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Information on EC 3.2.1.165 - exo-1,4-beta-D-glucosaminidase
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3.2.1.165 exo-1,4-beta-D-glucosaminidaseIUBMB Comments
Chitosan is a partially or totally N-deacetylated chitin derivative that is found in the cell walls of some phytopathogenic fungi and comprises D-glucosamine residues with a variable content of GlcNAc residues . Acts specifically on chitooligosaccharides and chitosan, having maximal activity on chitotetraose, chitopentaose and their corresponding alcohols . The enzyme can degrade GlcN-GlcNAc but not GlcNAc-GlcNAc . A member of the glycoside hydrolase family 2 (GH-2) .
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Word Map
- 3.2.1.165
- chitosans
- glucosamine
- chitin
-
deacetylation
-
nonreducing
- chitooligosaccharides
-
exo-type
- n-acetylglucosamine
- chitobiose
- orientalis
- thermococcus
- diacetylchitobiose
- glcnac2
-
transglycosylation
- synthesis
-
amycolatopsis
-
chitosanolytic
-
viscosimetric
- kodakaraensis
-
exo-splitting
- beta-mannosidase
- reesei
-
glcn-glcnac
-
chitosan-degrading
-
cm-sephadex
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
hydrolysis of chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini
Synonyms
exo-beta-d-glucosaminidase, glcnase, gls93, exo-chitosanase, exochitosanase, beta-glcnase, exo-beta-glucosaminidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CsxA
exo-beta-D-GlcNase
exo-beta-D-glucosaminidase
exo-chitosanase
exochitosanase
GlcNase
GlmA
Gls93
PBPRA0520 protein
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini
hydrolysis of chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini
-
-
-
-
hydrolysis of chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini
two-step mechanism and transglycosylation of the retaining glycoside hydrolase forming a glycosyl-enzyme intermediate
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis
-
cleaving 2-amino-2-deoxy-D-glucopyranose off oligosaccharides
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
chitosan exo-(1->4)-beta-D-glucosaminidase
Chitosan is a partially or totally N-deacetylated chitin derivative that is found in the cell walls of some phytopathogenic fungi and comprises D-glucosamine residues with a variable content of GlcNAc residues [4]. Acts specifically on chitooligosaccharides and chitosan, having maximal activity on chitotetraose, chitopentaose and their corresponding alcohols [1]. The enzyme can degrade GlcN-GlcNAc but not GlcNAc-GlcNAc [3]. A member of the glycoside hydrolase family 2 (GH-2) [4].
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CAS REGISTRY NUMBER
COMMENTARY
9012-33-3
c.f. EC 3.2.1.52
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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
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
-
-
-
-
?
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
-
-
?
chitobiose + H2O
glucosamine + glucosamine
-
(GlcN)6 is sequentially cleaved into GlcN5,GlcN4, GlcN3, GlcN2, and GlcN, glucosamine is the final product
-
-
?
chitohexaitol + H2O
?
-
94% of the activity with chitopentaose
-
-
?
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
-
-
?
chitopentaitol + H2O
?
-
99% of the activity with chitopentaose
-
-
?
chitopentaose + H2O
chitotetraose + glucosamine
-
(GlcN)6 is sequentially cleaved into GlcN5,GlcN4, GlcN3, GlcN2, and GlcN, glucosamine is the final product
-
-
?
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 + chitotriose
-
products at an early stage of reaction
-
-
?
chitotriitol + H2O
D-glucosamine + ?
-
85% of the activity with chitopentaitol
-
-
?
chitotriose + H2O
D-glucosamine + chitobiose
-
products at an early stage of reaction
-
-
?
colloidal chitin + H2O
D-glucosamine + ?
Penicillium sp. IB-37-2A
-
deacetylation degree 80-85%, 6.4% activity compared to soluble chitosan
-
-
?
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
-
-
?
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
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 + ?
Penicillium sp. IB-37-2A
-
deacetylation degree 80-85%, 100% activity
-
-
?
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
-
-
-
?
chitobiose + H2O
D-glucosamine
-
38% of the activity with chitopentaose
-
-
?
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 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
-
-
?
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
at the early stages of the reaction, chitopentaose is converted to D-glucosamine and chitotetraose
-
-
?
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
?
-
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 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 + ?
Aspergillus fumigatus IIT-004
-
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 + ?
Aspergillus fumigatus IIT-004
-
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
-
-
?
chitotetraitol + H2O
D-glucosamine + ?
-
97% of the activity with chitopentaitol
-
-
?
chitotetraitol + H2O
D-glucosamine + ?
