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4-methylumbelliferyl 2-amino-2-deoxy-beta-D-glucopyranoside + H2O
4-methylumbelliferone + 2-amino-2-deoxy-beta-D-glucopyranose
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucosaminide + H2O
4-nitrophenol + beta-D-glucosamine
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
4-nitrophenyl N,N'-diacetyl-beta-D-chitobioside + H2O
?
-
-
-
-
?
alpha-D-glucosaminyl fluoride + D-glucosamine
chitobiose + fluoride
beta-1,4-D-glucosamine tetrasaccharide
D-glucosamine + chitotriose
tetrasaccharide of chitosan efficiently depolymerizes chitosan to its constituent p-glucosamine monosaccharide in cooperation with endo-chitosanase
-
-
?
beta-glucan + H2O
?
-
13.6% activity compared to soluble chitosan
-
-
?
cellotetraose + H2O
?
-
-
-
-
?
chitobiitol + H2O
?
-
0.3% of the activity with chitopentaose
-
-
?
chitobiose + H2O
2 D-glucosamine
chitobiose + H2O
D-glucosamine
chitobiose + H2O
glucosamine + glucosamine
-
(GlcN)6 is sequentially cleaved into GlcN5,GlcN4, GlcN3, GlcN2, and GlcN, glucosamine is the final product
-
-
?
chitoheptaose + H2O
D-glucosamine + chitohexaose
chitohexaitol + H2O
?
-
94% of the activity with chitopentaose
-
-
?
chitohexaitol + H2O
D-glucosamine + ?
chitohexaose + H2O
2-amino-2-deoxy-D-glucopyranose + chitopentaose
-
GlcNn: polymerization degree of n=2-6, chitosan oligosaccharides, 0.96 nM exochiosanase, 10 mM ammonium acetate, pH 5.2, substrate concentrations: 6.25, 12.5, 25, 37.5 microM, hexa-N-acetylchitohexaose as control substrate at 25 microM
-
-
?
chitohexaose + H2O
chitopentaose + glucosamine
-
(GlcN)6 is sequentially cleaved into GlcN5,GlcN4, GlcN3, GlcN2, and GlcN, glucosamine is the final product
-
-
?
chitohexaose + H2O
D-glucosamine
chitohexaose + H2O
D-glucosamine + ?
chitohexaose + H2O
D-glucosamine + chitopentaose
chitopentaitol + H2O
?
-
99% of the activity with chitopentaose
-
-
?
chitopentaitol + H2O
D-glucosamine + ?
chitopentaose + H2O
chitotetraose + glucosamine
-
(GlcN)6 is sequentially cleaved into GlcN5,GlcN4, GlcN3, GlcN2, and GlcN, glucosamine is the final product
-
-
?
chitopentaose + H2O
D-glucosamine
chitopentaose + H2O
D-glucosamine + ?
-
-
-
?
chitopentaose + H2O
D-glucosamine + chitotetraose
chitosan + H2O
D-glucosamine + ?
chitotetraitol + H2O
?
-
as active as chitopentaose
-
-
?
chitotetraitol + H2O
D-glucosamine + ?
chitotetraose + H2O
chitotriose + glucosamine
-
(GlcN)6 is sequentially cleaved into GlcN5,GlcN4, GlcN3, GlcN2, and GlcN, glucosamine is the final product
-
-
?
chitotetraose + H2O
D-glucosamine
chitotetraose + H2O
D-glucosamine + chitotriose
-
products at an early stage of reaction
-
-
?
chitotriitol + H2O
?
-
85% of the activity with chitopentaose
-
-
?
chitotriitol + H2O
D-glucosamine
chitotriitol + H2O
D-glucosamine + ?
-
85% of the activity with chitopentaitol
-
-
?
chitotriose + H2O
?
-
-
-
?
chitotriose + H2O
chitobiose + D-glucosamine
chitotriose + H2O
D-glucosamine
chitotriose + H2O
D-glucosamine + chitobiose
-
products at an early stage of reaction
-
-
?
colloidal chitin + H2O
D-glucosamine + ?
-
deacetylation degree 80-85%, 6.4% activity compared to soluble chitosan
-
-
?
colloidal chitosan + H2O
beta-D-glucosamine + ?
colloidal chitosan + H2O
D-glucosamine + ?
