3.5.1.41: chitin deacetylase
This is an abbreviated version!
For detailed information about chitin deacetylase, go to the full flat file.
Word Map on EC 3.5.1.41
-
3.5.1.41
-
chitosan
-
deacetylases
-
colletotrichum
-
peritrophic
-
lindemuthianum
-
chitooligosaccharides
-
rouxii
-
chitosanase
-
chitin-binding
-
chitinolytic
-
n-deacetylated
-
acetamido
-
synthesis
-
absidia
-
peritrophin-a
-
larval-pupal
-
agriculture
-
medicine
-
drug development
-
analysis
- 3.5.1.41
- chitosan
- deacetylases
-
colletotrichum
-
peritrophic
- lindemuthianum
- chitooligosaccharides
- rouxii
- chitosanase
-
chitin-binding
-
chitinolytic
-
n-deacetylated
-
acetamido
- synthesis
- absidia
-
peritrophin-a
-
larval-pupal
- agriculture
- medicine
- drug development
- analysis
Reaction
Synonyms
AN9380.2, AnCDA, ANIA_09380, ArCE4, Blcda, BmCDA6, BmCDA7, BmCDA8, CDA, CDA-like protein, CDA1, Cda1p, CDA2, cda2aa, cda2b, Cda2p, CDA3, cda4, cda5a, cda5b, cdaYJ, CE4 deacetylase, CHD, chitin amidohydrolase,, chitin deacetylase, chitin deacetylase 1, chitin deacetylase 2, chitin deacetylase 2A, chitin deacetylase 2B, chitin deacetylase 3, chitin deacetylase 4, chitin deacetylase 5A, chitin deacetylase 5B, chitin deacetylase 6, chitin deacetylase 7, chitin deacetylase 8, chitin deacetylase 9, chitin deacetylase RC, chitin deacetylase-like protein, chitin deacetylase2, ChlD, ClCDA, D2 chitin deacetylase, Fpd1, FV-PDA, Hacda2, I3/2 chitin deacetylase, LmCDA1, LmCDA2, LmCDA2a, LmCDA2b, LmCDA4, LmCDA5a, LmCDA5b, midgut chitin deacetylase, More, MrCDA, N-acetylglucosamine deacetylase, NodB, NodB deacetylase, NodB homology domain-containing protein, PaCDA, PcCDA, pc_2566, PesCDA, PgtCDA, PODANS_1_4780, RC chitin deacetylase, ScCDA2, TcCDA1, TcCDA2A, TcCDA2B, TcCDA3, TcCDA4, TcCDA5A, TcCDA5B, TcCDA6, TcCDA7, TcCDA8, TcCDA9, VcCDA, VpCDA
ECTree
3.5.1.41 chitin deacetylaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.5.1.41 - chitin deacetylase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(N-acetyl-D-glucosamine)2 + H2O
(GlcN)GlcNAc + 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
-
-
-
-
?
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
?
acetylated chitosan oligomer + H2O
?
increasing activity with increasing degree of acetylation
-
-
?
chitobiose + acetate
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-D-glucose + 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%
-
-
?
crab chitosan + H2O
?
-
71-88% degree of deacetylation with 21-10% activity compared to water-soluble chitin with degree of deacetylation 50%
-
-
?
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)-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-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)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNbeta(1-4)GlcNAc + acetate
-
-
-
?
hexa-N-acetyl-chitohexaose + H2O
chitohexaose + 6 acetate
A0A1U8QU02
-
-
-
?
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
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'''-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
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
-
-
-
?
swollen chitin + H2O
?
-
8% degree of deacetylation with 6% activity compared to water-soluble chitin with degree of deacetylation 50%
-
-
?
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
-
-
-
?
acetylated chitin polymer + H2O
?
increasing activity with increasing chain length
-
-
?
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
?
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
?
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 xylan + H2O
?
A0A1U8QU02
the dominating products are fully deacetylated xylooligosaccharides
-
-
?
acetylated xylan + H2O
?
A0A1U8QU02
the dominating products are fully deacetylated xylooligosaccharides
-
-
?
acetylated xylan + H2O
?
Aspergillus nidulans CBS 112.46
A0A1U8QU02
the dominating products are fully deacetylated xylooligosaccharides
-
-
?
acetylated xylan + H2O
?
A0A1U8QU02
the dominating products are fully deacetylated xylooligosaccharides
-
-
?
acetylated xylan + H2O
?
Aspergillus nidulans M139
A0A1U8QU02
the dominating products are fully deacetylated xylooligosaccharides
-
-
?
acetylated xylan + H2O
?
Aspergillus nidulans NRRL 194
A0A1U8QU02
the dominating products are fully deacetylated xylooligosaccharides
-
-
?
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
-
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
-
powdered chitin, 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
-
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
-
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
-
reacetylated commercial chitosan with 52% acetylation degree is used as substrate, optimization of reaction conditions, overview
-
-
?
chitin + H2O
chitosan + acetate
-
reacetylated commercial chitosan with 52% acetylation degree is used as substrate, optimization of reaction conditions, overview
-
-
?
chitin + H2O
chitosan + acetate
-
partially N-deacetylated water soluble chitin
-
?
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
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
-
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
-
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
-
the enzyme deacetylates glycol chitin and chitin oligomers having degree of polymerization of more than four
-
-
?
chitin + H2O
chitosan + acetate
-
the enzyme deacetylates glycol chitin and chitin oligomers having degree of polymerization of more than four
-
-
?