-
97% of the activity with chitopentaitol
-
-
?
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
at the early stages of the reaction, chitotetraose is converted to D-glucosamine and chitotriose
-
-
?
chitotriose + H2O
chitobiose + D-glucosamine
-
(GlcN)6 is sequentially cleaved into GlcN5,GlcN4, GlcN3, GlcN2, and GlcN, glucosamine is the final product
-
-
?
chitotriose + H2O
D-glucosamine
-
92% of the activity with chitopentaose
-
-
?
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
D-glucosamine + ?
-
12% activity compared to crab shell chitosan with more than 90% degree of acetylation
-
-
?
glycol chitosan + H2O
D-glucosamine + ?
Penicillium sp. IB-37-2A
-
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
?
-
Aspergillus fumigatus IIT-004
-
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
-
-
?
additional information
?
-
-
preparation of alpha-chitin and chitosan from shrimp processing raw byproducts
-
-
?
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
-
-
?
additional information
?
-
-
preparation of alpha-chitin and chitosan from shrimp processing raw byproducts
-
-
?
additional information
?
-
-
the enzyme catalyzes transglycosylation reaction on chitobiose and chitotriose
-
-
?
additional information
?
-
-
the enzyme catalyzes transglycosylation reaction on chitobiose and chitotriose
-
-
?
additional information
?
-
Penicillium sp. IB-37-2A
-
no activity with carboxymethyl cellulose, cellulose, xylan and galactomannan
-
-
?
additional information
?
-
-
the enzyme fails to release a reducing sugar from avicel and carboxylmethyl cellulose
-
-
?
additional information
?
-
-
the enzyme fails to release a reducing sugar from avicel and carboxylmethyl cellulose
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme also catalyzes transglycosylation reactions
-
-
?
additional information
?
-
-
the enzyme also catalyzes transglycosylation reactions
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
?
-
-
the enzyme acts on beta-1,4-linkage of chitosan from its non-reducing end and produces D-glucosamine as the exclusive end product
-
-
?
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
EDTA
65% residual activity at 1 mg/ml, complete inhibition at 5 mg/ml
additional information
neither castanospermine nor australine are capable of inhibiting the enzyme at a concentration of 1 mM
-
Ag+
47.9% residual activity at 5 mg/ml, complete inhibition at 10 mg/ml
Mn2+
2.5% residual activity at 5 mg/ml, complete inhibition at 10 mg/ml
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.5
alpha-D-glucosaminyl fluoride
mutant enzyme D139E, at pH 7.0 and 37°C
1.4
GlcN(beta1-4)GlcN(beta1-4)GlcN(beta1-4)GlcN(beta1-4)GlcN
-
pH 7.0, 37°C
additional information
chitosan
Km-value (mg/ml): 0.104 (wild-type enzyme), 0.221 (mutant enzyme E409Q), 0.140 (mutant enzyme E415Q), 0.352 (mutant enzyme D513N), pH 4.0
additional information
additional information
-
Km-value for chitosan is 1.0 mg/ml
-
additional information
additional information
KM-value for high-molecular mass chitosan is 0.16 mg/ml
-
additional information
additional information
-
KM-value for high-molecular mass chitosan is 0.16 mg/ml
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.073
alpha-D-glucosaminyl fluoride
mutant enzyme D139E, at pH 7.0 and 37°C
27
chitohexaose
-
2-amino-2-deoxy-D-glucopyranose split off, pH 5.2, 20°C
97.6
GlcN(beta1-4)GlcN(beta1-4)GlcN(beta1-4)GlcN(beta1-4)GlcN
-
pH 7.0, 37°C
additional information
additional information
kcat for high-molecular mass chitosan is 2832 per min
-
additional information
additional information
-
kcat for high-molecular mass chitosan is 2832 per min
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
69.2
GlcN(beta1-4)GlcN(beta1-4)GlcN(beta1-4)GlcN(beta1-4)GlcN
-
pH 7.0, 37°C
0.0019
alpha-D-glucosaminyl fluoride
mutant enzyme D139A, at pH 7.0 and 37°C
0.0031
alpha-D-glucosaminyl fluoride
mutant enzyme D139S, at pH 7.0 and 37°C
0.021
alpha-D-glucosaminyl fluoride
mutant enzyme D139E, at pH 7.0 and 37°C
0.73
alpha-D-glucosaminyl fluoride