-
56% activity compared to crab shell chitosan with more than 90% degree of acetylation
-
-
?
crab shell chitosan + H2O
D-glucosamine + ?
-
more than 90% degree of acetylation, 100% activity
-
-
?
D-glucosamine + N-acetyl-D-glucosamine
chitodimer
-
15% (w/v) ammonium sulfate is optimum for catalyzing transglycosylation reaction
-
-
?
deacetylated chitosan + H2O
?
-
slight hydrolysis
-
-
?
GlcN(beta1-4)GlcN(beta1-4)GlcN + H2O
GlcN(beta1-4)GlcN + D-glucosamine
-
-
-
-
?
GlcN(beta1-4)GlcN(beta1-4)GlcN(beta1-4)GlcN + H2O
GlcN(beta1-4)GlcN(beta1-4)GlcN + D-glucosamine
-
-
-
-
?
GlcN(beta1-4)GlcN(beta1-4)GlcN(beta1-4)GlcN(beta1-4)GlcN + H2O
GlcN(beta1-4)GlcN(beta1-4)GlcN(beta1-4)GlcN + D-glucosamine
-
-
-
-
?
GlcNbeta(1-4)GlcNAc + H2O
D-glucosamine + N-acetylglucosamine
-
-
-
-
?
GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcNAc + H2O
GlcNbeta(1-4)GlcNbeta(1-4)GlcNAc + D-glucosamine
glycol chitosan + H2O
D-glucosamine + ?
laminarin + H2O
?
-
21.5% activity compared to soluble chitosan
-
-
?
p-nitrophenyl beta-D-glucosaminide + H2O
p-nitrophenol + beta-D-glucosamine
-
-
-
?
p-nitrophenyl-beta-D-glucosamine + H2O
D-glucosamine + p-nitrophenol
-
-
-
?
p-nitrophenyl-beta-D-N-acetylglucosaminide + H2O
p-nitrophenol + beta-D-N-acetylglucosamine
shrimp shell chitosan + H2O
D-glucosamine + ?
-
more than 90% degree of acetylation, 57% activity compared to crab shell chitosan with more than 90% degree of acetylation
-
-
?
soluble chitosan + H2O
D-glucosamine + ?
-
deacetylation degree 80-85%, 100% activity
-
-
?
additional information
?
-
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
alpha-D-glucosaminyl fluoride + D-glucosamine
chitobiose + fluoride
-
-
-
?
alpha-D-glucosaminyl fluoride + D-glucosamine
chitobiose + fluoride
-
-
-
?
cellobiose + H2O
?
-
-
-
-
?
cellobiose + H2O
?
-
-
-
-
?
cellopentaose + H2O
?
-
-
-
-
?
cellopentaose + H2O
?
-
-
-
-
?
cellotriose + H2O
?
-
-
-
-
?
cellotriose + H2O
?
-
-
-
-
?
chitin + H2O
?
-
-
-
-
?
chitobiose + H2O
2 D-glucosamine
-
-
-
-
?
chitobiose + H2O
2 D-glucosamine
-
-
-
?
chitobiose + H2O
?
-
-
-
?
chitobiose + H2O
?
-
-
-
?
chitobiose + H2O
D-glucosamine
-
-
-
-
?
chitobiose + H2O
D-glucosamine
-
-
-
?
chitobiose + H2O
D-glucosamine
-
38% of the activity with chitopentaose
-
-
?
chitobiose + H2O
D-glucosamine
-
-
-
-
?
chitobiose + H2O
D-glucosamine
-
-
-
-
?
chitobiose + H2O
D-glucosamine
-
-
-
-
?
chitobiose + H2O
D-glucosamine
-
-
-
-
?
chitobiose + H2O
D-glucosamine
-
-
-
-
?
chitobiose + H2O
D-glucosamine
-
-
-
-
?
chitobiose + H2O
D-glucosamine
-
-
-
-
?
chitobiose + H2O
D-glucosamine
-
-
-
?
chitoheptaose + H2O
D-glucosamine + chitohexaose
-
products at an early stage of reaction
-
-
?
chitoheptaose + H2O
D-glucosamine + chitohexaose
-
products at an early stage of reaction
-
-
?
chitohexaitol + H2O
D-glucosamine + ?
-
89% of the activity with chitopentaitol
-
-
?
chitohexaitol + H2O
D-glucosamine + ?
-
89% of the activity with chitopentaitol
-
-
?
chitohexaose + H2O
D-glucosamine
-
92% of the activity with chitopentaose
-
-
?
chitohexaose + H2O
D-glucosamine
-
chitohexaose is hydrolyzed to chitopentaose and D-glucosamine at the initial stage of the reaction. The final product is D-glucosamine
-
-
?
chitohexaose + H2O
D-glucosamine
-
chitohexaose is hydrolyzed to chitopentaose and D-glucosamine at the initial stage of the reaction. The final product is D-glucosamine
-
-
?
chitohexaose + H2O
D-glucosamine
at the early stages of the reaction, chitohexaose is converted to D-glucosamine and chitopentaose
-
-
?
chitohexaose + H2O
D-glucosamine
-
cleaved to chitopentaose and glusosamine in the initial stage of the reaction
-
-
?
chitohexaose + H2O
D-glucosamine
-
cleaved to chitopentaose and glusosamine in the initial stage of the reaction
-
-
?
chitohexaose + H2O
D-glucosamine + ?
-
-
-
?
chitohexaose + H2O
D-glucosamine + ?
-
chitohexaose is hydrolyzed to chitopentaose + D-glucosamine at the beginning, and then the resulting chitopentaose changes successively to a smaller chitooligosaccharide with concomitant brelease of D-glucosamine
-
-
?
chitohexaose + H2O
D-glucosamine + ?
-
chitohexaose is hydrolyzed to chitopentaose + D-glucosamine at the beginning, and then the resulting chitopentaose changes successively to a smaller chitooligosaccharide with concomitant brelease of D-glucosamine
-
-
?
chitohexaose + H2O
D-glucosamine + chitopentaose
-
chitohexaose is hydrolyzed to chitopentaose and D-glucosamine at the initial stage of the reaction. The final product is D-glucosamine
-
-
?
chitohexaose + H2O
D-glucosamine + chitopentaose
-
chitohexaose is hydrolyzed to chitopentaose and D-glucosamine at the initial stage of the reaction. The final product is D-glucosamine
-
-
?
chitopentaitol + H2O
D-glucosamine + ?
-
-
-
-
?
chitopentaitol + H2O
D-glucosamine + ?
-
-
-
-
?
chitopentaose + H2O
?
cleaved to chitotetraose and glucosamine in the initial stage of the reaction
-
-
?
chitopentaose + H2O
?
cleaved to chitotetraose and glucosamine in the initial stage of the reaction
-
-
?
chitopentaose + H2O
D-glucosamine
-
-
-
-
?
chitopentaose + H2O
D-glucosamine
-
-
-
-
?
chitopentaose + H2O
D-glucosamine
-
-
-
-
?
chitopentaose + H2O
D-glucosamine
at the early stages of the reaction, chitopentaose is converted to D-glucosamine and chitotetraose
-
-
?
chitopentaose + H2O
D-glucosamine
-
-
-
-
?
chitopentaose + H2O
D-glucosamine
-
-
-
-
?
chitopentaose + H2O
D-glucosamine + chitotetraose
-
products at an early stage of reaction
-
-
?
chitopentaose + H2O
D-glucosamine + chitotetraose
-
products at an early stage of reaction
-
-
?
chitosan + H2O
?
-
-
-
?
chitosan + H2O
?
-
90% of the activity with chitopentaose
-
-
?
chitosan + H2O
?
-
-
-
-
?
chitosan + H2O
?
-
-
-
-
?
chitosan + H2O
?
-
-
-
-
?
chitosan + H2O
?
-
-
-
-
?
chitosan + H2O
?
-
the exo-beta-D-glucosaminidase cleaves the glycosidic link of either GlcN-beta(1,4)-GlcN or GlcN-beta(1,4)-GlcNAc
-
-
?
chitosan + H2O
?
-
the exo-beta-D-glucosaminidase cleaves the glycosidic link of either GlcN-beta(1,4)-GlcN or GlcN-beta(1,4)-GlcNAc
-
-
?
chitosan + H2O
D-glucosamine + ?
-
-
-
?
chitosan + H2O
D-glucosamine + ?
-
-
-
-
?
chitosan + H2O
D-glucosamine + ?
-
-
-
-
?
chitosan + H2O
D-glucosamine + ?
-
-
-
-
?
chitosan + H2O
D-glucosamine + ?
