Information on EC 3.2.1.201 - (1->4)-2-acetamido-2-deoxy-beta-D-glucan diacetylchitobiohydrolase (non-reducing end)

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
3.2.1.201
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RECOMMENDED NAME
GeneOntology No.
(1->4)-2-acetamido-2-deoxy-beta-D-glucan diacetylchitobiohydrolase (non-reducing end)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of N,N'-diacetylchitobiose from the reducing end of chitin and chitodextrins
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
chitin degradation III (Serratia)
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SYSTEMATIC NAME
IUBMB Comments
(1->4)-2-acetamido-2-deoxy-beta-D-glucan diacetylchitobiohydrolase (reducing end)
The enzyme hydrolyses the second glycosidic (1->4) linkage from reducing ends of chitin and chitodextrin molecules, liberating N,N'-diacetylchitobiose disaccharides. cf. EC 3.2.1.200, exo-chitinase (non-reducing end).
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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-beta-D-N,N'-diacetylchitobioside + H2O
4-methylumbelliferone + N,N'-diacetylchitobiose
show the reaction diagram
alpha-chitin + H2O
?
show the reaction diagram
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activity is positively correlated to a decline in particle size and crystallinity of alpha-chitin, generated using a converge mill
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?
beta-chitin + H2O
?
show the reaction diagram
chitin + H2O
N,N'-diacetylchitobiose
show the reaction diagram
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sole product of the N-terminal catalytic domain, the domain mainly hydrolyzes the second glycosidic bond from the nonreducing end of the oligomers
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?
chitosan + H2O
N,N'-diacetylchitobiose
show the reaction diagram
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?
colloidal chitin + H2O
N,N'-diacetylchitobiose
show the reaction diagram
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?
ethylene glycol chitin + H2O
N,N'-diacetylchitobiose
show the reaction diagram
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
0.2-1 mM, 110% of initial activity
NaCl
0.2-1 mM, 110% of initial activity
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62.7
substrate chitin, N-terminal catalytic domain, pH 5.0, 80°C
477
substrate ethylene glycol chitin, N-terminal catalytic domain, pH 5.0, 80°C
2490
substrate colloidal chitin, N-terminal catalytic domain, pH 5.0, 80°C
3160
substrate chitosan, 70% deacetylated, N-terminal catalytic domain, pH 5.0, 80°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ChiA comprises an N-terminal domain, a catalytic (beta/alpha)8 barrel domain and a small (alpha +beta) domain, which is inserted into the (beta/alpha)8 barrel domain. The cocrystallized chito-oligosaccharide is inserted into the catalytic cleft from the reducing end when digested by ChiB
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ChiA crystallizes both by salting-in and salting-out in the presence of a variety of precipitating agents in a wide range of concentrations and pH values
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
stable for 60 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
protein precipitates at concentrations higher than 10 mg/ml in a variety of pH and ionic strength values
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ChiA binds nonspecifically polysaccharides, which are found in the growth medium. These sugar impurities have to be removed during the purification process
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture