Information on EC 3.2.1.49 - alpha-N-acetylgalactosaminidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
3.2.1.49
-
RECOMMENDED NAME
GeneOntology No.
alpha-N-acetylgalactosaminidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids
show the reaction diagram
-
-
-
-
Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids
show the reaction diagram
the enzyme exhibits an endo-enzyme activity in addition to an exo-activity
-
Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids
show the reaction diagram
double-displacement mechanism. First step: an oxygen atom from Asp140 attacks the electrophilic C1 of the hexose ring, cleaving the glycosidic linkage and creating a covalent enzyme-substrate intermediate. The second step involves a nucleophilic attack by a water molecule, which has been deprotonated by Asp201, on the covalent intermediate.
-
Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids
show the reaction diagram
double-displacement, or ping-pong, reaction mechanism and active site structure, overview
-
Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids
show the reaction diagram
a hydride at C3, activated by the interaction of the OH-3 hydroxyl with the conserved His228, is abstracted by NAD+ with oxidation of the OH-3 hydroxyl to a ketone. This activates H2 for proton abstraction by Tyr179, accompanied by elimination of the aglycone, thereby generating a 1,2-unsaturated intermediate. Water is then added to the anomeric center, followed by the reduction of the C3 ketone by the on-board NADH, completing the catalytic sequence and restoring NADH to NAD+ and the enzyme to its starting state to bind another substrate
A4Q8F7
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Glycosphingolipid biosynthesis - globo series
-
SYSTEMATIC NAME
IUBMB Comments
alpha-N-acetyl-D-galactosaminide N-acetylgalactosaminohydrolase
The human lysosomal enzyme is involved in the degradation of blood type A epitope.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-acetamido-2-deoxy-alpha-D-galactoside acetamidodeoxygalactohydrolase
-
-
-
-
4-nitrophenyl-alpha-N-acetylgalactosaminidase
-
-
-
-
AglA
A2QL72
gene name
alpha-acetylgalactosaminidase
-
-
-
-
alpha-galactosidase B
-
-
-
-
alpha-galactosidase B
-
-
alpha-GalNAc
-
-
alpha-GalNAcase
-
-
alpha-GalNAcase I
-
-
alpha-GalNAcase I
-
-
alpha-GalNAcase II
-
-
alpha-GalNAcase II
-
-
alpha-N-acetylgalactosaminidase blood group A2 degrading enzyme
-
-
alpha-N-galactosaminidase IV
-
-
alpha-N-galactosaminidase IV
Arenibacter latericius KMM 426
-
-
-
alpha-NAGA
-
-
alpha-NAGAL
-
-
alpha-NAGAL
P17050
-
alpha-NaGalase
-
-
envelope glycoprotein gp160
-
-
exo-alpha-N-acetylgalactosaminidase
-
-
-
-
N-acetyl-alpha-D-galactosaminidase
-
-
-
-
N-acetyl-alpha-galactosaminidase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9075-63-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
squid, two isozymes alpha-GalNAcase I and alpha-GalNAcase II
-
-
Manually annotated by BRENDA team
Arenibacter latericius KMM 426
KMM 426
-
-
Manually annotated by BRENDA team
bifunctional alpha-galactosidase and alpha-N-acetylgalactosaminidase
UniProt
Manually annotated by BRENDA team
bifunctional alpha-N-acetylgalactosaminidase and alpha-N-acetylgalactosidase
UniProt
Manually annotated by BRENDA team
strain CCIM K2, best producer of alpha-N-acetylgalactosaminase
-
-
Manually annotated by BRENDA team
Aspergillus niger CCIM
strain CCIM K2, best producer of alpha-N-acetylgalactosaminase
-
-
Manually annotated by BRENDA team
member of glycosyl hydrolase family 109
UniProt
Manually annotated by BRENDA team
Eremoplastron bovis
-
-
-
Manually annotated by BRENDA team
i.e. HIV-1, constitutive enzyme
-
-
Manually annotated by BRENDA team
skipjack tuna
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
enzyme deficiency in Fabry disease causes globotriaosylceramide accumulation in the liver, kidneys, and heart of Fabry patients, phenotype, overview. Wild-type enzyme intravenously injected into Fabry model mice prevents the globotriaosylceramide storage and improves the pathological changes in the organs, overview
malfunction
-
deficiency of alpha-NAGAL activity results in the lysosomal storage disorders Schindler disease and Kanzaki disease, molecular basis, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-nitrophenyl-alpha-D-galactoside + H2O
2-nitrophenol + alpha-D-galactose
show the reaction diagram
A2QL72
-
-
-
?
