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(N-acetyl-D-glucosamine)2 + H2O
(GlcN)GlcNAc + acetate
-
-
-
-
?
(N-acetyl-D-glucosamine)3
(GlcN)2GlcNAc + acetate
-
-
-
-
?
(N-acetyl-D-glucosamine)4
(GlcN)3GlcNAc + acetate
-
-
-
-
?
(N-acetyl-D-glucosamine)4 + H2O
(GlcN)3GlcNAc + acetate
-
-
-
-
?
(N-acetyl-D-glucosamine)5
(GlcN)4GlcNAc + acetate
-
-
-
-
?
(N-acetyl-D-glucosamine)5 + H2O
(GlcN)4GlcNAc + acetate
-
-
-
-
?
(N-acetyl-D-glucosamine)7 + H2O
(GlcN)6GlcNAc + acetate
-
-
-
-
?
2 N,N',N'',N''',N''''-pentaacetylchitopentaose + 3 H2O
GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc + GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc + 3 acetate
-
-
initial product: mixture of two isomers, no processivity
?
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-bromoacetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-D-glucose + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNbeta(1-4)GlcNAc + bromoacetate
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-chloroacetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-D-glucose + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNbeta(1-4)GlcNAc + chloroacetate
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-fluoroacetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-D-glucose + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNbeta(1-4)GlcNAc + fluoroacetate
-
-
-
?
3 N,N',N''-triacetylchitotriose + 2 H2O
GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN + GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc + GlcN-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc + 3 acetate
-
no detectable hydrolysis at low substrate concentrations i.e. 0.1 mM
initial product: mixture of three isomers
?
4-nitroacetanilide + H2O
4-nitroaniline + acetate
-
-
-
-
?
4-nitroacetanilide + H2O
?
acetylated chitin oligomer + H2O
?
acetylated chitin polymer + H2O
?
acetylated chitosan + H2O
?
acetylated chitosan oligomer + H2O
?
increasing activity with increasing degree of acetylation
-
-
?
acetylated chitosan oligosaccharide + H2O
?
acetylated chitosan polymer + H2O
?
acetylated glucoronoxylan + H2O
?
carboxymethylchitin + H2O
?
-
-
-
-
?
chitin + H2O
chitosan + acetate
chitin + H2O
deacetylated chitin + acetate
-
-
-
?
chitin pentamer + H2O
?
-
-
-
?
chitobiose + acetate
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-D-glucose + H2O
-
-
-
?
chitohexaose + H2O
?
-
-
-
-
?
chitooligosaccharides + H2O
?
chitooligosaccharides + H2O
deacetylated chitooligosaccharides + acetate
chitosan + H2O
deacetylated chitosan + acetate
chitosan hexamer + H2O
?
-
-
-
?
chitosan tetramer + acetate
beta-N-acetyl-D-glucosamine-(1-4)-beta-N-acetyl-D-glucosamine-(1-4)-beta-N-acetyl-D-glucosamine-(1-4)-D-glucosamine + H2O
-
-
beta-D-GlcNAc-(1-4)-beta-D-GlcNAc-(1-4)-beta-D-GlcNAc-(1-4)-D-GlcN
?
chitotetraose + acetate
? + H2O
-
-
mixture of partially acetylated compounds
?
CM chitin + H2O
?
-
8% degree of deacetylation with 13% activity compared to water-soluble chitin with degree of deacetylation 50%
-
-
?
colloidal chitin + H2O
deacetylated colloidal chitin + acetate
crab chitosan + H2O
?
-
71-88% degree of deacetylation with 21-10% activity compared to water-soluble chitin with degree of deacetylation 50%
-
-
?
crab crystalline chitin + H2O
?
-
worst substrate (0.5% deacetylation)
-
-
?
crab swollen chitin + H2O
?
-
1.7% deacetylation
-
-
?
di-N-acetylchitobiose + H2O
?
ethylene glycol chitin + H2O
chitosan + acetate
-
best substrate (24.5% deacetlyation)
-
-
?
GlcNAc-beta-(1-4)-GlcNAc + H2O
acetate + ?
-
20% of the Vmax obtained with glycol-chitin
-
-
?
GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN + 2 acetate
GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcNAc + acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcN-beta-(1-4)-GlcNAc + H2O
?
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcN-beta-(1-4)-GlcNAc + H2O
GlcNAc-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcNAc + GlcN-beta-(1-4)-GlcNAc-beta-(1-4)-GlcN-beta-(1-4)-GlcNAc + acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
acetate + ?
-
27% of the Vmax obtained with glycol-chitin
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
acetate + GlcN-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc + GlcNAc-beta-(1,4)-GlcN-beta-(1,4)-GlcNAc + GlcNAc-beta-(1,4)-GlcNAc-beta-(1,4)-GlcN
-
time courses for hydrolysis of the N-acetyl groups are followed spectrometrically
GlcN-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc, GlcNAc-beta-(1,4)-GlcN-beta-(1,4)-GlcNAc and GlcNAc-beta-(1,4)-GlcNAc-beta-(1,4)-GlcN are formed in the proportions 22:50:28
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
acetate + ?
-
50% of the Vmax obtained with glycol-chitin
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcN-beta-(1-4)-GlcNAc + acetate
-
time courses for hydrolysis of the N-acetyl groups are followed spectrometrically
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
acetate + ?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
acetate + ?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
GlcNAc-beta-1,4-GlcNAc + H2O
?
-
-
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
?
-
-
-
-
?
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-GlcNAc + H2O
?
-
-
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
?
-
-
-
-
?
GlcNAcbeta(1-4)GlcNAc + H2O
?
-
-
-
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
?
-
-
-
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNbeta(1-4)GlcNAc + acetate
-
-
-
?
GlcNAcGlcNAcGlcNAcGlcN + H2O
?
-
-
-
-
?
GlcNAcGlcNGlcNAcGlcNAc + H2O
?
-
-
-
-
?
GlcNGlcNAcGlcNAcGlcNAc + H2O
?
-
-
-
-
?
glycol chitin + H2O
chitosan + acetate
glycol chitin + H2O
deacetylated glycol chitin + acetate
glycol chitosan + H2O
?
-
-
-
-
?
glycol-chitin + H2O
? + acetate
-
-
-
-
?
hepta-N-acetylchitoheptaose + H2O
?
-
100% activity
-
-
?
hexa-N-acetyl-chitohexaose + H2O
chitohexaose + 6 acetate
A0A1U8QU02
-
-
-
?
hexa-N-acetyl-chitohexaose + H2O
chitohexaose + acetate
hexa-N-acetylchitohexaose + H2O
?
hexa-N-acetylchitohexaose + H2O
chitohexaose + acetate
-
-
-
-
?
monoacetylated chitopentaose + H2O
chitopentaose + acetate
-
-
-
-
?
monoacetylated chitotetraose + H2O
chitotetraose + acetate
-
-
-
-
?
monoacetylated chitotriose + H2O
chitotriose + acetate
-
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + 4 H2O
3 GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc + GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc + GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc + 4 acetate
-
-
initial product: mixture of three isomers, no processivity
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN + acetate
-
-
end product, initial products: (GlcN)3(GlcN)2GlcNAc + (GlcN)4GlcNAcGlcNAc, processive, reducing-end residue remains intact
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + 5 H2O
chitopentaose + 5 acetate
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
?
N,N',N'',N'''-tetraacetylchitotetraose + 4 H2O
chitotetraose + 4 acetate
N,N',N'',N'''-tetraacetylchitotetraose + H2O
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc + acetate
-
-
after 10 min, only product, no processivity
?
N,N',N''-triacetylchitotriose + 2 H2O
GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc + 2 acetate
N,N',N''-triacetylchitotriose + H2O
?
N,N'-diacetylchitobiose + H2O
?
N,N'-diacetylchitobiose + H2O
deacetylated chitooligosaccharides + acetate
N-acetylglucosamine + H2O
?
-
-
-
-
?
N-acetylglucosamine oligomer + H2O
?
p-nitrophenyl 2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranoside + acetate
p-nitrophenyl N,N'-diacetyl-beta-chitobioside + H2O
-
-
-
?
penta-N-acetyl-chitopentaose + H2O
chitopentaose + 5 acetate
A0A1U8QU02
-
-
-
?
penta-N-acetyl-chitopentaose + H2O
chitopentaose + acetate
penta-N-acetylchitopentaose + H2O
?
peritrophic matrix chitin + H2O
?
-
-
-
?
shrimp alpha-chitin powder + H2O
?
-
0.7% deacetylation
-
-
?
shrimp swollen chitin + H2O
?
-
2.1% deacetylation
-
-
?
squid beta-chitin powder + H2O
?
-
3.6% deacetylation
-
-
?
swollen chitin + H2O
?
-
8% degree of deacetylation with 6% activity compared to water-soluble chitin with degree of deacetylation 50%
-
-
?
tetra-N-acetyl-chitotetraose + H2O
chitotetraose + acetate
tetra-N-acetylchitotetraose + H2O
?
tri-N-acetylchitotriose + H2O
?
WSCT-50 + H2O
? + acetate
additional information
?
-
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-bromoacetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-D-glucose + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNbeta(1-4)GlcNAc + bromoacetate
-
-
-
?
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-bromoacetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-D-glucose + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNbeta(1-4)GlcNAc + bromoacetate
-
-
-
?