-
fully deacetylated chitosan
-
-
?
chitosan + H2O
D-glucosamine + ?
-
chitosan with more than 50% degree of acetylation, 9% activity compared to crab shell chitosan chitosan with more than 90% degree of acetylation
-
-
?
chitosan + H2O
D-glucosamine + ?
-
chitosan with more than 60% degree of acetylation, 21% activity compared to crab shell chitosan chitosan with more than 90% degree of acetylation
-
-
?
chitosan + H2O
D-glucosamine + ?
-
chitosan with more than 70% degree of acetylation, 43% activity compared to crab shell chitosan with more than 90% degree of acetylation
-
-
?
chitosan + H2O
D-glucosamine + ?
-
chitosan with more than 80% degree of acetylation, 68% activity compared to crab shell chitosan with more than 90% degree of acetylation
-
-
?
chitosan + H2O
D-glucosamine + ?
-
-
-
-
?
chitosan + H2O
D-glucosamine + ?
-
chitosan with more than 50% degree of acetylation, 9% activity compared to crab shell chitosan chitosan with more than 90% degree of acetylation
-
-
?
chitosan + H2O
D-glucosamine + ?
-
chitosan with more than 60% degree of acetylation, 21% activity compared to crab shell chitosan chitosan with more than 90% degree of acetylation
-
-
?
chitosan + H2O
D-glucosamine + ?
-
only glucosamine is produced as final product after prolonged reaction
-
-
?
chitosan + H2O
D-glucosamine + ?
-
only glucosamine is produced as final product after prolonged reaction
-
-
?
chitosan + H2O
D-glucosamine + ?
100% activity with 95% deacetylated chitosan, 88% activity with 83% deacetylated chitosan, 80% activity with 70% deacetylated chitosan, and 68% activity with 60% deacetylated chitosan
-
-
?
chitosan + H2O
D-glucosamine + ?
-
soluble chitosan, powdered chitosan and colloidal chitosan
-
-
?
chitosan + H2O
D-glucosamine + ?
-
soluble chitosan, powdered chitosan and colloidal chitosan
-
-
?
chitosan + H2O
D-glucosamine + ?
-
only D-glucosamine is produced after prolonged hydrolysis
-
-
?
chitosan + H2O
D-glucosamine + ?
-
only D-glucosamine is produced after prolonged hydrolysis
-
-
?
chitosan + H2O
D-glucosamine + ?
-
-
-
?
chitosan + H2O
D-glucosamine + ?
chitosan 10B
-
-
?
chitotetraitol + H2O
D-glucosamine + ?
-
97% of the activity with chitopentaitol
-
-
?
chitotetraitol + H2O
D-glucosamine + ?
-
97% of the activity with chitopentaitol
-
-
?
chitotetraose + H2O
?
-
-
-
-
?
chitotetraose + H2O
?
-
-
-
?
chitotetraose + H2O
D-glucosamine
-
99% of the activity with chitopentaose
-
-
?
chitotetraose + H2O
D-glucosamine
-
at first, the enzyme predominantly produces D-glucosamine and chitotriose, which is further degraded into D-glucosamine and chitobiose. The transglycosylation product, chitopentaose, is also produced, together with a lesser amount of chitohexaose
-
-
?
chitotetraose + H2O
D-glucosamine
-
-
-
-
?
chitotetraose + H2O
D-glucosamine
-
-
-
-
?
chitotetraose + H2O
D-glucosamine
-
-
-
-
?
chitotetraose + H2O
D-glucosamine
at the early stages of the reaction, chitotetraose is converted to D-glucosamine and chitotriose
-
-
?
chitotriitol + H2O
D-glucosamine
-
-
-
-
?
chitotriitol + H2O
D-glucosamine
-
-
-
-
?
chitotriose + H2O
chitobiose + D-glucosamine
-
(GlcN)6 is sequentially cleaved into GlcN5,GlcN4, GlcN3, GlcN2, and GlcN, glucosamine is the final product
-
-
?
chitotriose + H2O
chitobiose + D-glucosamine
-
-
-
-
?
chitotriose + H2O
D-glucosamine
-
92% of the activity with chitopentaose
-
-
?
chitotriose + H2O
D-glucosamine
-
-
-
-
?
chitotriose + H2O
D-glucosamine
-
-
-
?
colloidal chitosan + H2O
beta-D-glucosamine + ?