wild type enzyme, at pH 7.0 and 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.175
(1R,2R,3R,7S,7aR)-3-(aminomethyl)hexahydro-1H-pyrrolizine-1,2,7-triol
-
0.00061
(1S,6S,7R,8R)-6-aminooctahydroindolizine-1,7,8-triol
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.005
-
crude extract, using 4-nitrophenyl beta-D-glucoside as substrate, at pH 7.0, 37°C
0.046
-
purified enzyme, using 4-nitrophenyl beta-D-glucoside as substrate, at pH 7.0, 37°C
additional information
-
real-time MS as high sensitivity method to measure chitosanase activity quickly and with low substrate concentration, simultaneous detection of substrate and product
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
5.8
-
electrospun polyacrylonitrile nanofibrous membranes-immobilized enzyme
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 4.5
-
pH 3.5: about 60% of maximal activity, pH 4.5: about 50% of maximal activity
4 - 6
-
pH 4.0: about 55% of maximal activity, pH 6.0: about 60% of maximal activity
4 - 8
the recombinant enzyme expressed in Escherichia coli shows about 40% activity at pH 4.0, about 80% activity at pH 5.0, 100% activity at pH 5.5, about 90% activity at pH 6.0, and about 20% activity at pH 8.0. The recombinant enzyme expressed in Pichia pastoris shows about 70% activity at pH 4.0, about 90% activity at pH 5.0, 100% activity at pH 5.5, about 95% activity at pH 6.0, and about 20% activity at pH 8.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
50
60
50
-
electrospun polyacrylonitrile nanofibrous membranes-immobilized enzyme
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
-
30°C: about 70% of maximal activity, 60°C: about 45% of maximal activity
30 - 70
-
30°C: about 40% of maximal activity, 70°C: about 75% of maximal activity
37 - 100
37°C: about 20% of maximal activity, 100°C: about 20% of maximal activity
40 - 60
the recombinant enzyme expressed in Escherichia coli shows more than 45% activity between 40 and 60°C. The recombinant enzyme expressed in Pichia pastoris shows more than 70% activity between 40 and 60°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
screening of natural sources and isolation and identification of Penicillium decumbens strain CFRNT15 with exo-beta-D-glucosaminidase activity
-
-
brenda
screening of natural sources and isolation and identification of Penicillium decumbens strain CFRNT15 with exo-beta-D-glucosaminidase activity
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
of cells grown in medium with chitosan
brenda
additional information
additional information
-
solid substrate fermentation for enhanced enzyme production, optimized conditions for maximal enzyme production are 22°C, 75% w/w moisture, 120 h fermentation, 5.0% w/w chitosan, 0.05% w/w CaCl2, 0.5% w/w MgSO4, and 15.1% w/v inoculum
brenda
additional information
-
solid substrate fermentation for enhanced enzyme production, optimized conditions for maximal enzyme production are 22°C, 75% w/w moisture, 120 h fermentation, 5.0% w/w chitosan, 0.05% w/w CaCl2, 0.5% w/w MgSO4, and 15.1% w/v inoculum
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (2068 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
105000
93000
predicted molecular mass from atomic model, confirmed by SDS-PAGE of recombinant scxA gene product lacking carbohydrate-binding module
100000
x * 100000, the recombinant Gls93 has the two molecular forms, ca. 105000 Da and 100000 Da, whose difference is caused by N-glycosylation, SDS-PAGE
105000
x * 105000, the recombinant Gls93 has the two molecular forms, ca. 105000 Da and 100000 Da, whose difference is caused by N-glycosylation, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
x * 100000, the recombinant Gls93 has the two molecular forms, ca. 105000 Da and 100000 Da, whose difference is caused by N-glycosylation, SDS-PAGE
?
x * 105000, the recombinant Gls93 has the two molecular forms, ca. 105000 Da and 100000 Da, whose difference is caused by N-glycosylation, SDS-PAGE
?
-
x * 100000, the recombinant Gls93 has the two molecular forms, ca. 105000 Da and 100000 Da, whose difference is caused by N-glycosylation, SDS-PAGE
-
?