2-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
2-nitrophenol + alpha-N-acetylgalactosamine
show the reaction diagram
G5D7B5
-
-
-
?
2-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
2-nitrophenol + alpha-N-acetylgalactosamine
show the reaction diagram
A2QL72
-
-
-
?
2-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
2-nitrophenol + alpha-N-acetylgalactosamine
show the reaction diagram
A4Q8F7
-
-
-
?
2-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
2-nitrophenol + alpha-N-acetylgalactosamine
show the reaction diagram
Aspergillus niger, Aspergillus niger CCIM
-
enzyme acts with retention of the anomeric configuration
-
-
?
4-methylumbelliferyl-alpha-D-galactopyranoside + H2O
4-methylumbelliferone + alpha-D-galactopyranose
show the reaction diagram
-
-
-
-
-
4-methylumbelliferyl-alpha-D-galactopyranoside + H2O
4-methylumbelliferone + alpha-D-galactopyranose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-alpha-D-galactopyranoside + H2O
4-methylumbelliferone + alpha-D-galactopyranose
show the reaction diagram
P17050
substrate of engineered enzyme mutant S188E/A191L, not of the wild-type enzyme
-
-
?
4-methylumbelliferyl-alpha-D-galactosaminide + H2O
4-methylumbelliferone + alpha-D-galactosamine
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-N-acetylgalactosaminide + H2O
4-nitrophenol + N-acetyl-D-galactosamine
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-N-acetylgalactosaminide + H2O
4-nitrophenol + N-acetyl-D-galactosamine
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-N-acetylgalactosaminide + H2O
4-nitrophenol + N-acetyl-D-galactosamine
show the reaction diagram
-
substrate binding and active site structure, active-site interactions and ligand binding, overview. Inactive enzyme conformation, overview
-
-
?
4-nitrophenyl-N-acetyl-alpha-D-galactosamide + H2O
4-nitrophenol + N-acetyl-alpha-D-galactosamine
show the reaction diagram
-
-
-
-
?
blood group A glycoconjugate + H2O
?
show the reaction diagram
-
alpha-N-acetylgalactosaminidase blood group A2 degrading activity, substrate from human erythrocytes and plasma, alpha-N-acetylgalactosaminidase blood group A2 degrading activity, substrate from human and murine erythrocytes and plasma
-
-
?
Forssman hapten + H2O
?
show the reaction diagram
-
-
-
-
?
Forssman hapten + H2O
?
show the reaction diagram
-
-
-
-
?
Forssman hapten + H2O
?
show the reaction diagram
-
-
-
-
-
Forssman hapten + H2O
?
show the reaction diagram
-
-
-
-
?
GalNAc-alpha-1,3-GalNAc-beta-1,3-Gal-alpha-1,4-Gal-beta-1,4-Glc-beta-1,1-ceramide + H2O
alpha-N-acetylgalactosamine + GalNAc-beta-1,3-Gal-alpha-1,4-Gal-beta-1,4-Glc-beta-1,1-ceramide
show the reaction diagram
-
i.e. Forssman hapten glycolipid
-
-
?
GalNAc-alpha-1,3-GalNAc-beta-1,3-Gal-alpha-1,4-Gal-beta-1,4-Glc-beta-1,1-ceramide + H2O
alpha-N-acetylgalactosamine + GalNAc-beta-1,3-Gal-alpha-1,4-Gal-beta-1,4-Glc-beta-1,1-ceramide
show the reaction diagram
-
i.e. Forssman hapten glycolipid, production of globoside by both isozymes
-
-
?
GalNAc-alpha1-O-Ser + H2O
?
show the reaction diagram
-
-
-
-
?
GalNAc-alpha1-O-Thr + H2O
?
show the reaction diagram
-
-
-
-
?
o-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
o-nitrophenol + alpha-N-acetylgalactosamine
show the reaction diagram
-
-
-
-
?
o-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
o-nitrophenol + alpha-N-acetylgalactosamine
show the reaction diagram
-
-
-
-
?
o-nitrophenyl-N-acetyl-alpha-D-galactosaminide + H2O
o-nitrophenol + N-acetyl-alpha-D-galactosamine
show the reaction diagram
-
-
-
-
?
o-nitrophenyl-N-acetyl-alpha-D-galactosaminide + H2O
o-nitrophenol + N-acetyl-alpha-D-galactosamine
show the reaction diagram
-
substrate from the blood type A2 antigen producing H antigen, blood type O
-
-
?
ovine submaxillary asialoglycoprotein + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl 2-acetamide-2-deoxy-3-O-(beta-D-galactopyranosyl)-alpha-D-galactopyranoside + H2O
p-nitrophenol + 2-acetamide-2-deoxy-3-O-(beta-D-galactopyranosyl)-alpha-D-galactopyranoside
show the reaction diagram
-
-
-
-
?
p-nitrophenyl alpha-D-galactopyranoside + H2O
p-nitrophenol + alpha-D-galactopyranose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl N-acetyl-alpha-D-galactosaminide + H2O
p-nitrophenol + N-acetyl-alpha-D-galactosamine
show the reaction diagram
-
-
-
-
?
p-nitrophenyl N-acetyl-alpha-D-galactosaminide + H2O
p-nitrophenol + N-acetyl-D-galactosamine
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-2-deoxy-alpha-D-galactopyranoside + H2O
p-nitrophenol + 2-deoxy-alpha-D-galactopyranose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-N-acetyl-D-galactoaminide + H2O
p-nitrophenol + alpha-N-acetyl-D-galactosamine
show the reaction diagram
-
the Hep-G2 cell lysate hydrolyzes the exo-type substrate
-
-
?
p-nitrophenyl-alpha-N-acetyl-D-galactosaminide + H2O
p-nitrophenol + alpha-N-acetyl-D-galactosamine
show the reaction diagram
Arenibacter latericius, Arenibacter latericius KMM 426
-
-
-
-
?
p-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
p-nitrophenol + alpha-N-acetylgalactosamine
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
p-nitrophenol + alpha-N-acetylgalactosamine
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
p-nitrophenol + alpha-N-acetylgalactosamine
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-N-acetyl-alpha-D-galactosaminide + H2O
p-nitrophenol + N-acetyl-alpha-D-galactosamine
show the reaction diagram
-
-
-
-
-
p-nitrophenyl-N-acetyl-alpha-D-galactosaminide + H2O
p-nitrophenol + N-acetyl-alpha-D-galactosamine
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-N-acetyl-alpha-D-galactosaminide + H2O
p-nitrophenol + N-acetyl-alpha-D-galactosamine
show the reaction diagram
Q8XNK8
-
-
-
?
phenyl-alpha-N-acetylglucosaminide + H2O
N-acetylgalactosamine + phenol
show the reaction diagram
-
-
-
?
serum vitamin D3-binding protein + H2O
?
show the reaction diagram
-
i.e. Gc protein, the human substrate is the precursor of the principal macrophage activating factor, MAF, the deglycosylated prrecursor cannot be converted, which leads to immunosuppression
-
-
?
serum vitamin D3-binding protein + H2O
?
show the reaction diagram
-
i.e. Gc protein, human substrate, deglycosylation of the substrate
-
-
?
globotriaosylceramide + H2O
?
show the reaction diagram
P17050
wild-type and engineered mutant enzymes
-
-
?
additional information
?
-
-
Gal-beta-GalNAc-alpha-PNP is no substrate for Hep-G2 cell lysate, the enzyme of tumor cell lysate reduces the macrophage activing potency of GcMAF
-
-
-
additional information
?