-
-
-
?
colloidal chitosan + H2O
beta-D-glucosamine + ?
-
-
-
?
GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcNAc + H2O
GlcNbeta(1-4)GlcNbeta(1-4)GlcNAc + D-glucosamine
-
(GlcN)3-GlcNAc (mono-N-acetylated chitotetraose, the reducing end residue is N-acetylated) is at first degraded into (GlcN)2-GlcNAc, and then into GlcN-GlcNAc. After a longer incubation period, the substrate is finally hydrolyzed into monosaccharides, GlcN and GlcNAc
-
-
?
GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcNAc + H2O
GlcNbeta(1-4)GlcNbeta(1-4)GlcNAc + D-glucosamine
-
(GlcN)3-GlcNAc is a mono-N-acetylated chitotetraose, the reducing end residue is N-acetylated. D-glucosamine is produced from the nonreducing end together with the transglycosylation products
-
-
?
glycol chitosan + H2O
?
-
-
-
-
?
glycol chitosan + H2O
?
-
-
-
-
?
glycol chitosan + H2O
?
-
4% of the activity with chitosan
-
-
?
glycol chitosan + H2O
?
-
4% of the activity with chitosan
-
-
?
glycol chitosan + H2O
D-glucosamine + ?
-
12% activity compared to crab shell chitosan with more than 90% degree of acetylation
-
-
?
glycol chitosan + H2O
D-glucosamine + ?
-
-
-
-
?
glycol chitosan + H2O
D-glucosamine + ?
-
631.3% activity compared to soluble chitosan
-
-
?
p-nitrophenyl-beta-D-N-acetylglucosaminide + H2O
p-nitrophenol + beta-D-N-acetylglucosamine
-
-
-
-
?
p-nitrophenyl-beta-D-N-acetylglucosaminide + H2O
p-nitrophenol + beta-D-N-acetylglucosamine
-
-
-
-
?
additional information
?
-
no activity is detectable against p-nitrophenyl derivatives of beta-D-glucopyranoside, beta-D-xylopyranoside, beta-D-mannoside, beta-D-glucuronide, beta-D-galactoside, beta-D-N-acetylgalactosaminide, beta-D-N-acetylglucosaminide and alpha-D-N-acetylglucosaminide
-
-
?
additional information
?
-
-
no activity is detectable against p-nitrophenyl derivatives of beta-D-glucopyranoside, beta-D-xylopyranoside, beta-D-mannoside, beta-D-glucuronide, beta-D-galactoside, beta-D-N-acetylgalactosaminide, beta-D-N-acetylglucosaminide and alpha-D-N-acetylglucosaminide
-
-
?
additional information
?
-
-
Chitosanases hydrolyze beta-1,4-glycosidic linkage of chitosan, a polysaccharide consisting mainly of D-glucosamine with a variable content of N-acetyl-D-glucosamine
-
-
?
additional information
?
-
cleaving nonreducing beta-D-glucosamine residues of oligosaccharides, highly specific due to pocket for N2 group of glucosaminidase discriminating it from glucose
-
-
?
additional information
?
-
-
cleaving nonreducing beta-D-glucosamine residues of oligosaccharides, highly specific due to pocket for N2 group of glucosaminidase discriminating it from glucose
-
-
?
additional information
?
-
-
no degradation of cellulose and starch. The exo-beta-D-glucosaminidase exhibits transglycosylation activity, resulting in the one-residue elongated oligomers
-
-
?
additional information
?
-
-
no activity with flaked chitin, colloidal chitin and cellulose
-
-
?
additional information
?
-
-
no activity with flaked chitin, colloidal chitin and cellulose
-
-
?
additional information
?
-
-
no degradation of cellulose and starch. The exo-beta-D-glucosaminidase exhibits transglycosylation activity, resulting in the one-residue elongated oligomers
-
-
?
additional information
?
-
no hydrolysis of colloid chitin and carboxymethylcellulose
-
-
?
additional information
?
-
-
the enzyme acts on beta-1,4-linkage of chitosan from its non-reducing end and produces D-glucosamine as the exclusive end product
-
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additional information
?
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preparation of alpha-chitin and chitosan from shrimp processing raw byproducts
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additional information
?
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the enzyme acts on beta-1,4-linkage of chitosan from its non-reducing end and produces D-glucosamine as the exclusive end product
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?
additional information
?
