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Information on EC 3.2.1.165 - exo-1,4-beta-D-glucosaminidase and Organism(s) Amycolatopsis orientalis and UniProt Accession Q56F26

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IUBMB 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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This record set is specific for:
Amycolatopsis orientalis
UNIPROT: Q56F26
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The taxonomic range for the selected organisms is: Amycolatopsis orientalis
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
exo-beta-D-glucosaminidase
-
exo-beta-D-glucosaminidase
-
-
exo-beta-glucosaminidase
-
-
exochitosanase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
-
cleaving 2-amino-2-deoxy-D-glucopyranose off oligosaccharides
transglycosylation
-
only at high substrate concentrations
PATHWAY SOURCE
PATHWAYS
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].
CAS REGISTRY NUMBER
COMMENTARY hide
9012-33-3
c.f. EC 3.2.1.52
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
-
-
?
beta-1,4-D-glucosamine tetrasaccharide
D-glucosamine + chitotriose
show the reaction diagram
tetrasaccharide of chitosan efficiently depolymerizes chitosan to its constituent p-glucosamine monosaccharide in cooperation with endo-chitosanase
-
-
?
chitobiose + H2O
D-glucosamine
show the reaction diagram
-
-
-
?
chitohexaose + H2O
D-glucosamine + ?
show the reaction diagram
-
-
-
?
chitopentaose + H2O
D-glucosamine + ?
show the reaction diagram
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
?
chitosan + H2O
D-glucosamine + ?
show the reaction diagram
-
-
-
?
chitotetraose + H2O
?
show the reaction diagram
-
-
-
?
chitotriose + H2O
?
show the reaction diagram
-
-
-
?
p-nitrophenyl beta-D-glucosaminide + H2O
p-nitrophenol + beta-D-glucosamine
show the reaction diagram
-
-
-
?
p-nitrophenyl-beta-D-glucosamine + H2O
D-glucosamine + p-nitrophenol
show the reaction diagram
-
-
-
?
chitobiitol + H2O
?
show the reaction diagram
-
0.3% of the activity with chitopentaose
-
-
?
chitobiose + H2O
D-glucosamine
show the reaction diagram
chitohexaitol + H2O
?
show the reaction diagram
-
94% of the activity with chitopentaose
-
-
?
chitohexaose + H2O
2-amino-2-deoxy-D-glucopyranose + chitopentaose
show the reaction diagram
-
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
D-glucosamine
show the reaction diagram
-
92% of the activity with chitopentaose
-
-
?
chitopentaitol + H2O
?
show the reaction diagram
-
99% of the activity with chitopentaose
-
-
?
chitopentaose + H2O
D-glucosamine
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
90% of the activity with chitopentaose
-
-
?
chitotetraitol + H2O
?
show the reaction diagram
-
as active as chitopentaose
-
-
?
chitotetraose + H2O
?
show the reaction diagram
-
-
-
-
?
chitotetraose + H2O
D-glucosamine
show the reaction diagram
chitotriitol + H2O
?
show the reaction diagram
-
85% of the activity with chitopentaose
-
-
?
chitotriose + H2O
D-glucosamine
show the reaction diagram
-
92% of the activity with chitopentaose
-
-
?
GlcNbeta(1-4)GlcNAc + H2O
D-glucosamine + N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcNAc + H2O
GlcNbeta(1-4)GlcNbeta(1-4)GlcNAc + D-glucosamine
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-1,4-D-glucosamine tetrasaccharide
D-glucosamine + chitotriose
show the reaction diagram
tetrasaccharide of chitosan efficiently depolymerizes chitosan to its constituent p-glucosamine monosaccharide in cooperation with endo-chitosanase
-
-
?
chitosan + H2O
D-glucosamine + ?
show the reaction diagram
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
additional information
neither castanospermine nor australine are capable of inhibiting the enzyme at a concentration of 1 mM
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
27
chitohexaose
-
2-amino-2-deoxy-D-glucopyranose split off, pH 5.2, 20°C
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
of cells grown in medium with chitosan
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
EBDG_AMYOR
1032
1
110633
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110557
x * 110557, calculated from sequence
93000
predicted molecular mass from atomic model, confirmed by SDS-PAGE of recombinant scxA gene product lacking carbohydrate-binding module
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 110557, calculated from sequence
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D469A
catalytic acid/base
E541A
catalytic nucleophile
D469A
-
inactive mutant enzyme
D469E
-
inactive mutant enzyme
E541D
-
inactive mutant enzyme
E541Q
-
inactive mutant enzyme
S468N/D469E
-
inactive mutant enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from culture supernatant
SP-Sepharose ion exchange chromatography followed by hydroxyapatite column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Streptomyces lividans
Streptomyces lividans TK-24 with shuttle vector pFD666, M14 medium, pH 4.2
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
efficient tool for industrial production of glucosamine monosaccharide
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Fukamizo, T.; Brzezinski, R.
Structure and function of exo-beta-glucosaminidase from Amycolatopsis orientalis
J. Appl. Glycosci.
54
133-138
2007
Amycolatopsis orientalis
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team