-
-
the enzyme hydrolyzes the terminal N-actyl-alpha-D-galactosamine from the blood type A2 antigen producing H antigen, blood type O
-
-
-
additional information
?
-
-
the enzyme inactivates the macrophage activing factor produced from Gc protein and this results in reduced phagocytic activity and superoxide-generation capacity of monocytes/macrophages
-
-
-
additional information
?
-
-
the enzyme is highly selective for terminal N-acetylgalactosamine residues
-
-
-
additional information
?
-
-
the enzyme is highly selective for terminal N-acetylgalactosamine residues, sugars other than N-acetyl-alpha-D-galactosaminide are no substrates
-
-
-
additional information
?
-
-
the enzyme is highly selective for terminal N-acetylgalactosamine residues, sugars other than N-acetyl-alpha-D-galactosaminide are not substrates. the enzyme degrades blood A epitope
-
-
-
additional information
?
-
-
enzyme deficiency, due to missense mutations at residue R329 causing structural changes in the enzyme leading to differing substrate specificity, causes the Kanzaki disease, an autosomal recessine storage disorder with accumulation of GalNAcalpha1-O-Ser/Thr in the lysosome and increased urinary excretion of O-linked sialylglycopeptides, phenotype, overview
-
-
-
additional information
?
-
-
the enzyme plays a dual role in regulating both infectivity and immunosuppression, the HIV-1 viral envelope glycoprotein gp160 shows alpha-N-galactosaminidase activity
-
-
-
additional information
?
-
-
alpha-NAGAL is a lysosomal exoglycosidase that cleaves terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids
-
-
-
additional information
?
-
-
the enzyme hydrolyzes alpha-N-acetylgalactosyl residues from glycolipids and glycoproteins
-
-
-
additional information
?
-
P17050
Ser188 and Ala191 play important roles in the recognition of an N-acetylgalactosamine residue in NAGA
-
-
-
additional information
?
-
-
the enzyme also shows activity with 4-nitrophenyl alpha-D-galactosaminide
-
-
-
additional information
?
-
-
the enzyme glycosylizes free serine and threonine residues in the native and the N-tert-butoxycarbonyl-protected analogue protein to gain the Tn antigen. The enzyme catalyzes glycosylations yielding to a series of 2-acetamido-2-deoxy-alpha-D-galactobiosides using 2-acetamido-2-deoxy-D-galactopyranose as a glycosyl donor, identification of isomers alpha-D-GalpNAc-1,6-D-GalpNAc, alpha-D-GalpNAc-1,3-D-GalpNAc, and alpha-D-GalpNAc-1,6-D-GalfNAc
-
-
-
additional information
?
-
A4Q8F7
enzyme efficiently cleaves blood group A antigen. Unusual catalytic mechanism involving NAD+. NagA might adopt a mechanism similar to that of glycosyl hydrolase family 4 enzymes utilizing an oxidation-elimination-addition-reduction sequence
-
-
-
additional information
?
-
A2QL72
preference for alpha-N-acetyl-D-galactosaminide over alpha-D-galactoside. alpha-N-acetylgalactosaminidase activity uses a retaining mechanism
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
serum vitamin D3-binding protein + H2O
?
show the reaction diagram
-
i.e. Gc protein, the human substrate is the precursor of the principal macrophage activating factor, MAF, the deglycosylated prrecursor cannot be converted, which leads to immunosuppression
-
-
?
blood group A glycoconjugate + H2O
?
show the reaction diagram
-
alpha-N-acetylgalactosaminidase blood group A2 degrading activity, substrate from human erythrocytes and plasma
-
-
?
additional information
?
-
-
enzyme deficiency, due to missense mutations at residue R329 causing structural changes in the enzyme leading to differing substrate specificity, causes the Kanzaki disease, an autosomal recessine storage disorder with accumulation of GalNAcalpha1-O-Ser/Thr in the lysosome and increased urinary excretion of O-linked sialylglycopeptides, phenotype, overview
-
-
-
additional information
?
-
-
the enzyme plays a dual role in regulating both infectivity and immunosuppression
-
-
-
additional information
?