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preparation of alpha-chitin and chitosan from shrimp processing raw byproducts
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?
additional information
?
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the enzyme catalyzes transglycosylation reaction on chitobiose and chitotriose
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additional information
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the enzyme catalyzes transglycosylation reaction on chitobiose and chitotriose
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additional information
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no activity with carboxymethyl cellulose, cellulose, xylan and galactomannan
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additional information
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the enzyme fails to release a reducing sugar from avicel and carboxylmethyl cellulose
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additional information
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the enzyme fails to release a reducing sugar from avicel and carboxylmethyl cellulose
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additional information
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the enzyme cleaves the beta-1->4-glycosidic bonds between GlcN-GlcN and GlcN-GlcNAc but not between GlcNAc-GlcN or GlcNAc-GlcNAc, cleavage of GlcN-GlcNAc, a partially acetylated chitooligomer mixture, overview. The purified enzyme displays high activity toward chitosan and (GlcN)6. No significant activity with N-carboxymethyl chitosan, or chitin, also synthetic p-nitrophenyl-beta-D-glucosaminide is not hydrolyzed. Chitosan with higher deacetylation degrees is hydrolyzed more efficiently than chitosan with lower deacetylation values. Substrate specifiicty analysis using massspectrometry. Paecilomyces exo-beta-D-GlcNase can accelerate the hydrolysis of p-nitrophenyl-beta-D-N-acetylglucosaminide, p-nitrophenyl-beta-D-N,N'-diacetylchitobioside, and p-nitrophenyl-beta-D-N-acetylgalactosaminide to release the corresponding sugar
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additional information
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the enzyme also catalyzes transglycosylation reactions
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additional information
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the enzyme also catalyzes transglycosylation reactions
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(1R,2R,3R,7S,7aR)-3-(aminomethyl)hexahydro-1H-pyrrolizine-1,2,7-triol
modest competitive inhibitor of CsxA
(1S,6S,7R,8R)-6-aminooctahydroindolizine-1,7,8-triol
potent competitive inhibitor of CsxA
2-Hydroxy-5-nitrobenzyl bromide
4-chloromercuribenzoate
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88% residual activity at 1 mM
AlCl3
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10 mM, 37% inhibition
Ba2+
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98% residual activity at 1 mM
Cd2+
-
90% residual activity at 1 mM
CuSO4
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10 mM, 55% inhibition
dithiothreitol
-
90% residual activity at 1 mM
EDTA
65% residual activity at 1 mg/ml, complete inhibition at 5 mg/ml
HgCl2
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10 mM, complete inhibition
iodoacetate
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93% residual activity at 1 mM
K+
84.6% residual activity at 10 mg/ml
N-bromosuccinimide
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10 mM, 34% inhibition
N-ethylmaleimide
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66% residual activity at 1 mM
p-chloromercuribenzoic acid
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2.5 mM, 86% inhibition
Pb(NO3)2
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10 mM, 47% inhibition
SDS
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54% residual activity at 10 mM
Triton X-100
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88% residual activity at 1 mM
Tween 20
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76% residual activity at 1 mM
Urea
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90.4% residual activity at 10 mM
ZnSO4
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10 mM, 21% inhibition
additional information
neither castanospermine nor australine are capable of inhibiting the enzyme at a concentration of 1 mM
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2-Hydroxy-5-nitrobenzyl bromide
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2.5 mM, complete inhibition
2-Hydroxy-5-nitrobenzyl bromide
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65% residual activity at 1 mM
Ag+
47.9% residual activity at 5 mg/ml, complete inhibition at 10 mg/ml
Ag+
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complete inhibition at 1 mM
Ca2+
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88% residual activity at 1 mM
Ca2+
76.8% residual activity at 10 mg/ml
Co2+
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32% residual activity at 1 mM
Co2+
4.8% residual activity at 10 mg/ml
Cu2+
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98% residual activity at 1 mM
Cu2+
19.3% residual activity at 10 mg/ml
Cu2+
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complete inhibition at 10 mM
Fe2+
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87% residual activity at 1 mM
Fe2+
16.1% residual activity at 10 mg/ml
Fe2+
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82.5% residual activity at 10 mM
Hg2+
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76% residual activity at 1 mM
Hg2+
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complete inhibition at 1 mM
Mg2+
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95% residual activity at 1 mM
Mg2+
55.8% residual activity at 10 mg/ml
Mn2+
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98% residual activity at 1 mM
Mn2+
2.5% residual activity at 5 mg/ml, complete inhibition at 10 mg/ml
Ni2+
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87% residual activity at 1 mM
Ni2+
82.9% residual activity at 10 mg/ml
Ni2+
-
40.5% residual activity at 10 mM
Zn2+
55.8% residual activity at 10 mg/ml
Zn2+
-
36.5% residual activity at 10 mM
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Zhang, X.Y.; Dai, A.L.; Zhang, X.K.; Kuroiwa, K.; Kodaira, R.; Shimosaka, M.; Okazaki, M.