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-chloroacetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-D-glucose + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNbeta(1-4)GlcNAc + chloroacetate
-
-
-
?
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-chloroacetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-D-glucose + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNbeta(1-4)GlcNAc + chloroacetate
-
-
-
?
4-nitroacetanilide + H2O
?
-
-
-
-
?
4-nitroacetanilide + H2O
?
-
-
-
-
?
acetylated chitin oligomer + H2O
?
-
-
-
?
acetylated chitin oligomer + H2O
?
-
-
-
?
acetylated chitin oligomer + H2O
?
-
-
-
?
acetylated chitin oligomer + H2O
?
-
-
-
?
acetylated chitin oligomer + H2O
?
-
-
-
?
acetylated chitin polymer + H2O
?
-
-
-
?
acetylated chitin polymer + H2O
?
-
-
-
?
acetylated chitin polymer + H2O
?
increasing activity with increasing chain length
-
-
?
acetylated chitosan + H2O
?
A0A1U8QU02
-
-
-
?
acetylated chitosan + H2O
?
A0A1U8QU02
-
-
-
?
acetylated chitosan + H2O
?
A0A1U8QU02
-
-
-
?
acetylated chitosan + H2O
?
A0A1U8QU02
-
-
-
?
acetylated chitosan + H2O
?
A0A1U8QU02
-
-
-
?
acetylated chitosan + H2O
?
A0A1U8QU02
-
-
-
?
acetylated chitosan + H2O
?
-
activity with chitosan with an acetylation degree (DDA) of 40%, no activity with chitosan with DDA of 75 or 85%
-
-
?
acetylated chitosan oligosaccharide + H2O
?
-
the recombinant isolated catalytic domain displays deacetylase activity on chitooligosaccharides with a degree of polymerization (DP) larger than 3, generating mono- and di-deacetylated products with a pattern different from those of closely related fungal CDAs. On a DP5 substrate, PcCDA gave a single mono-deacetylated product in the penultimate position from the non-reducing end (ADAAA) which is then transformed into a di-deacetylated product (ADDAA). Structure-function relationships with regard to specificity and pattern of deacetylation
-
-
?
acetylated chitosan oligosaccharide + H2O
?
-
the recombinant isolated catalytic domain displays deacetylase activity on chitooligosaccharides with a degree of polymerization (DP) larger than 3, generating mono- and di-deacetylated products with a pattern different from those of closely related fungal CDAs. On a DP5 substrate, PcCDA gave a single mono-deacetylated product in the penultimate position from the non-reducing end (ADAAA) which is then transformed into a di-deacetylated product (ADDAA). Structure-function relationships with regard to specificity and pattern of deacetylation
-
-
?
acetylated chitosan oligosaccharide + H2O
?
-
-
-
?
acetylated chitosan oligosaccharide + H2O
?
analysis of deacetylation pattern of ScCDA2, MALDI-TOF-MS analysis, overview. ScCDA2 shows highest activity on colloidal chitin, followed by alpha-chitin, and then beta-chitin
-
-
?
acetylated chitosan oligosaccharide + H2O
?
-
-
-
?
acetylated chitosan oligosaccharide + H2O
?
analysis of deacetylation pattern of ScCDA2, MALDI-TOF-MS analysis, overview. ScCDA2 shows highest activity on colloidal chitin, followed by alpha-chitin, and then beta-chitin
-
-
?
acetylated chitosan polymer + H2O
?
-
-
-
?
acetylated chitosan polymer + H2O
?
-
-
-
?
acetylated chitosan polymer + H2O
?
increasing activity with increasing chain length
-
-
?
acetylated chitosan polymer + H2O
?
increasing activity with increasing degree of acetylation
-
-
?
acetylated chitosan polymer + H2O
?
increasing activity with increasing chain length
-
-
?
acetylated glucoronoxylan + H2O
?
A0A1U8QU02
-
-
-
?
acetylated glucoronoxylan + H2O
?
A0A1U8QU02
-
-
-
?
acetylated glucoronoxylan + H2O
?
A0A1U8QU02
-
-
-
?
acetylated glucoronoxylan + H2O
?
A0A1U8QU02
-
-
-
?
acetylated glucoronoxylan + H2O
?
A0A1U8QU02
-
-
-
?
acetylated glucoronoxylan + H2O
?
A0A1U8QU02
-
-
-
?
acetylated xylan + H2O
?
A0A1U8QU02
the dominating products are fully deacetylated xylooligosaccharides
-
-
?
acetylated xylan + H2O
?
A0A1U8QU02
the dominating products are fully deacetylated xylooligosaccharides
-
-
?
acetylated xylan + H2O
?
A0A1U8QU02
the dominating products are fully deacetylated xylooligosaccharides
-
-
?
acetylated xylan + H2O
?
A0A1U8QU02
the dominating products are fully deacetylated xylooligosaccharides
-
-
?
acetylated xylan + H2O
?
A0A1U8QU02
the dominating products are fully deacetylated xylooligosaccharides
-
-
?
acetylated xylan + H2O
?
A0A1U8QU02
the dominating products are fully deacetylated xylooligosaccharides
-
-
?
alpha-chitin + H2O
?
-
-
-
?
alpha-chitin + H2O
?
-
-
-
?
alpha-chitin + H2O
?
-
-
-
?
alpha-chitin + H2O
?
-
-
-
?
alpha-chitin + H2O
?
-
-
-
?
alpha-chitin + H2O
?
-
-
-
?
alpha-chitin + H2O
?
-
-
-
?
beta-chitin + H2O
?
-
-
-
?
beta-chitin + H2O
?
-
-
-
?
beta-chitin + H2O
?
-
-
-
?
beta-chitin + H2O
?
-
-
-
?
beta-chitin + H2O
?
-
-
-
?
beta-chitin + H2O
?
-
-
-
?
beta-chitin + H2O
?
-
-
-
?
chitin + H2O
?
A0A1U8QU02
-
-
-
?
chitin + H2O
?
A0A1U8QU02
-
-
-
?
chitin + H2O
?
A0A1U8QU02
-
-
-
?
chitin + H2O
?
A0A1U8QU02
-
-
-
?
chitin + H2O
?
A0A1U8QU02
-
-
-
?
chitin + H2O
?
A0A1U8QU02
-
-
-
?
chitin + H2O
?
-
enzyme exhibits high activity on fungal chitosan (78%), shrimp chitosan (83%), partially deacetylated chitin (77%), and chitohexaose (120%)
-
-
?
chitin + H2O
?
chitin oligomers are deacetylated with recombinant ScCDA2 to form partially acetylated chitosan oligosaccharides
-
-
?
chitin + H2O
?
chitin oligomers are deacetylated with recombinant ScCDA2 to form partially acetylated chitosan oligosaccharides
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
colloidal chitin
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
Absidia orchidis vel coerulea
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
colloidal chitin
-
?
chitin + H2O
chitosan + acetate
-
colloidal chitin
-
?
chitin + H2O
chitosan + acetate
-
powdered chitin, poor
-
?
chitin + H2O
chitosan + acetate
-
poor
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
colloidal chitin
-
?
chitin + H2O
chitosan + acetate
-
powdered chitin, poor
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
colloidal chitin
-
?
chitin + H2O
chitosan + acetate
Amylomyces rouxii IM-80 / CCUG 22422 / CBS 416.77 / CCM F-220 / DSM 1191 / ATCC 24905
-
-
-
?
chitin + H2O
chitosan + acetate
Amylomyces rouxii IM-80 / CCUG 22422 / CBS 416.77 / CCM F-220 / DSM 1191 / ATCC 24905
-
poor
-
?
chitin + H2O
chitosan + acetate
Amylomyces rouxii IM-80 / CCUG 22422 / CBS 416.77 / CCM F-220 / DSM 1191 / ATCC 24905
-
-
-
?
chitin + H2O
chitosan + acetate
Amylomyces rouxii IM-80 / CCUG 22422 / CBS 416.77 / CCM F-220 / DSM 1191 / ATCC 24905
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
substrate is colloidal chitin, the enzyme is an endo-chitin de-N-acetylase
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
reacetylated commercial chitosan with 52% acetylation degree is used as substrate, optimization of reaction conditions, overview
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
reacetylated commercial chitosan with 52% acetylation degree is used as substrate, optimization of reaction conditions, overview
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
amorphous chitin
-
?
chitin + H2O
chitosan + acetate
-
partially N-deacetylated water soluble chitin
-
?
chitin + H2O
chitosan + acetate
-
chitin 50
-
?
chitin + H2O
chitosan + acetate
the enzyme is an endo-chitin de-N-acetylase
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
the enzyme is an endo-chitin de-N-acetylase
-
-
?
chitin + H2O
chitosan + acetate
chitosan is necessary for cell wall integrity in Cryptococcus neoformans
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
Cunninghamella ramosa
-
-
-
-
?
chitin + H2O
chitosan + acetate
Cunninghamella ramosa URM 1918
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
19% activity compared to WSCT-50
-
-
?
chitin + H2O
chitosan + acetate
-
19% activity compared to WSCT-50
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
the enzyme is active on WSCT-50, glycol chitin, and crab chitosan (DD 71-88%) for deacetylation with a wide range of affinities (7-100%). Among them, WSCT-50 is the most accessible substrate
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
the enzyme is active on WSCT-50, glycol chitin, and crab chitosan (DD 71-88%) for deacetylation with a wide range of affinities (7-100%). Among them, WSCT-50 is the most accessible substrate
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
100% activity
-
-
?
chitin + H2O
chitosan + acetate
-
the enzyme deacetylates glycol chitin and chitin oligomers having degree of polymerization of more than four
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
100% activity
-
-
?
chitin + H2O
chitosan + acetate
-
the enzyme deacetylates glycol chitin and chitin oligomers having degree of polymerization of more than four
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
natural crystalline chitin is a very poor substrate for the enzyme
-
-
?
chitin + H2O
chitosan + acetate
-
natural crystalline chitin is a very poor substrate for the enzyme, dissolution and reprecipitation of the substrate increase the activity 5fold
-
-
?
chitin + H2O
chitosan + acetate
-
catalyzes hydrolysis of the acetamido groups of N-acetylglucosamine of chitin in fungal cell walls
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
the enzyme has high deacetylating activity on amorphous chitin from Aspergillus niger mycelium (37% deacylation) and water-soluble chitosan (33%) but low activity on shrimp crystalline chitin (3.7%)
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin + H2O
chitosan + acetate
-
-
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
chitin hexamer + H2O
?