-
x * 105000, the recombinant Gls93 has the two molecular forms, ca. 105000 Da and 100000 Da, whose difference is caused by N-glycosylation, SDS-PAGE
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
the recombinant Gls93 has the two molecular forms, ca. 105000 Da and 100000 Da, whose difference is caused by N-glycosylation
glycoprotein
-
the recombinant Gls93 has the two molecular forms, ca. 105000 Da and 100000 Da, whose difference is caused by N-glycosylation
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
E541A mutant in complex with a natural β-1,4-D-glucosamine tetrasaccharide substrate and both E541A and D469A mutants in complex with a pNP-beta-D-glucosaminide synthetic substrate
sitting drop vapor diffusion method, using 10% (w/v) PEG 6000, 0.1 M HEPES/NaOH (pH 7.5) and 5% (w/v) 2-methyl-2,4-pentanediol
in complex with D-glucosamine, sitting drop vapor diffusion method, using in 100 mM Tris-HCl (pH 8.5) and 20% (w/v) polyethylene glycol 1000
-
hanging drop vapor diffusion method, using 14% (w/v) PEG 8000 and 0.2 M ammonium acetate in 0.1 M cacodylate buffer pH 7.0 for enzyme form Gls93-F1 or 20% (w/v) PEG 4000 and 0.2 M sodium isothiocyanate for enzyme form Gls93-F2
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D469A
F769W
D139A
the mutation significantly decreases the hydrolytic activity compared to the wild type enzyme. The mutant enzyme exclusively exhibits glycosynthase activity using alpha-D-glucosaminyl fluoride and D-glucosamine as substrates
D139E
compared with the wild type, the hydrolytic activity of the mutant is significantly suppressed (less than 0.1%), and the fluoride release activity also decreases to less than 3%
D139S
the mutation significantly decreases the hydrolytic activity compared to the wild type enzyme
D143A
the mutation significantly decreases the hydrolytic activity compared to the wild type enzyme
E555A
the mutation significantly decreases the hydrolytic activity compared to the wild type enzyme
D139A
-
the mutation significantly decreases the hydrolytic activity compared to the wild type enzyme. The mutant enzyme exclusively exhibits glycosynthase activity using alpha-D-glucosaminyl fluoride and D-glucosamine as substrates
-
D139E
-
compared with the wild type, the hydrolytic activity of the mutant is significantly suppressed (less than 0.1%), and the fluoride release activity also decreases to less than 3%
-
D139S
-
the mutation significantly decreases the hydrolytic activity compared to the wild type enzyme
-
D143A
-
the mutation significantly decreases the hydrolytic activity compared to the wild type enzyme
-
E555A
-
the mutation significantly decreases the hydrolytic activity compared to the wild type enzyme
-
E181Q
D464A
specific acitivity is 0.44% compared to the activity of the wild-type enzyme
D464N
specific acitivity is 1.9% compared to the activity of the wild-type enzyme
D513N
specific acitivity is 72% compared to the activity of the wild-type enzyme
D655N
specific acitivity is 103% compared to the activity of the wild-type enzyme
E409Q
specific acitivity is 77% compared to the activity of the wild-type enzyme
E415Q
specific acitivity is 53% compared to the activity of the wild-type enzyme
E470Q
specific acitivity is 99% compared to the activity of the wild-type enzyme
F769W
the mutation significantly enhances the specific activity and hydrolysis velocity compared to the wild type enzyme
F769W
Aspergillus oryzae FL402
-
the mutation significantly enhances the specific activity and hydrolysis velocity compared to the wild type enzyme
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 8
Penicillium sp. IB-37-2A
-
the enzyme demonstrates high pH stability at pH 3.0-8.0, and it loses more than 50% of its original activity at pH values above 8.0
752333
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
55
Penicillium sp. IB-37-2A
-
the enzyme demonstrates high temperature stability at 30-55°C and is almost inactive at 65°C
60
50
the recombinant enzyme from Pichia pastoris remains about 80% activity after 25 h at 50°C, while the recombinant enzyme from Escherichia coli is completely inactive (0.48% residual activity) after 3 h at 50°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
electrospun polyacrylonitrile nanofibrous membranes-immobilized enzyme retains more than 50% of its catalytic activity after 10 batches of uses in aqueous solution
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
25°C, electrospun polyacrylonitrile nanofibrous membranes-immobilized enzyme, 30 days, 40% loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
acetone fractionation, DEAE Sepharose column chromatography, CM-Sepharose column chromatography, and Superdex 200 gel filtration
-
ammonium sulfate precipitation, Q-Sepharose column chromatography, phenyl Sepharose column chromatography, and Sephacryl S-100 gel filtration
native enzyme by cation-exchange chromatography from chitosan-grown cells
-
Ni-NTA column chromatography, HiTrap Q column chromatography and Superdex 200 gel filtration
recombinant enzyme
SP-Sepharose ion exchange chromatography followed by hydroxyapatite column chromatography
-
ultrafiltration, affinity sorption on colloidal chitosan and hydrophobic chromatography on phenyl-Sepharose CL 4B
Penicillium sp. IB-37-2A
-
Ni-NTA column chromatography, HiTrap Q column chromatography and Superdex 200 gel filtration
-
Ni-NTA column chromatography, HiTrap Q column chromatography and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta (DE3)pLysS cells
expressed in Pichia pastoris GS115 cells and Escherichia coli Rosetta (DE3) pLysS cells
Streptomyces lividans TK-24 with shuttle vector pFD666, M14 medium, pH 4.2
-
the His-tagged enzyme His-csx is expressed in Escherichia coli BL21(DE3) cells
wild type and mutant enzymes are expressed in Escherichia coli BL21(DE3) cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
efficient tool for industrial production of glucosamine monosaccharide
synthesis
-
enzymatic formation of chitooligosaccharides by transglycosylation
synthesis
-
production of N-acetylglucosamine from chitosan by enzymatic degradation
synthesis
-
production of N-acetylglucosamine from chitosan by enzymatic degradation
synthesis
-
enzymatic formation of chitooligosaccharides by transglycosylation
-
synthesis
Chryseobacterium indologenes HANYOO
-
production of N-acetylglucosamine from chitosan by enzymatic degradation
-
synthesis
Comamonas koreensis HANWOO
-
production of N-acetylglucosamine from chitosan by enzymatic degradation
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Biosci. Biotechnol. Biochem.
