, M.; Uehara, R.; Hakamata, W.; Nishio, T.
Chitin oligosaccharide deacetylase from Shewanella baltica ATCC BAA-1091
Biosci. Biotechnol. Biochem.
81
547-550
2017
Shewanella baltica (A3D2G6), Shewanella baltica, Shewanella baltica OS155 (A3D2G6), Shewanella baltica ATCC BAA-1091 (A3D2G6)
brenda
Kaczmarek, M.; Struszczyk-Swita, K.; Li, X.; Szczesna-Antczak, M.; Daroch, M.
Enzymatic modifications of chitin, chitosan, and chitooligosaccharides
Front. Bioeng. Biotechnol.
7
243
2019
Shewanella baltica (A3D2G6), Puccinia graminis f. sp. tritici (E3K3D7), Vibrio cholerae serotype O1 (Q9KSH6), Vibrio cholerae serotype O1 El Tor Inaba N16961 (Q9KSH6), Puccinia graminis f. sp. tritici race SCCL (E3K3D7), Shewanella baltica OS155 (A3D2G6), Puccinia graminis f. sp. tritici CRL 75-36-700-3 (E3K3D7), Shewanella baltica ATCC BAA-1091 (A3D2G6), Vibrio cholerae serotype O1 ATCC 39315 (Q9KSH6)
brenda
Hirano, T.; Okubo, M.; Tsuda, H.; Yokoyama, M.; Hakamata, W.; Nishio, T.
Chitin heterodisaccharide, released from chitin by chitinase and chitin oligosaccharide deacetylase, enhances the chitin-metabolizing ability of Vibrio parahaemolyticus
J. Bacteriol.
201
e00270-19
2019
Vibrio parahaemolyticus RIMD 2210633 (Q87LH9), Vibrio parahaemolyticus RIMD 2210633
brenda
Jiang, Z.; Lv, X.; Liu, Y.; Shin, H.D.; Li, J.; Du, G.; Liu, L.
Biocatalytic production of glucosamine from N-acetylglucosamine by diacetylchitobiose deacetylase
J. Microbiol. Biotechnol.
28
1850-1858
2018
Pyrococcus horikoshii (O58235), Pyrococcus horikoshii DSM 12428 (O58235), Pyrococcus horikoshii NBRC 100139 (O58235), Pyrococcus horikoshii JCM 9974 (O58235), Pyrococcus horikoshii ATCC 700860 (O58235), Pyrococcus horikoshii OT-3 (O58235)
brenda
Kim, E.J.; Park, M.K.; Byun, H.J.; Kang, G.J.; Yu, L.; Kim, H.J.; Shim, J.G.; Lee, H.; Lee, C.H.
YdjC chitooligosaccharide deacetylase homolog induces keratin reorganization in lung cancer cells involvement of interaction between YDJC and CDC16
Oncotarget
9
22915-22928
2018
Homo sapiens (A8MPS7), Homo sapiens
brenda
Hamer, S.; Cord-Landwehr, S.; Biarnes, X.; Planas, A.; Waegeman, H.; Moerschbacher, B.; Kolkenbrock, S.
Enzymatic production of defined chitosan oligomers with a specific pattern of acetylation using a combination of chitin oligosaccharide deacetylases
Sci. Rep.
5
8716
2015
Vibrio cholerae, Rhizobium sp. (A0A0N7AXL7), Rhizobium sp. GRH2 (A0A0N7AXL7)
brenda
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