-
-
-
?
chitin hexamer + H2O
?
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin oligomer + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitin-50 + H2O
?
-
-
-
-
?
chitooligosaccharides + H2O
?
-
-
-
r
chitooligosaccharides + H2O
?
-
active on chitooligosaccharides with at least two N-acetyl-glucosamine residues, but the activity increased with the number of N-acetyl-glucosamine residues
-
-
?
chitooligosaccharides + H2O
deacetylated chitooligosaccharides + acetate
-
-
-
?
chitooligosaccharides + H2O
deacetylated chitooligosaccharides + acetate
AnCDA is active towards chitooligosaccharides with a DP of 2 to 6
-
-
?
chitooligosaccharides + H2O
deacetylated chitooligosaccharides + acetate
-
-
-
?
chitooligosaccharides + H2O
deacetylated chitooligosaccharides + acetate
-
-
-
?
chitooligosaccharides + H2O
deacetylated chitooligosaccharides + acetate
-
-
-
?
chitooligosaccharides + H2O
deacetylated chitooligosaccharides + acetate
-
-
-
-
?
chitooligosaccharides + H2O
deacetylated chitooligosaccharides + acetate
the activity increases with the degree of acetylation. The minimal substrate is tetraacetylchitotetraose, the enzyme is not able to act on shorter substrates
-
-
?
chitooligosaccharides + H2O
deacetylated chitooligosaccharides + acetate
the activity increases with the degree of acetylation. The minimal substrate is tetraacetylchitotetraose, the enzyme is not able to act on shorter substrates
-
-
?
chitooligosaccharides + H2O
deacetylated chitooligosaccharides + acetate
Puccinia graminis f. sp. tritici race SCCL
the activity increases with the degree of acetylation. The minimal substrate is tetraacetylchitotetraose, the enzyme is not able to act on shorter substrates
-
-
?
chitooligosaccharides + H2O
deacetylated chitooligosaccharides + acetate
-
-
-
?
chitooligosaccharides + H2O
deacetylated chitooligosaccharides + acetate
-
Vibrio cholera chitin deacetylase has a broader specificity, being active on DP2 to DP6 substrates. VcCDA is 10fold more active on DP2 than DP4 substrates, and it is highly specific for deacetylation of the penultimate residue from the non-reducing end, generating monodeacetylated products with the pattern
-
-
?
chitooligosaccharides + H2O
deacetylated chitooligosaccharides + acetate
-
the enzyme from Vibrio parahaemolyticus only deacetylate DP2 and DP3 substrates
-
-
?
chitosan + H2O
?
Absidia orchidis vel coerulea
-
-
-
-
?
chitosan + H2O
?
Absidia orchidis vel coerulea NCAIM F00642
-
-
-
-
?
chitosan + H2O
deacetylated chitosan + acetate
-
-
-
?
chitosan + H2O
deacetylated chitosan + acetate
-
-
-
-
?
colloidal chitin + H2O
?
-
-
-
-
?
colloidal chitin + H2O
?
-
-
-
?
colloidal chitin + H2O
?
-
-
-
?
colloidal chitin + H2O
?
-
-
-
?
colloidal chitin + H2O
?
high activity
-
-
?
colloidal chitin + H2O
?
high activity
-
-
?
colloidal chitin + H2O
?
high activity
-
-
?
colloidal chitin + H2O
?
high activity
-
-
?
colloidal chitin + H2O
?
high activity
-
-
?
colloidal chitin + H2O
?
high activity
-
-
?
colloidal chitin + H2O
?
high activity
-
-
?
colloidal chitin + H2O
deacetylated colloidal chitin + acetate
-
-
-
?
colloidal chitin + H2O
deacetylated colloidal chitin + acetate
-
-
-
?
colloidal chitin + H2O
deacetylated colloidal chitin + acetate
-
-
-
?
colloidal chitin + H2O
deacetylated colloidal chitin + acetate
Puccinia graminis f. sp. tritici race SCCL
-
-
-
?
di-N-acetylchitobiose + H2O
?
-
35% activity compared to hepta-N-acetylchitoheptaose
-
-
?
di-N-acetylchitobiose + H2O
?
-
35% activity compared to hepta-N-acetylchitoheptaose
-
-
?
di-N-acetylchitobiose + H2O
?
-
0.6% deacetylation
-
-
?
di-N-acetylchitobiose + H2O
?
-
0.6% deacetylation
-
-
?
di-N-acetylchitobiose + H2O
?
-
marginal activity, 16.3% activity compared to glycol chitin
-
-
?
GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN + 2 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN + 2 acetate
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
acetate + ?
-
Vmax is 1.67fold higher compated to glycol-chitin
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
acetate + ?
-
time courses for hydrolysis of the N-acetyl groups are followed spectrometrically
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
acetate + ?
-
30% of the Vmax obtained with glycol-chitin
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
acetate + ?
-
time courses for hydrolysis of the N-acetyl groups are followed spectrometrically
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
glycol chitin + H2O
?
-
-
-
-
?
glycol chitin + H2O
?
-
best substrate
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
lysozyme digests of glycol chitin: poor
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
lysozyme digests of glycol chitin: poor
-
?
glycol chitin + H2O
chitosan + acetate
Amylomyces rouxii IM-80 / CCUG 22422 / CBS 416.77 / CCM F-220 / DSM 1191 / ATCC 24905
-
-
-
?
glycol chitin + H2O
chitosan + acetate
Amylomyces rouxii IM-80 / CCUG 22422 / CBS 416.77 / CCM F-220 / DSM 1191 / ATCC 24905
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
the chitin deacetylase activity from Flammulina velutipes is determined as around 13fold higher on substrate of chitosan than glycol chitin
-
-
r
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
chitosan + acetate
-
-
-
?
glycol chitin + H2O
deacetylated glycol chitin + acetate
-
-
-
?
glycol chitin + H2O
deacetylated glycol chitin + acetate
-
-
-
?
glycol chitin + H2O
deacetylated glycol chitin + acetate
-
-
-
r
glycol chitin + H2O
deacetylated glycol chitin + acetate
-
-
-
?
glycol chitin + H2O
deacetylated glycol chitin + acetate
-
-
-
?
glycol chitin + H2O
deacetylated glycol chitin + acetate
-
-
-
-
?
glycol chitin + H2O
deacetylated glycol chitin + acetate
-
-
-
?
glycol chitin + H2O
deacetylated glycol chitin + acetate
-
-
-
?
glycol chitin + H2O
deacetylated glycol chitin + acetate
Puccinia graminis f. sp. tritici race SCCL
-
-
-
?
hexa-N-acetyl-chitohexaose + H2O
chitohexaose + acetate
-
-
-
?
hexa-N-acetyl-chitohexaose + H2O
chitohexaose + acetate
-
-
-
?
hexa-N-acetyl-chitohexaose + H2O
chitohexaose + acetate
-
-
-
-
?
hexa-N-acetyl-chitohexaose + H2O
chitohexaose + acetate
-
-
-
-
?
hexa-N-acetylchitohexaose + H2O
?
-
95.3% activity compared to hepta-N-acetylchitoheptaose
-
-
?
hexa-N-acetylchitohexaose + H2O
?
-
95.3% activity compared to hepta-N-acetylchitoheptaose
-
-
?
hexa-N-acetylchitohexaose + H2O
?
-
33.2% deacetylation
-
-
?
hexa-N-acetylchitohexaose + H2O
?
-
33.2% deacetylation
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
?
-
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
?
-
39% deacetylation
-
-
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + 5 H2O
chitopentaose + 5 acetate
-
-
end product, initial products: (GlcN)3GlcNAcGlcNAc + (GlcN)4GlcNAc
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + 5 H2O
chitopentaose + 5 acetate
-
-
end product
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
?
-
-
-
-
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
?
-
-
-
-
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
?
-
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + 4 H2O
chitotetraose + 4 acetate
-
-
initial products: (GlcN)2GlcNAcGlcNAC + (GlcN)3GlcNAc, end product
?
N,N',N'',N'''-tetraacetylchitotetraose + 4 H2O
chitotetraose + 4 acetate
Amylomyces rouxii IM-80 / CCUG 22422 / CBS 416.77 / CCM F-220 / DSM 1191 / ATCC 24905
-
-
initial products: (GlcN)2GlcNAcGlcNAC + (GlcN)3GlcNAc, end product
?
N,N',N'',N'''-tetraacetylchitotetraose + 4 H2O
chitotetraose + 4 acetate
-
-
end product
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
?
-
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
?
-
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
?
-
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
?
-
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
?
-
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
?
-
22% deacetylation
-
-
?
N,N',N''-triacetylchitotriose + 2 H2O
GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc + 2 acetate
-
-
end product, initial products: GlcNGlcNAcGlcNAc + (GlcN)2GlcNAc
?
N,N',N''-triacetylchitotriose + 2 H2O
GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc + 2 acetate
Amylomyces rouxii IM-80 / CCUG 22422 / CBS 416.77 / CCM F-220 / DSM 1191 / ATCC 24905
-
-
end product, initial products: GlcNGlcNAcGlcNAc + (GlcN)2GlcNAc
?
N,N',N''-triacetylchitotriose + H2O
?
-
-
-
-
?
N,N',N''-triacetylchitotriose + H2O
?
-
poor
-
-
?
N,N',N''-triacetylchitotriose + H2O
?
-
processive, reducing-end residue remains intact
-
-
?
N,N',N''-triacetylchitotriose + H2O
?
-
poor
-
-
?
N,N',N''-triacetylchitotriose + H2O
?
Amylomyces rouxii IM-80 / CCUG 22422 / CBS 416.77 / CCM F-220 / DSM 1191 / ATCC 24905
-
processive, reducing-end residue remains intact
-
-
?
N,N',N''-triacetylchitotriose + H2O
?
-
-
-
-
?
N,N',N''-triacetylchitotriose + H2O
?
-
-
-
-
?
N,N',N''-triacetylchitotriose + H2O
?
-
high substrate concentration needed
-
-
?
N,N',N''-triacetylchitotriose + H2O
?
-
-
-
-
?
N,N',N''-triacetylchitotriose + H2O
?
-
29% deacetylation
-
-
?
N,N'-diacetylchitobiose + H2O
?
-
-
-
-
?
N,N'-diacetylchitobiose + H2O
?
-
-
-
r
N,N'-diacetylchitobiose + H2O
?
-
-
-
-
?
N,N'-diacetylchitobiose + H2O
deacetylated chitooligosaccharides + acetate
-
-
-
-
?
N,N'-diacetylchitobiose + H2O
deacetylated chitooligosaccharides + acetate
-
high substrate concentration needed
-
-
?
N,N'-diacetylchitobiose + H2O
deacetylated chitooligosaccharides + acetate
the enzyme deacetylates the non-reducing GlcNAc of N,N'-diacetylchitobiose
-
-
r
N,N'-diacetylchitobiose + H2O
deacetylated chitooligosaccharides + acetate
-
17% deacetylation
-
-
?
N-acetylglucosamine oligomer + H2O
?
-
the enzyme can deacetylate (GlcNAc)2-7. The highest enzyme activity was achieved when chitin heptamer is used as a substrate
-
-
?
N-acetylglucosamine oligomer + H2O
?
-
the enzyme can deacetylate (GlcNAc)2-7. The highest enzyme activity was achieved when chitin heptamer is used as a substrate
-
-
?
penta-N-acetyl-chitopentaose + H2O
chitopentaose + acetate
-
-
-
?
penta-N-acetyl-chitopentaose + H2O
chitopentaose + acetate
-
-
-
?
penta-N-acetyl-chitopentaose + H2O
chitopentaose + acetate
-
-
-
-
?
penta-N-acetyl-chitopentaose + H2O
chitopentaose + acetate
-
-
-
-
?
penta-N-acetylchitopentaose + H2O
?
-
75.7% activity compared to hepta-N-acetylchitoheptaose
-
-
?
penta-N-acetylchitopentaose + H2O
?
-
75.7% activity compared to hepta-N-acetylchitoheptaose
-
-
?
penta-N-acetylchitopentaose + H2O
?
-
25.8% deacetylation
-
-
?
penta-N-acetylchitopentaose + H2O
?
-
25.8% deacetylation
-
-
?
penta-N-acetylchitopentaose + H2O
?
-
highly active, 121.8% activity compared to glycol chitin
-
-
?
tetra-N-acetyl-chitotetraose + H2O
chitotetraose + acetate
-
-
-
?
tetra-N-acetyl-chitotetraose + H2O
chitotetraose + acetate
-
-
-
?
tetra-N-acetyl-chitotetraose + H2O
chitotetraose + acetate
-
-
-
-
?
tetra-N-acetyl-chitotetraose + H2O
chitotetraose + acetate
-
-
-
-
?
tetra-N-acetylchitotetraose + H2O
?
-
41.8% activity compared to hepta-N-acetylchitoheptaose
-
-
?
tetra-N-acetylchitotetraose + H2O
?
-
25.5% deacetylation
-
-
?
tetra-N-acetylchitotetraose + H2O
?
-
25.5% deacetylation
-
-
?
tri-N-acetylchitotriose + H2O
?
-
38.9% activity compared to hepta-N-acetylchitoheptaose
-
-
?
tri-N-acetylchitotriose + H2O
?
-
6.3% deacetylation
-
-
?
tri-N-acetylchitotriose + H2O
?
-
marginal activity, 25.94% activity compared to glycol chitin
-
-
?
WSCT-50 + H2O
? + acetate
-
100% activity, water-soluble chitin with degree of deacetylation 50%
-
-
?
WSCT-50 + H2O
? + acetate
-
water-soluble chitin with degree of deacetylation of 50%
-
-
?
additional information
?
-
-
chitin deacetylase is not effective on natural insoluble crystalline chitin
-
-
?
additional information
?
-
Absidia orchidis vel coerulea
-
chitin deacetylase (ChD) is the only known enzyme that catalyzes the deacetylation of the N-acetyl-D-glucosamine units (D-GlcNAc) in chitin or chitosan, releasing D-glucosamine (D-GlcN) and acetic acid (AcOH)
-
-
?
additional information
?
-
Absidia orchidis vel coerulea NCAIM F00642
-
chitin deacetylase (ChD) is the only known enzyme that catalyzes the deacetylation of the N-acetyl-D-glucosamine units (D-GlcNAc) in chitin or chitosan, releasing D-glucosamine (D-GlcN) and acetic acid (AcOH)
-
-
?
additional information
?
-
-
chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview
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additional information
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MrCDA is a specific enzyme for beta-1,4-GlcNAc polymers, such as glycol-chitin, colloidal chitin, chitosan, and chitin. IIt also deacetylates acetylxylan, but it is inactive on peptidoglycan or acetyl heparin polymers. It is active on chitooligosaccharides, and its activity increases with the degree of polymerization (DP), with triacetylchitotriose being the smallest substrate it acts on. The enzyme deacetylates its substrates following a multiple-attack mechanism, but the resulting pattern depends on the DP of the substrate: DP3, DP6, and DP7 substrates are not fully deacetylated, leaving the reducing GlcNAc unmodified, whereas DP4 and DP5 substrates are fully deacetylated. In all cases, deacetylation starts at the non-reducing end residue, and then proceeds to the neighboring monomer towards the reducing end
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. ArCE4 is active on alpha- and beta-chitin, chitosan (DA 64%), and acetylxylan. On COS substrates, activity increases with increasing DP, with higher activity against DP5 compared to DP6, and no activity on GlcNAc. The enzyme acts by a multiple-chain mechanism, as shown with DP5 substrate, where different mono- and di-deacetylated products are obtained. The first deacelylation happens at all three internal positions, whereas di-deacetylation mainly occurs at the GlcNAc unit next to the reducing end, and at either of the two other internal units (ADDAA and ADADA). Although other minor products are formed, it seems that the reducing end unit is not deacetylated
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additional information
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CDA catalyzes the deacetylation of monomeric acetyl glucosamine residues of chitin by multiple attack mechanism
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additional information
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CDA catalyzes the deacetylation of monomeric acetyl glucosamine residues of chitin by multiple attack mechanism
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additional information
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CDA catalyzes the deacetylation of monomeric acetyl glucosamine residues of chitin by multiple attack mechanism
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin, the Aspergillus nidulans chitin deacetylase is inactive on colloidal chitin and carboxymethyl chitin at lower rates, and it is inactive on GlcNAc, acrylamide, bisacrylamide, albumin, and casein
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additional information
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A0A1U8QU02
enzyme AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and cetylxylan, but not on peptidoglycan. AnCDA catalyses mono-deacetylation of (GlcNAc)2 and full deacetylation of (GlcNAc)3-6 in a non-processive manner. Deacetylation of the reducing end sugar is much slower than deacetylation of the other sugars in chito-oligomers. AnCDA shows no activity on peptidoglycan, but the enzyme is active on oligomeric acetylxylan and acetylated glucuronoxylan, as well as on chitosan with an initial fraction of acetylated residues. AnCDA is active on insoluble chitin. Substrate specificity and MALDI-ToF-mass spectrometric product analysis, overview
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additional information
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substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. No activity on peptidoglycan. The enzyme is inactive towards GlcNAc, and catalyzes the mono-deacetylation of (GlcNAc)2. The deacetylation rate exhibits a counter-intuitive relationship with the length of the chitooligosaccharide substrates: odd-numbered chitooligosaccharides (DP5, DP3) have higher apparent rate constants than even-numbered oligomers (DP4, DP2). Monitoring of products formation with the DP6 substrate showed that the first deacetylation event occurs at random positions, except for the reducing end, which reacts much more slowly to yield the fully deacetylated product
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additional information
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A0A1U8QU02
enzyme AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and cetylxylan, but not on peptidoglycan. AnCDA catalyses mono-deacetylation of (GlcNAc)2 and full deacetylation of (GlcNAc)3-6 in a non-processive manner. Deacetylation of the reducing end sugar is much slower than deacetylation of the other sugars in chito-oligomers. AnCDA shows no activity on peptidoglycan, but the enzyme is active on oligomeric acetylxylan and acetylated glucuronoxylan, as well as on chitosan with an initial fraction of acetylated residues. AnCDA is active on insoluble chitin. Substrate specificity and MALDI-ToF-mass spectrometric product analysis, overview
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additional information
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A0A1U8QU02
enzyme AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and cetylxylan, but not on peptidoglycan. AnCDA catalyses mono-deacetylation of (GlcNAc)2 and full deacetylation of (GlcNAc)3-6 in a non-processive manner. Deacetylation of the reducing end sugar is much slower than deacetylation of the other sugars in chito-oligomers. AnCDA shows no activity on peptidoglycan, but the enzyme is active on oligomeric acetylxylan and acetylated glucuronoxylan, as well as on chitosan with an initial fraction of acetylated residues. AnCDA is active on insoluble chitin. Substrate specificity and MALDI-ToF-mass spectrometric product analysis, overview
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additional information
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A0A1U8QU02
enzyme AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and cetylxylan, but not on peptidoglycan. AnCDA catalyses mono-deacetylation of (GlcNAc)2 and full deacetylation of (GlcNAc)3-6 in a non-processive manner. Deacetylation of the reducing end sugar is much slower than deacetylation of the other sugars in chito-oligomers. AnCDA shows no activity on peptidoglycan, but the enzyme is active on oligomeric acetylxylan and acetylated glucuronoxylan, as well as on chitosan with an initial fraction of acetylated residues. AnCDA is active on insoluble chitin. Substrate specificity and MALDI-ToF-mass spectrometric product analysis, overview
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additional information
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enzyme AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and cetylxylan, but not on peptidoglycan. AnCDA catalyses mono-deacetylation of (GlcNAc)2 and full deacetylation of (GlcNAc)3-6 in a non-processive manner. Deacetylation of the reducing end sugar is much slower than deacetylation of the other sugars in chito-oligomers. AnCDA shows no activity on peptidoglycan, but the enzyme is active on oligomeric acetylxylan and acetylated glucuronoxylan, as well as on chitosan with an initial fraction of acetylated residues. AnCDA is active on insoluble chitin. Substrate specificity and MALDI-ToF-mass spectrometric product analysis, overview
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additional information
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A0A1U8QU02
enzyme AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and cetylxylan, but not on peptidoglycan. AnCDA catalyses mono-deacetylation of (GlcNAc)2 and full deacetylation of (GlcNAc)3-6 in a non-processive manner. Deacetylation of the reducing end sugar is much slower than deacetylation of the other sugars in chito-oligomers. AnCDA shows no activity on peptidoglycan, but the enzyme is active on oligomeric acetylxylan and acetylated glucuronoxylan, as well as on chitosan with an initial fraction of acetylated residues. AnCDA is active on insoluble chitin. Substrate specificity and MALDI-ToF-mass spectrometric product analysis, overview
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additional information
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A0A1U8QU02
enzyme AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and cetylxylan, but not on peptidoglycan. AnCDA catalyses mono-deacetylation of (GlcNAc)2 and full deacetylation of (GlcNAc)3-6 in a non-processive manner. Deacetylation of the reducing end sugar is much slower than deacetylation of the other sugars in chito-oligomers. AnCDA shows no activity on peptidoglycan, but the enzyme is active on oligomeric acetylxylan and acetylated glucuronoxylan, as well as on chitosan with an initial fraction of acetylated residues. AnCDA is active on insoluble chitin. Substrate specificity and MALDI-ToF-mass spectrometric product analysis, overview
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disruption of pdaA does not affect vegetative growth and sporulation but affects spore germination. When L-alanine is added into the spore suspension, the spores of the pdaA disruption mutant shows a slow and partial reduction in absorbance at OD600 and becomes phase pale gray compared with phase dark of the wild-type strain. In contrast with the outgrowing of wild-type spores after gernination, the pdaA mutant spores are blocked at the stage of spore germination
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the enzyme catalyses the hydrolysis of the acetamido group in the N-acetylglucosamine units of chitin and chitosan, generating glucosamine units and acetic acid
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the enzyme catalyses the hydrolysis of the acetamido group in the N-acetylglucosamine units of chitin and chitosan, generating glucosamine units and acetic acid
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no activity with peritrophic matrix chitin by isozyme BmCDA6
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additional information
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no activity with peritrophic matrix chitin by isozyme BmCDA6
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additional information
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no activity with peritrophic matrix chitin by isozyme BmCDA6
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additional information
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no activity with peritrophic matrix chitin by isozyme BmCDA6
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additional information
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binding study of an N-acetylglucosaminyl trimer to the enzyme, computational docking
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additional information
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binding study of an N-acetylglucosaminyl trimer to the enzyme, computational docking
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additional information
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substrate specificity, overview, no activity with chitotriose
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additional information
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substrate specificity, overview, no activity with chitotriose
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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the recombinant enzyme deacetylates the complex oligosaccharide substrates with various acetyls produced by endo-chitosanase from Aspergillus fumigatus hydrolyzing chitosan. Substrate and product identification by mass spectrometric analysis, overview. (GlcNAc)4 is fully deacetylated into (GlcN)4, and the enzyme deacetylates (GlcNAc)4 and (GlcNAc)5 much faster than (GlcNAc)3 and (GlcNAc)2. Chitotriose is also fully deacetylated through a random deacetylation process, while chitobiose (GlcNAc)2, is only deacetylated at the non-reducing GlcNAc residue. The enzyme exclusively produces Glc-NGlcNAc, and cannot deacetylate GlcNAc
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additional information
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substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. The enzyme from Colletotrichum lindemuthianum is able to fully deacetylate chitooligosaccharides with a DP equal to or greater than 3, while it only deacetylates the non-reducing GlcNAc of N,N'-diacetylchitobiose. This enzyme is reversible, as it is also able to catalyze the acetylation of chitosan oligomers
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additional information
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binding study of an N-acetylglucosaminyl trimer to the enzyme, computational docking
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additional information
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substrate specificity, overview, no activity with chitotriose
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additional information
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substrate specificity, overview, no activity with chitotriose
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additional information
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Cda1 preferably deacetylates the nonreducing end residue of (GlcNAc)2, the internal or nonreducing end residue of (GlcNAc)3 and the nonreducing residue of (GlcNAc)6 after deacetylating the internal residues. Cda1 prefers chitohexaose with higher degrees of acetylation for deacetylation. Pathway of chitin deacetylation. Comparison of isozymes Cda1 and Cda2, overview. No activity of Cda1 with colloidal chitin, chitin powder, and N-acetylglucosamine
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additional information
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Cda2 preferably deacetylates the reducing end residue of (GlcNAc)2, the internal or reducing end residue of (GlcNAc)3 and the reducing residue of (GlcNAc)6 after deacetylating the internal residues. Cda2 shows a weaker preference for chitohexaose with varying degrees of acetylation. Pathway of chitin deacetylation. #Comparison of isozymes Cda1 and Cda2, overview. No activity of Cda2 with colloidal chitin, chitin powder, and N-acetylglucosamine
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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the enzyme has a function in assembly of intraluminal chitinous filament, septate-junction-dependent luminal deposition of the enzyme restricts tube elongation in the trachea, tubular function is critically dependent on the length and diameter of their constituting branches in tubular organs such as kidney, products of genes verm and serp are required, molecular mechanisms, overview
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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the recombinant FV-PDA catalyses deacetylation of N-acetyl-chitooligomers, from dimer to pentamer, glycol chitin and colloidal chitin
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additional information
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the recombinant FV-PDA catalyses deacetylation of N-acetyl-chitooligomers, from dimer to pentamer, glycol chitin and colloidal chitin
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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GlcNAc, colloidal chitin, regenerated chitin, beta-chitin and crystal crab chitins with different particle size are not deacetylated by the crude enzyme
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additional information
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GlcNAc, colloidal chitin, regenerated chitin, beta-chitin and crystal crab chitins with different particle size are not deacetylated by the crude enzyme
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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no activity with GlcNAc
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additional information
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no activity with GlcNAc
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additional information
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the enzyme is not able to deacetylate N-acetyl glucosamine
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additional information
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no activity with N-acetyl glucosamine, marginal activity towards (GlcNAc)2 and (GlcNAc)3
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additional information
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the enzyme is not able to deacetylate N-acetyl glucosamine
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additional information
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no activity with N-acetyl glucosamine, marginal activity towards (GlcNAc)2 and (GlcNAc)3
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additional information
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PesCDA modifies chitin oligomers, the products are partially deacetylated chitosan oligomers with a specific acetylation pattern: GlcNAc-GlcNAc-(GlcN)n-GlcNAc (n > 1). Substrate specificity with activity against chitosan polymers that have degrees of acetylation of 10-60% as well as against colloidal chitin, alpha-chitin and beta-chitin, overview
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additional information
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PesCDA modifies chitin oligomers, the products are partially deacetylated chitosan oligomers with a specific acetylation pattern: GlcNAc-GlcNAc-(GlcN)n-GlcNAc (n > 1). Substrate specificity with activity against chitosan polymers that have degrees of acetylation of 10-60% as well as against colloidal chitin, alpha-chitin and beta-chitin, overview
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additional information
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substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. PesCDA acts better on colloidal chitin as substrate, but it is also active on chitosans with a degree of acetylation (DA) of 10-60% (higher activity with a higher DA), as well as on chitooligosaccharides. It is not able to deacetylate crystalline chitin, neither alpha- or beta-allomorphs. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms
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additional information
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substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. PcCDA deacetylates chitooligosaccharides, requiring at least four GlcNAc units in order to be active, but it prefers longer substrates. For DP4 and DP5 substrates, it first deacetylates the penultimate residue from the non-reducing end, and continues to the next residue towards the reducing end, with a pattern of acetylation
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additional information
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substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. PcCDA deacetylates chitooligosaccharides, requiring at least four GlcNAc units in order to be active, but it prefers longer substrates. For DP4 and DP5 substrates, it first deacetylates the penultimate residue from the non-reducing end, and continues to the next residue towards the reducing end, with a pattern of acetylation