Purification and characterization of chitosanase and exo-beta-D-glucosaminidase from a Koji mold, Aspergillus oryzae IAM2660
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Aspergillus oryzae, Aspergillus oryzae IAM2660
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Purification and properties of exo-beta-D-glucosaminidase from Penicillium sp. and its applications
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Penicillium sp., Penicillium sp. AF9-P-112
-
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Nogawa, M.; Takahashi, H.; Kashiwagi, A.; Ohshima, K.; Okada, H.; Morikawa, Y.
Purification and characterization of exo-beta-D-glucosaminidase from a cellulolytic fungus, Trichoderma reesei PC-3-7
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64
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Trichoderma reesei, Trichoderma reesei PC-3-7
brenda
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Cloning and heterologous expression of the exo-beta-D-glucosaminidase-encoding gene (gls93) from a filamentous fungus, Trichoderma reesei PC-3-7
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72
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Trichoderma reesei (Q4R1C4), Trichoderma reesei, Trichoderma reesei PC-3-7 (Q4R1C4), Trichoderma reesei PC-3-7
brenda
Cote, N.; Fleury, A.; Dumont-Blanchette, E.; Fukamizo, T.; Mitsutomi, M.; Brzezinski, R.
Two exo-beta-D-glucosaminidases/exochitosanases from actinomycetes define a new subfamily within family 2 of glycoside hydrolases
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Amycolatopsis orientalis (Q56F26), Amycolatopsis orientalis
brenda
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Talaromyces funiculosus, Talaromyces funiculosus KY616
-
brenda
Fukamizo, T.; Fleury, A.; Cote, N.; Mitsutomi, M.; Brzezinski, R.
Exo-beta-D-glucosaminidase from Amycolatopsis orientalis: catalytic residues, sugar recognition specificity, kinetics, and synergism
Glycobiology
16
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2006
Amycolatopsis orientalis
brenda
Fukamizo, T.; Brzezinski, R.
Structure and function of exo-beta-glucosaminidase from Amycolatopsis orientalis
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54
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Amycolatopsis orientalis
-
brenda
Tanaka, T.; Fukui, T.; Atomi, H.; Imanaka, T.
Characterization of an exo-beta-D-glucosaminidase involved in a novel chitinolytic pathway from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
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185
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2003
Thermococcus kodakarensis (Q76HN4)
brenda
Nanjo, F.; Katsumi, R.; Sakai, K.
Purification and characterization of an exo-beta-D-glucosaminidase, a novel type of enzyme, from Nocardia orientalis
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265
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Amycolatopsis orientalis
brenda
Ji, J.H.; Yang, J.S.; Hur, J.W.
Purification and characterization of the exo-beta -D-glucosaminidase from Aspergillus flavus IAM2044
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13
269-275
2003
Aspergillus flavus, Aspergillus flavus IAM2044
-
brenda
Jung, W.J.; Kuk, J.H.; Kim, K.Y.; Jung, K.C.; Park, R.D.
Purification and characterization of exo-beta-D-glucosaminidase from Aspergillus fumigatus S-26
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45
125-131
2006
Aspergillus fumigatus, Aspergillus fumigatus S-26
brenda
Dennhart, N.; Fukamizo, T.; Brzezinski, R.; Lacombe-Harvey, M.E.; Letzel, T.