-
-
alpha-NAGAL is a lysosomal exoglycosidase that cleaves terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids
-
-
-
additional information
?
-
-
the enzyme hydrolyzes alpha-N-acetylgalactosyl residues from glycolipids and glycoproteins
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
A4Q8F7
binds 1 NAD+ per subunit. The NAD+ cannot dissociate
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
slight activation of both isozymes
Cu2+
-
slight activation of both isozymes
K+
-
slight activation of both isozymes
Mg2+
-
activates
Mg2+
-
slight activation of both isozymes
Na+
-
slight activation of both isozymes
Zn2+
-
slight activation of both isozymes
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,2'-dianisidine
-
2 mM, 70% of original activity
Acetylimidazole
-
5 mM, 30% of original activity
Ag+
-
isoenzyme II
Ag+
-
moderate inhibition of isozyme alpha-GalNAcase I, strong inhibition of isozyme alpha-GalNAcase II
Ca2+
-
1 mM, complete loss of activity
carbodiimide
-
1.8 mM, complete loss of activity
Cu2+
-
isoenzyme II
D-galactose
-
isoenzyme I
D-galactose
-
-
D-galactose
-
about 10% inhibition of isozymes alpha-GalNAcase I and isozyme alpha-GalNAcase II
D-glucose
-
-
Diethylpyrocarbonate
-
2 mM, 60% of original activity
Fe2+
-
-
-
Hg2+
-
isoenzyme II
Hg2+
-
10 mM, 12% residual activity
Hg2+
-
slight inhibition of isozyme alpha-GalNAcase I, strong inhibition of isozyme alpha-GalNAcase II
N-Acetyl-D-galactosamine
-
57% and 62% inhibition of isozyme alpha-GalNAcase I and isozyme alpha-GalNAcase II
N-Acetyl-D-galactosamine
-
-
N-acetyl-D-glucosamine
-
-
N-acetylgalactosamine
-
-
N-acetylgalactosamine
-
-
N-acetylgalactosamine
-
-
N-acetylgalactosamine
-
-
N-bromosuccinimide
-
1.8 mM, complete loss of activity
N-ethylmaleimide
-
1.8 mM, 60% of original activity
p-chloromercuribenzoate
-
1.8 mM, complete loss of activity
Pb2+
-
10 mM, 30% residual activity
additional information
-
not inhibitory: Ca2+, Mg2+, Mn2+, Ag+
-
additional information
-
no inhibition by D-glucose, N-acetyl-D-glucosamine, and Mn2+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Trypsin
-
the enzyme needs to be proteolytically activated, activation of the enzyme by trypsin
-
additional information
-
the enzyme is inducible in patients peripheral blood mononuclear cells by HIV-1 provirus-inducing agent, overview
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.56
-
2-nitrophenyl-alpha-N-acetylgalactosaminide
G5D7B5
pH 3.5, 37C
0.73
-
2-nitrophenyl-alpha-N-acetylgalactosaminide
-
pH 3.0, 35C
0.73
-
2-nitrophenyl-alpha-N-acetylgalactosaminide
A2QL72
pH not specified in the publication, temperature not specified in the publication
6.8
-
4-methylumbelliferyl-alpha-D-galactopyranoside
-
-
0.7
-
4-nitrophenyl alpha-D-N-acetylgalactosaminide
-
recombinant wild-type enzyme
0.89
-
4-nitrophenyl alpha-D-N-acetylgalactosaminide
-
recombinant mutant N201Q
0.036
-
Forssman hapten
-
-
0.59
-
Forssman hapten
-
-
1.04
-
GalNAc-alpha-1,3-GalNAc-beta-1,3-Gal-alpha-1,4-Gal-beta-1,4-Glc-beta-1,1-ceramide
-
pH 4.2, 37C, isozyme alpha-GalNAcase I
1.79
-
GalNAc-alpha-1,3-GalNAc-beta-1,3-Gal-alpha-1,4-Gal-beta-1,4-Glc-beta-1,1-ceramide
-
pH 4.2, 37C
7
-
N-acetyl-alpha-D-galactosaminide
-
-
8.8
-
o-nitrophenyl-alpha-D-fucopyranoside
-
-
1.3
-
o-nitrophenyl-alpha-N-acetylgalactosaminide
-
-
2.4
-