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additional information
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analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing
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additional information
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analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing
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additional information
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substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. The enzyme is active on soluble glycol-chitin, chitosan polymers with a high DA, and chitooligosaccharides, and shows low activity on insoluble alpha- and beta-chitin, which is reduced further by deletion of the CBM domains. On chitooligosaccharides, it is active against oligomers with a DP >2, leading to fully deacetylated products. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms. The mode of action of Podospora anserina CDA on DP3 and DP4 substrates reveals that it follows a multiple-chain mechanism. With the trimer, all possible isomers are found for both mono- and di-deacetylated intermediate products, although the first deacetylation event has a clear preference for the reducing end. This is not the case for the tetramer and pentamer substrates, where the residue next to the reducing end is preferentially deacetylated first, with the second deacetylation occurring mainly next to the existing GlcNH2 unit on either side. Overall, larger oligomers are deacetylated faster, with deacetylation of the reducing end occurring as a late event
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additional information
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analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing
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additional information
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analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing
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additional information
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analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing
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additional information
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analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing
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additional information
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mass spectrometric sequencing of the products obtained by enzymatic deacetylation of chitin oligomers, i.e. tetramers to hexamers, revealing that PgtCDA generates paCOS with specific acetylation patterns of A-A-D-D, A-A-D-D-D, and A-A-D-D-D-D, respectively (A = GlcNAc, D = GlcN), indicating that PgtCDA cannot deacetylate the two GlcNAc units closest to the oligomer's nonreducing end. Detailed product analysis, detection method, overview. Pronounced regioselectivity of the enzyme
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additional information
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mass spectrometric sequencing of the products obtained by enzymatic deacetylation of chitin oligomers, i.e. tetramers to hexamers, revealing that PgtCDA generates paCOS with specific acetylation patterns of A-A-D-D, A-A-D-D-D, and A-A-D-D-D-D, respectively (A = GlcNAc, D = GlcN), indicating that PgtCDA cannot deacetylate the two GlcNAc units closest to the oligomer's nonreducing end. Detailed product analysis, detection method, overview. Pronounced regioselectivity of the enzyme
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additional information
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substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms. The enzyme from Puccinia graminis is not active on insoluble polymers such as alpha- or beta-chitin. The sequence of the products obtained by enzymatic deacetylation of tetramers to hexamers reveals that the enzyme specifically deacetylates all but the last two GlcNAc units on the non-reducing end via a multiple-chain mechanism
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additional information
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substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms. The enzyme from Puccinia graminis is not active on insoluble polymers such as alpha- or beta-chitin. The sequence of the products obtained by enzymatic deacetylation of tetramers to hexamers reveals that the enzyme specifically deacetylates all but the last two GlcNAc units on the non-reducing end via a multiple-chain mechanism
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additional information
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Puccinia graminis f. sp. tritici race SCCL
substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms. The enzyme from Puccinia graminis is not active on insoluble polymers such as alpha- or beta-chitin. The sequence of the products obtained by enzymatic deacetylation of tetramers to hexamers reveals that the enzyme specifically deacetylates all but the last two GlcNAc units on the non-reducing end via a multiple-chain mechanism
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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ScCDA2 can hydrolyze N-acetamido groups rather than the reducing ends of chitin oligosaccharides, producing fully defined chitosan oligosaccharides by a multiple attack mode of action. Furthermore, ScCDA2 is able to remove about 8% and 20% of the acetyl groups from crystalline chitin and colloidal chitin. Partially acetylated chitosan oligosaccharides (COS) consist of N-acetylglucosamine (GlcNAc) and glucosamine (GlcN) residues. Enzyme ScCDA2 produces COS with specific acetylation patterns of DAAA, ADAA, AADA, DDAA, DADA, ADDA and DDDA, respectively. ScCDA2 does not deacetylate the GlcNAc unit that is closest to the reducing end of the oligomer furthermore ScCDA2 has a multiple-attack deacetylation mechanism on chitin oligosaccharides. ScCDA2 also exhibits about 8% and 20% deacetylation activity on crystalline chitin and colloid chitin, respectively. ScCDA2 has a multiple-attack deacetylation mechanism on chitin oligosaccharides
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additional information
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ScCDA2 can hydrolyze N-acetamido groups rather than the reducing ends of chitin oligosaccharides, producing fully defined chitosan oligosaccharides by a multiple attack mode of action. Furthermore, ScCDA2 is able to remove about 8% and 20% of the acetyl groups from crystalline chitin and colloidal chitin. Partially acetylated chitosan oligosaccharides (COS) consist of N-acetylglucosamine (GlcNAc) and glucosamine (GlcN) residues. Enzyme ScCDA2 produces COS with specific acetylation patterns of DAAA, ADAA, AADA, DDAA, DADA, ADDA and DDDA, respectively. ScCDA2 does not deacetylate the GlcNAc unit that is closest to the reducing end of the oligomer furthermore ScCDA2 has a multiple-attack deacetylation mechanism on chitin oligosaccharides. ScCDA2 also exhibits about 8% and 20% deacetylation activity on crystalline chitin and colloid chitin, respectively. ScCDA2 has a multiple-attack deacetylation mechanism on chitin oligosaccharides
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additional information
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ScCDA2 can hydrolyze N-acetamido groups rather than the reducing ends of chitin oligosaccharides, producing fully defined chitosan oligosaccharides by a multiple attack mode of action. Furthermore, ScCDA2 is able to remove about 8% and 20% of the acetyl groups from crystalline chitin and colloidal chitin. Partially acetylated chitosan oligosaccharides (COS) consist of N-acetylglucosamine (GlcNAc) and glucosamine (GlcN) residues. Enzyme ScCDA2 produces COS with specific acetylation patterns of DAAA, ADAA, AADA, DDAA, DADA, ADDA and DDDA, respectively. ScCDA2 does not deacetylate the GlcNAc unit that is closest to the reducing end of the oligomer furthermore ScCDA2 has a multiple-attack deacetylation mechanism on chitin oligosaccharides. ScCDA2 also exhibits about 8% and 20% deacetylation activity on crystalline chitin and colloid chitin, respectively. ScCDA2 has a multiple-attack deacetylation mechanism on chitin oligosaccharides
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additional information
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chitin deacetylase is required for proper spore formation in Schizosaccharomyces pombe
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additional information
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chitin deacetylase is required for proper spore formation in Schizosaccharomyces pombe
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additional information
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Cda1 interacts with itself
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additional information
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Cda1 interacts with itself
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. NodB is active on chitooligosaccharides from DP2 to DP5 with no differences in kcat, but Km decreases with increasing DP. Specifically, kcat/KM is 5fold higher for DP5 than for DP2 substrates. DP4 or DP5 substrates are the natural substrates depending on the rhizobial strain. NodB only deacetylates the non-reducing end residue, but traces of a second deacetylation event are seen upon long incubations
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additional information
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the reaction mechanism governs the regioselectivity
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additional information
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the reaction mechanism governs the regioselectivity
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview
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additional information
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chitin deacetylase is not effective on natural insoluble crystalline chitin
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additional information
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substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview
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evolution
CDA belongs to the carbohydrate esterase family 4 (CE4) according to the classification of the CAZY database
evolution
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chitin deacetylases belong to family 4 of carbohydrate esterases. All CE4 enzymes share the NodB homologous domain, with a distorted (beta/alpha)8 barrel structure17 that contains the catalytic active site
evolution
A0A1U8QU02
chitin deacetylases belong to the family 4 of carbohydrate esterases (CE4)
evolution
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comparison of isozymes Cda1 and Cda2, sequence and structure comparison. The predicted Cda1 structure shows more hydrophobic aromatic amino acids on the surface near subsite +1 in the active site than on the surface near subsite -1, whereas the predicted Cda2 structure has more hydrophobic aromatic amino acids on the surface near subsite -1 than on the surface near subsite +1, which may be the molecular basis of the distinctive catalytic features between Cda1 and Cda2. Notably, Cda1 has a high transcription level in the nonelongating basal stipe region, whereas Cda2 has a high transcription level in the elongating apical stipe region, and the transcription level of the former is approximately five times that of the latter. Correspondingly, the molar ratio of GlcN/GlcNAc increased from 0.15 in the cell wall of the apical stipe region to 0.22 in the cell wall of the basal stipe region. Different modes of action of Cda1 and Cda2 may be related to their functions in the different stipe regions. Mode of action of Cda1 and Cda2 with chitin oligomers, overview
evolution
evolutionary relationships, phylogenetic analysis
evolution
sequence comparisons to CDAs from Tribolium castaneum, Bombyx mori, Drosophila melanogaster, Anopheles gambiae, Oxya chinensis, and Choristoneura funiferana
evolution
the CDA from Podospora anserina (PaCDA) is closely related to Colletotrichum lindemuthianum CDA in the catalytic domain, but unique in having two chitin-binding domains. The catalytic domain of PaCDA is also functionally similar to Colletotrichum lindemuthianum CDA, though differing in detail
evolution
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the CdaYJ is homologous to some known chitin deacetylases and contains conserved chitin deacetylase active sites. CdaYJ protein exhibits a long N-terminal and a relative short C-terminal. Phylogenetic analysis reveals that CdaYJ shows highest homology to CDAs from Alphaproteobacteria. Construction of metagenomic library of the Arctic deep-sea sediments, phylogenetic analysis of CdaYJ
evolution
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the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms
evolution
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the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms
evolution
the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms
evolution
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the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms
evolution
the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms
evolution
the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms
evolution
the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms
evolution
the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms
evolution
the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms
evolution
the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms
evolution
the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms
evolution
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chitin deacetylases belong to the family 4 of carbohydrate esterases (CE4)
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evolution
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chitin deacetylases belong to the family 4 of carbohydrate esterases (CE4)
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evolution
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chitin deacetylases belong to the family 4 of carbohydrate esterases (CE4)
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evolution
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the CDA from Podospora anserina (PaCDA) is closely related to Colletotrichum lindemuthianum CDA in the catalytic domain, but unique in having two chitin-binding domains. The catalytic domain of PaCDA is also functionally similar to Colletotrichum lindemuthianum CDA, though differing in detail
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evolution
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the CDA from Podospora anserina (PaCDA) is closely related to Colletotrichum lindemuthianum CDA in the catalytic domain, but unique in having two chitin-binding domains. The catalytic domain of PaCDA is also functionally similar to Colletotrichum lindemuthianum CDA, though differing in detail
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evolution
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the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms
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evolution
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chitin deacetylases belong to family 4 of carbohydrate esterases. All CE4 enzymes share the NodB homologous domain, with a distorted (beta/alpha)8 barrel structure17 that contains the catalytic active site
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evolution
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CDA belongs to the carbohydrate esterase family 4 (CE4) according to the classification of the CAZY database
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evolution
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chitin deacetylases belong to the family 4 of carbohydrate esterases (CE4)
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evolution
Puccinia graminis f. sp. tritici race SCCL
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the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms
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evolution
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the CDA from Podospora anserina (PaCDA) is closely related to Colletotrichum lindemuthianum CDA in the catalytic domain, but unique in having two chitin-binding domains. The catalytic domain of PaCDA is also functionally similar to Colletotrichum lindemuthianum CDA, though differing in detail
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evolution
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chitin deacetylases belong to the family 4 of carbohydrate esterases (CE4)
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evolution
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the CDA from Podospora anserina (PaCDA) is closely related to Colletotrichum lindemuthianum CDA in the catalytic domain, but unique in having two chitin-binding domains. The catalytic domain of PaCDA is also functionally similar to Colletotrichum lindemuthianum CDA, though differing in detail
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evolution
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the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms
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malfunction
enzyme silencing results in abnormal molting phenotypes
malfunction
analysis of LmCDA5a knockout mutant phenotype, overview. Silencing of LmCDA5a does not affect the chitin content and organization
malfunction
analysis of LmCDA5a knockout mutant phenotype, overview. Silencing of LmCDA5b does not affect the chitin content and organization
malfunction
LmCDA2-deficient cuticle is less compact suggesting that LmCDA2 is needed for chitin packaging. Animals with reduced LmCDA2 activity die at molting, underlining that correct chitin organization is essential for survival
malfunction
silencing of LmCDA4 does not affect the chitin content and organization
metabolism
CDA is a key enzyme involved in the chitin metabolism
metabolism
model for plant cell recognition of fungi containing chitin in their cell walls and hypothetical fungal strategy to overcome recognition by the plant immune system. Chitin in the fungal cell wall, consisting of N-acetyl-D-glucosamine units, is degraded by plant chitinases
physiological function
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chitin deacetylase is required for proper spore formation
physiological function
-
the enzyme is associated with cell wall synthesis
physiological function
the strong expression of CfCDA2 in the epidermis of molting individuals points to an important role of this gene in the molting process of Choristoneura fumiferana
physiological function
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chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases
physiological function
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chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases
physiological function
chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases
physiological function
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chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases
physiological function
chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases
physiological function
chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases
physiological function
chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases
physiological function
chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases
physiological function
chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases
physiological function
chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases. Enzyme AnCDA is secreted into the extracellular medium to deacetylate the chitin oligomers produced by chitinases during cell autolysis
physiological function
chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases. NodB deacetylases are involved in the biosynthesis of Nod factors, the morphogenic signal molecules produced by rhizobia, which initiate the development of root nodules in leguminous plants
physiological function
chitin deacetylase converts chitin into chitosan, the N-deacetylated form of chitin, which influences the mechanical and permeability properties of structures such as the cuticle and peritrophic matrices
physiological function
in fungi, the key enzymes that convert chitin to chitosan are chitin deacetylases (CDA). Chitin deacetylase from the endophytic fungus Pestalotiopsis sp. efficiently inactivates the elicitor activity of chitin oligomers in rice cells. A bioactivity assay where suspension-cultured rice cells are incubated with the PesCDA products (processed chitin hexamers), chitosan oligomer products no longer elicit the plant immune system, unlike the substrate hexamers. The endophytic enzyme can prevent the endophyte from being recognized by the plant immune system
physiological function
LmCDA2-mediated chitin deacetylation at the beginning of chitin production is a decisive reaction that triggers helicoidal arrangement of subsequently assembled chitin-protein microfibrils. In the body cuticle of nymphs of the migratory locust Locusta migratoria, helicoidal chitin organization is changed to an organization with unidirectional microfibril orientation. The enzyme is involved in cuticle organization. LmCDA2 is needed for tracheal cuticle formation and feeding, and LmCDA2 is required for locust molting and development
physiological function
proposed function of the enzyme in conversion of the insoluble substrate colloidal chitin
physiological function
the CDA enzyme plays a significant role only during the growth phase of the fungus
physiological function
the enzyme is involved in the molting process of Locusta migratoria
physiological function
the enzyme is invovled in the molting process of Locusta migratoria
physiological function
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the enzyme might have a role in pathogenicity
physiological function
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proposed function of the enzyme in conversion of the insoluble substrate colloidal chitin
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physiological function
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proposed function of the enzyme in conversion of the insoluble substrate colloidal chitin
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physiological function
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chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases
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physiological function
-
the enzyme might have a role in pathogenicity
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physiological function
Puccinia graminis f. sp. tritici race SCCL
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chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases
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physiological function
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proposed function of the enzyme in conversion of the insoluble substrate colloidal chitin
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physiological function
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proposed function of the enzyme in conversion of the insoluble substrate colloidal chitin
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physiological function
-
chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases
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physiological function
-
the CDA enzyme plays a significant role only during the growth phase of the fungus
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additional information
the enzyme sequence has a 16 amino acid residue signal peptide, a putative polysaccharide deacetylase-like domain (residues 46-182), and 15 cysteine residues present in three clusters, residues 24-83, 183-243, and 332-365, structure comparison, overview
additional information
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the enzyme sequence has a 16 amino acid residue signal peptide, a putative polysaccharide deacetylase-like domain (residues 46-182), and 15 cysteine residues present in three clusters, residues 24-83, 183-243, and 332-365, structure comparison, overview
additional information
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the enzyme structure shows presence of 56.26% alpha-helical and 15.63% beta-helical structures, structure comparison, overview
additional information
the isoforms differ only in the alternatively spliced region, representing 43 and 37 amino acid residues in isoforms A and B, respectively
additional information
the isoforms differ only in the alternatively spliced region, representing 43 and 37 amino acid residues in isoforms A and B, respectively
additional information
-
the isoforms differ only in the alternatively spliced region, representing 43 and 37 amino acid residues in isoforms A and B, respectively
additional information
Absidia orchidis vel coerulea
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chitin deacetylase is the only known enzyme that can deacetylate the N-acetyl-D-glucosamine units in chitin and chitosan to D-glucosamine
additional information
A0A1U8QU02
His-His-Asp catalytic triad
additional information
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identification and characterization of a chitin deacetylase from a metagenomic library of deep-sea sediments of the arctic ocean, genotyping
additional information
mode of action on chitin, overview
additional information
-
mode of action on chitin, overview
additional information
molecular structure-function relationships, three-dimensional modeling. Bioinformatic analysis of the chitin deacetylase PgtCDA gene
additional information
-
molecular structure-function relationships, three-dimensional modeling. Bioinformatic analysis of the chitin deacetylase PgtCDA gene
additional information
ScCDA2 has a multiple-attack deacetylation mechanism on chitin oligosaccharides, acetylation patterns, overview. Active site residues are Asp102 and His250. Homology modeling and substrate binding specificity of ScCDA2 using crystal structures (PDB ID: 5LFZ, 2CC0 and 2C1G) as templates. The docking results show that chitin lies in the substrate-binding pocket which is surrounded by six loops, His250, Asp102, Asp103, His149 and His153. Asp103, His149 and His153 form a coordinate bond with Zn2+, and the metal ion serves as a Lewis acid to assist the water affinity attack on the carbon atom on the amide bond. The adjacent His250 and Asp102 play a catalytic role through protonation, and the common action of these amino acids leads to the cleaving of the acetyl group
additional information
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ScCDA2 has a multiple-attack deacetylation mechanism on chitin oligosaccharides, acetylation patterns, overview. Active site residues are Asp102 and His250. Homology modeling and substrate binding specificity of ScCDA2 using crystal structures (PDB ID: 5LFZ, 2CC0 and 2C1G) as templates. The docking results show that chitin lies in the substrate-binding pocket which is surrounded by six loops, His250, Asp102, Asp103, His149 and His153. Asp103, His149 and His153 form a coordinate bond with Zn2+, and the metal ion serves as a Lewis acid to assist the water affinity attack on the carbon atom on the amide bond. The adjacent His250 and Asp102 play a catalytic role through protonation, and the common action of these amino acids leads to the cleaving of the acetyl group
additional information
the chitin deacetylase from Colletotrichum lindemuthianum follows the multiple-chain mechanism, in which the enzyme forms an active enzyme-polymer complex, and catalyzes the hydrolysis of only one acetyl group before it dissociates and forms a new active complex
additional information
the chitin deacetylase from Mucor rouxii follows the multiple-attack mechanism, in which binding of the enzyme to the polysaccharide chain is followed by a number of sequential deacetylations, after which the enzyme binds to another chain
additional information
the chitin deacetylase from Rhizobium follows the single-chain mechanism, which refers to processive enzymes in which a number of catalytic events occur on a single substrate molecule, leading to sequential deacetylation
additional information
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the chitin deacetylase from Vibrio follows the single-chain mechanism, which refers to processive enzymes in which a number of catalytic events occur on a single substrate molecule, leading to sequential deacetylation
additional information
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the chitin deacetylase from Vibrio follows the single-chain mechanism, which refers to processive enzymes in which a number of catalytic events occur on a single substrate molecule, leading to sequential deacetylation
additional information
the enzyme from Pestalotiopsis sp. follows a multiple-chain mechanism in which all residues are deacetylated, except the reducing end, and the last two GlcNAc residues from the non-reducing end, with a pattern of deacetylation
additional information
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the extracellular CE4 deacetylase has two CBM18 chitin binding modules, molecular modelling of the PcCDA catalytic domain and ligand docking using 2IW0 and 2Y8U as templates, overview. Structure-function relationships with regard to specificity and pattern of deacetylation. The catalytic domain (CE4 domain, residues 107 to 303) is flanked by two (N- and C-terminal) CBM18 modules (residues 30 to 74 and 360 to 441, respectively). These family 18 carbohydrate binding modules are typically involved in chitin binding. PcCDA full-length protein includes 25 cysteine residues, of which only two are located in the CE4 catalytic domain
additional information
Absidia orchidis vel coerulea NCAIM F00642
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chitin deacetylase is the only known enzyme that can deacetylate the N-acetyl-D-glucosamine units in chitin and chitosan to D-glucosamine
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additional information
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His-His-Asp catalytic triad
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additional information
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His-His-Asp catalytic triad
-
additional information
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His-His-Asp catalytic triad
-
additional information
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mode of action on chitin, overview
-
additional information
-
mode of action on chitin, overview
-
additional information
-
the extracellular CE4 deacetylase has two CBM18 chitin binding modules, molecular modelling of the PcCDA catalytic domain and ligand docking using 2IW0 and 2Y8U as templates, overview. Structure-function relationships with regard to specificity and pattern of deacetylation. The catalytic domain (CE4 domain, residues 107 to 303) is flanked by two (N- and C-terminal) CBM18 modules (residues 30 to 74 and 360 to 441, respectively). These family 18 carbohydrate binding modules are typically involved in chitin binding. PcCDA full-length protein includes 25 cysteine residues, of which only two are located in the CE4 catalytic domain
-
additional information
-
ScCDA2 has a multiple-attack deacetylation mechanism on chitin oligosaccharides, acetylation patterns, overview. Active site residues are Asp102 and His250. Homology modeling and substrate binding specificity of ScCDA2 using crystal structures (PDB ID: 5LFZ, 2CC0 and 2C1G) as templates. The docking results show that chitin lies in the substrate-binding pocket which is surrounded by six loops, His250, Asp102, Asp103, His149 and His153. Asp103, His149 and His153 form a coordinate bond with Zn2+, and the metal ion serves as a Lewis acid to assist the water affinity attack on the carbon atom on the amide bond. The adjacent His250 and Asp102 play a catalytic role through protonation, and the common action of these amino acids leads to the cleaving of the acetyl group
-
additional information
-
His-His-Asp catalytic triad
-
additional information
-
mode of action on chitin, overview
-
additional information
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His-His-Asp catalytic triad
-
additional information
-
mode of action on chitin, overview
-
additional information
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the enzyme structure shows presence of 56.26% alpha-helical and 15.63% beta-helical structures, structure comparison, overview
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Rhizopus arrhizus
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Scopulariopsis brevicaulis
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Scopulariopsis brevicaulis
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Rhizopus stolonifer (Q32XH4)
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Rhizopus circinans
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Chitin deacetylases: properties and applications
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Absidia orchidis vel coerulea
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Expression studies of Bacillus licheniformis chitin deacetylase in E. coli Rosetta cells
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Bacillus licheniformis
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Yu, R.; Liu, W.; Li, D.; Zhao, X.; Ding, G.; Zhang, M.; Ma, E.; Zhu, K.; Li, S.; Moussian, B.; Zhang, J.
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Locusta migratoria (A0A2R2PTF2), Locusta migratoria (A0A2R2PTF4), Locusta migratoria
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Absidia orchidis vel coerulea, Absidia orchidis vel coerulea NCAIM F00642
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Han, G.; Li, X.; Zhang, T.; Zhu, X.; Li, J.
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Helicoverpa armigera (A0A0A7R7B5), Helicoverpa armigera
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Zhu, X.Y.; Zhao, Y.; Zhang, H.D.; Wang, W.X.; Cong, H.H.; Yin, H.
Characterization of the specific mode of action of a chitin deacetylase and separation of the partially acetylated chitosan oligosaccharides
Mar. Drugs
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Saccharomyces cerevisiae (Q06703), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q06703)
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Narayanan, K.; Parameswaran, B.; Pandey, A.
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Aspergillus flavus (A0A3M7JTD4), Aspergillus flavus, Aspergillus flavus P6B2 (A0A3M7JTD4)
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Zhao, P.; Zhang, X.; Liu, X.; Zhao, X.; Yu, R.; Dong, W.; Ma, E.; Zhang, J.; Zhang, M.
Eukaryotic expression, affinity purification and enzyme activity of chitin deacetylase in Locusta migratoria
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Locusta migratoria (A0A2R2PTF2), Locusta migratoria (A0A2R2PTF4), Locusta migratoria (A0A2R2PTG7)
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Yu, R.; Ding, G.; Liu, W.; Zhang, M.; Zhao, X.; Han, P.; Ma, E.; Zhang, J.
Molecular characterization and biological function of chitin deacetylase genes in Locusta migratoria
Sci. Agric. Sin.
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Locusta migratoria, Locusta migratoria (A0A509ZI24)
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Cord-Landwehr, S.; Melcher, R.L.; Kolkenbrock, S.; Moerschbacher, B.M.
A chitin deacetylase from the endophytic fungus Pestalotiopsis sp. efficiently inactivates the elicitor activity of chitin oligomers in rice cells
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Pestalotiopsis sp. (A0A1L3THR9), Pestalotiopsis sp.
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Aspergillus nidulans (A0A1U8QU02), Aspergillus nidulans ATCC 38163 (A0A1U8QU02), Aspergillus nidulans CBS 112.46 (A0A1U8QU02), Aspergillus nidulans FGSC A4 (A0A1U8QU02), Aspergillus nidulans FGSC A4, Aspergillus nidulans M139 (A0A1U8QU02), Aspergillus nidulans NRRL 194 (A0A1U8QU02)
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Aranda-Martinez, A.; Grifoll-Romero, L.; Aragunde, H.; Sancho-Vaello, E.; Biarnes, X.; Lopez-Llorca, L.V.; Planas, A.
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Pochonia chlamydosporia, Pochonia chlamydosporia 123
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