64
1896-1902
2000
Aspergillus oryzae, Aspergillus oryzae IAM2660
brenda
Uchida, Y.; Takeda, H.; Ohkuma, A.; Seki, K.
Purification and properties of exo-beta-D-glucosaminidase from Penicillium sp. and its applications
Adv. Chitin Sci.
2
244-249
1997
Penicillium sp., Penicillium sp. AF9-P-112
-
brenda
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
Appl. Environ. Microbiol.
64
890-895
1998
Trichoderma reesei, Trichoderma reesei PC-3-7
brenda
Ike, M.; Isami, K.; Tanabe, Y.; Nogawa, M.; Ogasawara, W.; Okada, H.; Morikawa, Y.
Cloning and heterologous expression of the exo-beta-D-glucosaminidase-encoding gene (gls93) from a filamentous fungus, Trichoderma reesei PC-3-7
Appl. Microbiol. Biotechnol.
72
687-695
2006
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
Biochem. J.
394
675-686
2006
Amycolatopsis orientalis (Q56F26), Amycolatopsis orientalis
brenda
Matsumura, S.; Yao, E.; Toshima, K.
One-step preparation of alkyl beta-D-glucosaminide by the transglycosylation of chitosan and alcohol using purified exo-beta-D-glucosaminidase
Biotechnol. Lett.
21
451-456
1999
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
1064-1072
2006
Amycolatopsis orientalis
brenda
Fukamizo, T.; Brzezinski, R.
Structure and function of exo-beta-glucosaminidase from Amycolatopsis orientalis
J. Appl. Glycosci.
54
133-138
2007
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
J. Bacteriol.
185
5175-5181
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
J. Biol. Chem.
265
10088-10094
1990
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
J. Microbiol. Biotechnol.
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
Protein Expr. Purif.
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
J. Biotechnol.
134
253-260
2008
Amycolatopsis orientalis
brenda
van Bueren, A.L.; Ghinet, M.G.; Gregg, K.; Fleury, A.; Brzezinski, R.; Boraston, A.B.
The structural basis of substrate recognition in an exo-beta-D-glucosaminidase involved in chitosan hydrolysis
J. Mol. Biol.
385
131-139
2009
Amycolatopsis orientalis (Q56F26), Amycolatopsis orientalis
brenda
Sakamoto, Y.; Ike, M.; Tanaka, N.; Suzuki, Y.; Ogasawara, W.; Okada, H.; Nonaka, T.; Morikawa, Y.; Nakamura, K.T.
Crystallization and preliminary X-ray crystallographic studies of an exo-beta-D-glucosaminidase from Trichoderma reesei
Acta Crystallogr. Sect. F
66
309-312
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
Carbohydr. Res.
344
1046-1049
2009
Aspergillus sp. (C3U4R9)
brenda
Pluvinage, B.; Ghinet, M.G.; Brzezinski, R.; Boraston, A.B.; Stubbs, K.A.
Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine-configured castanospermine and an amino-australine analogue
Org. Biomol. Chem.
7
4169-4172
2009
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
Glycobiology
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
Carbohydr. Polym.
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
J. Mol. Catal. B
55
55-60
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
6
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
Biochem. J.
473
463-472
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
Int. J. Biol. Macromol.
112
1115-1121
2018
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
J. Biol. Chem.
292
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
J. Microbiol. Biotechnol.
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
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