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
-
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 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
-
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
-
-
?
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
-
-
?
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
?
-
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
chitosan + acetate
-
lysozyme digests of glycol chitin: poor
-
?
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
-
the chitin deacetylase activity from Flammulina velutipes is determined as around 13fold higher on substrate of chitosan than glycol chitin
-
-
r
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
Puccinia graminis f. sp. tritici race SCCL
-
-
-
?
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
-
-
?
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'''-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
?
-
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
?
-
processive, reducing-end residue remains intact
-
-
?
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
?
-
high substrate concentration needed
-
-
?
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-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
?
-
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-acetylchitotetraose + H2O
?
-
41.8% activity compared to hepta-N-acetylchitoheptaose
-
-
?
tri-N-acetylchitotriose + H2O
?
-
38.9% activity compared to hepta-N-acetylchitoheptaose
-
-
?
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
chitin deacetylase is not effective on natural insoluble crystalline chitin
-
-
?
additional information
?
-
-
chitin deacetylase is not effective on natural insoluble crystalline chitin
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
CDA catalyzes the deacetylation of monomeric acetyl glucosamine residues of chitin by multiple attack mechanism
-
-
?
additional information
?
-
-
CDA catalyzes the deacetylation of monomeric acetyl glucosamine residues of chitin by multiple attack mechanism
-
-
?
additional information
?
-
Aspergillus flavus P6B2
CDA catalyzes the deacetylation of monomeric acetyl glucosamine residues of chitin by multiple attack mechanism
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
Aspergillus nidulans CBS 112.46
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
Aspergillus nidulans M139
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
-
-
?
additional information
?
-
Aspergillus nidulans NRRL 194
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the enzyme catalyses the hydrolysis of the acetamido group in the N-acetylglucosamine units of chitin and chitosan, generating glucosamine units and acetic acid
-
-
?
additional information
?
-
-
the enzyme catalyses the hydrolysis of the acetamido group in the N-acetylglucosamine units of chitin and chitosan, generating glucosamine units and acetic acid
-
-
?
additional information
?
-
no activity with peritrophic matrix chitin by isozyme BmCDA6
-
-
?
additional information
?
-
no activity with peritrophic matrix chitin by isozyme BmCDA6
-
-
?
additional information
?
-
no activity with peritrophic matrix chitin by isozyme BmCDA6
-
-
?
additional information
?
-
-
no activity with peritrophic matrix chitin by isozyme BmCDA6
-
-
?
additional information
?
-
binding study of an N-acetylglucosaminyl trimer to the enzyme, computational docking
-
-
?
additional information
?
-
-
binding study of an N-acetylglucosaminyl trimer to the enzyme, computational docking
-
-
?
additional information
?
-
substrate specificity, overview, no activity with chitotriose
-
-
?
additional information
?
-
-
substrate specificity, overview, no activity with chitotriose
-
-
?
additional information
?
-
-
chitin deacetylase is not effective on natural insoluble crystalline chitin
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
binding study of an N-acetylglucosaminyl trimer to the enzyme, computational docking
-
-
?
additional information
?
-
substrate specificity, overview, no activity with chitotriose
-
-
?
additional information
?
-
-
substrate specificity, overview, no activity with chitotriose
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
chitin deacetylase is not effective on natural insoluble crystalline chitin
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
chitin deacetylase is not effective on natural insoluble crystalline chitin
-
-
?
additional information
?
-
the recombinant FV-PDA catalyses deacetylation of N-acetyl-chitooligomers, from dimer to pentamer, glycol chitin and colloidal chitin
-
-
?
additional information
?
-
-
the recombinant FV-PDA catalyses deacetylation of N-acetyl-chitooligomers, from dimer to pentamer, glycol chitin and colloidal chitin
-
-
?
additional information
?
-
-
chitin deacetylase is not effective on natural insoluble crystalline chitin
-
-
?
additional information
?
-
-
chitin deacetylase is not effective on natural insoluble crystalline chitin
-
-
?
additional information
?
-
-
GlcNAc, colloidal chitin, regenerated chitin, beta-chitin and crystal crab chitins with different particle size are not deacetylated by the crude enzyme
-
-
?
additional information
?
-
-
GlcNAc, colloidal chitin, regenerated chitin, beta-chitin and crystal crab chitins with different particle size are not deacetylated by the crude enzyme
-
-
?
additional information
?
-
-
chitin deacetylase is not effective on natural insoluble crystalline chitin
-
-
?
additional information
?
-
-
chitin deacetylase is not effective on natural insoluble crystalline chitin
-
-
?
additional information
?
-
-
chitin deacetylase is not effective on natural insoluble crystalline chitin
-
-
?
additional information
?
-
-
the enzyme is not able to deacetylate N-acetyl glucosamine
-
-
?
additional information
?
-
-
no activity with N-acetyl glucosamine, marginal activity towards (GlcNAc)2 and (GlcNAc)3
-
-
?
additional information
?
-
-
the enzyme is not able to deacetylate N-acetyl glucosamine
-
-
?
additional information
?
-
-
no activity with N-acetyl glucosamine, marginal activity towards (GlcNAc)2 and (GlcNAc)3
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing
-
-
?
additional information
?
-
-
analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing
-
-
?
additional information
?
-
analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing
-
-
?
additional information
?
-
analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing
-
-
?
additional information
?
-
analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
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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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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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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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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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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