Information on EC 3.2.1.53 - beta-N-acetylgalactosaminidase

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

EC NUMBER
COMMENTARY hide
3.2.1.53
-
RECOMMENDED NAME
GeneOntology No.
beta-N-acetylgalactosaminidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-beta-D-galactosaminides
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
beta-N-acetyl-D-galactosaminide N-acetylgalactosaminohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9054-43-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
AT173-1
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-
Manually annotated by BRENDA team
Bacillus sp. AT173-1
AT173-1
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
desert and oasis flies studied, male and female, Neot Hakikar (oasis), Jordan Valley spring (wet), Kfar Adumim starved (arid), Jordan Valley autumn (arid)
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-
Manually annotated by BRENDA team
rat
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-
Manually annotated by BRENDA team
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-N-acetylgalactosaminide + H2O
4-methylumbelliferone + N-acetyl-beta-D-galactosamine
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-N-acetylgalactosaminide + H2O
4-methylumbelliferone + N-acetyl-beta-D-galactosamine
show the reaction diagram
4-nitrophenyl beta-N-acetylglucosaminide + H2O
beta-N-acetylglucosamine + 4-nitrophenol
show the reaction diagram
1-3% of the activity with 4-nitrophenyl beta-N-acetylgalactosaminide
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-
?
4-nitrophenyl N-acetyl-beta-D-galactosaminopyranoside + H2O
N-acetyl-D-galactosamine + 4-nitrophenol
show the reaction diagram
-
-
-
?
4-nitrophenyl-N-acetyl-beta-D-galactosaminide + H2O
4-nitrophenol + N-acetyl-beta-D-glucosamine
show the reaction diagram
-
activity measured in whole fly homogenates, substrate concentration of 6 mM in citrate buffer, flies of arid regions tend to produce more beta-N-acetylgalactosaminidase than those originating in sugar-rich environments
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-
?
beta-N-acetylgalactosaminylated oligosaccharides + H2O
?
show the reaction diagram
beta-phenyl-N-acetylgalactosamines + H2O
?
show the reaction diagram
-
substrate specificity 85%
-
-
?
GalNAc-beta-1,3-Gal-alpha-1,4-Gal-beta-1,4-Glc-beta-1,1-Cer + H2O
GalNAc + Gal-alpha-1,4-Gal-beta-1,4-Glc-beta-1,1-Cer
show the reaction diagram
i.e. globotetraosylceramide, 39% of the activity with GalNAc-1,4-Gal-1,4-Glc-1,1-Cer
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-
?
GalNAc-beta-1,4-Gal-beta-1,4-Glc-beta-1,1-Cer
GalNAc + Gal-beta-1,4-Glc-beta-1,1-Cer
show the reaction diagram
i.e. asialo-GM2
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-
?
N-acetyl-beta-D-galactosaminides + H2O
?
show the reaction diagram
N-acetyl-beta-D-galactosaminides + H2O
N-acetyl-D-galactosamine + an alcohol
show the reaction diagram
p-nitrophenyl beta-N-acetylgalactosaminide + H2O
?
show the reaction diagram
additional information
?
-
enzyme cleaves the nonreducing terminal beta-GalNAc residues of gangliotriaosylceramide and globotetraosylceramide. Enzyme prefers the GalNAc-1,4-linkage over the GalNAc-1,3-linkage
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-N-acetylgalactosaminylated oligosaccharides + H2O
?
show the reaction diagram
N-acetyl-beta-D-galactosaminides + H2O
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
relative activity in presence of MgSO4 10 mM 104%
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AgNO3
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-
Fe2+
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enzyme activity completely inhibited in the presence of 10 mM FeSO4
Hg2+
5 mM, strong inhibition
mannose
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inhibition of beta-N-acetylgalactosaminidase but activation of alpha-N-acetylgalactosaminidase, three concentrations of 10, 50, and 100 mM tested
methyl 2,5-dideoxy-2,5-imino-D-allonamide
methyl 2,5-dideoxy-2,5-imino-D-mannonamide
methyl 2,5-dideoxy-2,5-imino-D-talonamide
methyl 2,5-dideoxy-2,5-imino-L-gulonamide
N-acetylgalactosamine
N-acetylgalactosaminide thiazoline
competitive
N-acetylglucosamine
N-acetylglucosaminide thiazoline
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Ni2+
5 mM, strong inhibition
p-hydroxymercuribenzoate
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-
Urea
-
relative activity in presence of 2 M 32%
Zn2+
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enzyme activity completely inhibited in the presence of 10 mM ZnSO4
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
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-
N-ethylmaleimide
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1mM solution increase the reaction rates 2-3fold
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.42
4-methylumbelliferyl beta-N-acetylgalactosaminide
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-
0.09 - 1.74
4-nitrophenyl beta-N-acetylgalactosaminide
0.35 - 1
p-nitrophenyl beta-acetylgalactosaminide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 7.3
4-nitrophenyl beta-N-acetylgalactosaminide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 20.9
4-nitrophenyl beta-N-acetylgalactosaminide
8925
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000013
N-acetylgalactosaminide thiazoline
pH 6.0, 37C
0.0468
N-acetylglucosaminide thiazoline
pH 6.0, 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0028 - 0.0095
methyl 2,5-dideoxy-2,5-imino-D-allonamide
0.00035 - 0.001
methyl 2,5-dideoxy-2,5-imino-D-mannonamide
0.0036 - 0.025
methyl 2,5-dideoxy-2,5-imino-D-talonamide
0.0073 - 0.026
methyl 2,5-dideoxy-2,5-imino-L-gulonamide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15.4
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-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
p-nitrophenyl beta-N-acetylgalactosaminide
6.6
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assay at, pH-optimum estimated for
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
not active below, p-nitrophenyl beta-N-acetylgalactosaminide
5.5 - 9.5
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enzyme retains more than 80% activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 45
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enzyme gradually inactivated in solution at 4C, reactivated by incubation with DTT
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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whole fly homogenates
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
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SDS-PAGE, enzyme denatured with SDS and 2-mercaptoethanol
54000
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native enzyme, gel filtration
82000
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sucrose density gradient centrifugation
115000
x * 115000, SDS-PAGE
210000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 115000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
cysteine, stabilization
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dithiothreitol, stabilization
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
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inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20 C, inactivation after several weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D607E
Km is increased by 5-fold, the kcat is decreased to 1.4% of wild-type
D607N
activity is completely abolished
E608D
Km value is decreased to about 57% and the kcat value is decreased to about 5.2% of wild-type
E608Q
Km value is decreased to about 26% and the kcat value is decreased to about 1.1% of wild-type
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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comparison of glycolytic and chitinolytic enzyme activities between desert and oasis flies of Phlebotomus papatasi to evaluate potential differences in susceptibility to infection with Leishmania major