Oligosaccharide hydrolysis by chitosanase enzymes monitored by real-time electrospray ionization-mass spectrometry
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134
253-260
2008
Amycolatopsis orientalis
brenda
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The structural basis of substrate recognition in an exo-beta-D-glucosaminidase involved in chitosan hydrolysis
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385
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2009
Amycolatopsis orientalis (Q56F26), Amycolatopsis orientalis
brenda
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Crystallization and preliminary X-ray crystallographic studies of an exo-beta-D-glucosaminidase from Trichoderma reesei
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66
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2010
Trichoderma reesei (Q4R1C4), Trichoderma reesei
brenda
Li, S.; Wang, C.; Xia, W.
Expression, purification, and characterization of exo-beta-D-glucosaminidase of Aspergillus sp. CJ22-326 from Escherichia coli
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344
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Aspergillus sp. (C3U4R9)
brenda
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Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine-configured castanospermine and an amino-australine analogue
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7
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Amycolatopsis orientalis (Q56F26)
brenda
Honda, Y.; Shimaya, N.; Ishisaki, K.; Ebihara, M.; Taniguchi, H.
Elucidation of exo-beta-D-glucosaminidase activity of a family 9 glycoside hydrolase (PBPRA0520) from Photobacterium profundum SS9
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21
503-511
2011
Photobacterium profundum, Photobacterium profundum SS9
brenda
Chao, C.F.; Chen, Y.Y.; Cheng, C.Y.; Li, Y.K.
Catalytic function of a newly purified exo-beta-D-glucosaminidase from the entomopathogenic fungus Paecilomyces lilacinus
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93
615-621
2013
Purpureocillium lilacinum
brenda
Nidheesh, T.; Gaurav Kumar, P.; Suresh, P.
Enzymatic degradation of chitosan and production of D-glucosamine by solid substrate fermentation of exo-beta-D-glucosaminidase (exochitosanase) by Penicillium decumbens CFRNT15
Int. Biodeter. Biodegrad.
97
97-106
2015
Penicillium decumbens, Penicillium decumbens CFRNT15
-
brenda
Ike, M.; Ogasawara, W.; Okada, H.; Morikawa, Y.
The essential acidic amino acid residues for catalytic activity of an exo-beta-D-glucosaminidase from Trichoderma reesei
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2008
Trichoderma reesei (Q4R1C4)
-
brenda
Sinha, S.; Chand, S.; Tripathi, P.
Enzymatic production of glucosamine and chitooligosaccharides using newly isolated exo-beta-D-glucosaminidase having transglycosylation activity
3 Biotech
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13
2016
Aspergillus fumigatus, Aspergillus fumigatus IIT-004
brenda
Honda, Y.; Arai, S.; Suzuki, K.; Kitaoka, M.; Fushinobu, S.
The crystal structure of an inverting glycoside hydrolase family 9 exo-beta-D-glucosaminidase and the design of glycosynthase
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473
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2016
Photobacterium profundum (Q6LUT2), Photobacterium profundum, Photobacterium profundum SS9 (Q6LUT2)
brenda
Kim, T.I.; Lim, D.H.; Baek, K.S.; Jang, S.S.; Park, B.Y.; Mayakrishnan, V.
Production of chitinase from Escherichia fergusonii, chitosanase from Chryseobacterium indologenes, Comamonas koreensis and its application in N-acetylglucosamine production
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1115-1121
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Chryseobacterium indologenes, Comamonas koreensis, Chryseobacterium indologenes HANYOO, Comamonas koreensis HANWOO
brenda
Mine, S.; Watanabe, M.; Kamachi, S.; Abe, Y.; Ueda, T.
The structure of an archaeal beta-glucosaminidase provides insight into glycoside hydrolase evolution
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4996-5006
2017
Pyrococcus horikoshii, Thermococcus kodakarensis (Q76HN4)
brenda
Wu, D.; Wang, L.; Li, Y.; Zhao, S.; Peng, N.; Liang, Y.
Heterologous expression and characterization of a thermostable exo-beta-D-glucosaminidase from Aspergillus oryzae
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26
347-355
2016
Aspergillus oryzae (W8E1X9), Aspergillus oryzae FL402 (W8E1X9)
brenda
Aktuganov, G.E.; Galimzianova, N.F.; Gilvanova, E.A.; Pudova, E.A.; Kuzmina, L.Y.; Melentiev, A.I.; Safina, V.R.
Purification and characterization of exo-beta-1,4-glucosaminidase produced by chitosan-degrading fungus, Penicillium sp. IB-37-2A
World J. Microbiol. Biotechnol.
35
18
2019
Penicillium sp. IB-37-2A
brenda