o-nitrophenyl-alpha-N-acetylgalactosaminide
-
-
1.58
-
o-nitrophenyl-N-acetyl-alpha-D-galactosaminide
-
pH 7.0, 37C
1.62
-
o-nitrophenyl-N-acetyl-alpha-D-galactosaminide
-
pH 6.5, 37C, recombinant enzyme
0.05
-
ovine submaxillary asialoglycoprotein
-
-
-
1.27
-
p-nitrophenyl N-acetyl-alpha-D-galactosaminide
-
enzyme from HIV patient serum, at pH 6.1
4.83
-
p-nitrophenyl N-acetyl-alpha-D-galactosaminide
-
constitutive lung enzyme, at pH 4.3
14.7
-
p-nitrophenyl-2-deoxy-alpha-D-galactopyranoside
-
-
0.38
-
p-nitrophenyl-alpha-N-acetyl-D-galactosaminide
-
pH 7.2, 36C
0.23
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
-
-
0.6
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
-
-
0.77
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
-
-
0.8
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
-
-
0.8
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
-
-
1.3
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
-
-
1.55
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
-
isoenzyme II
2.2
5.8
p-nitrophenyl-alpha-N-acetylgalactosaminide
-
three isoforms
2.4
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
-
-
2.5
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
-
-
3.33
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
-
isoenzyme I
4.2
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
-
-
6.6
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
-
-
1.1
-
p-nitrophenyl-N-acetyl-alpha-D-galactosaminide
-
pH 6.5, 37C, recombinant enzyme
1.35
-
p-nitrophenyl-N-acetyl-alpha-D-galactosaminide
-
pH 7.0, 37C
50
-
phenyl-alpha-N-acetylglucosaminide
-
-
1.27
-
serum vitamin D3-binding protein
-
pH 6.1, 37C
-
4.83
-
serum vitamin D3-binding protein
-
pH 4.3, 37C
-
3.97
-
GalNAc-alpha-1,3-GalNAc-beta-1,3-Gal-alpha-1,4-Gal-beta-1,4-Glc-beta-1,1-ceramide
-
pH 4.2, 37C, isozyme alpha-GalNAcase II
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetics, recombinant wild-type and mutant enzymes
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
16.3
-
4-nitrophenyl alpha-D-N-acetylgalactosaminide
-
recombinant wild-type enzyme
17.1
-
4-nitrophenyl alpha-D-N-acetylgalactosaminide
-
recombinant mutant N201Q
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0002
-
-
cell extract of gingival keratinocyte
0.0003
-
-
cell extract of gingival fibroblast
0.0004
-
-
cell extract of embryonic lung fibroblast
0.0012
-
-
pH 5.0, Chang liver cell
0.0021
-
-
pH 5.0, Hep-G2 cell
0.0026
-
-
pH 5.0, HCT116 cell
0.005
-
-
cell extract of gingival carcinoma
0.012
-
-
cell extract of salivary gland carcinoma
3.1
-
A2QL72
substrate 2-nitrophenyl-alpha-D-galactoside, pH not specified in the publication, temperature not specified in the publication
4.5
-
-
purified placental enzyme
8.33
-
-
purified recombinant enzyme mutant
19.56
-
-
purified isozyme alpha-GalNAcase I
24.2
-
-
purified isozyme alpha-GalNAcase II
33.5
-
-
pH 3.0, 35C
33.5
-
A2QL72
substrate 2-nitrophenyl-alpha-N-acetylgalactosaminide, pH not specified in the publication, temperature not specified in the publication
42.3
-
G5D7B5
pH 3.5, 37C
51.2
-
-
recombinant enzyme
56.4
-
-
native enzyme
2279
-
-
purified fraction from salivary gland carcinoma
84110
-
-
purified recombinant enzyme
additional information
-
-
list of rumen bacteria and protozoa
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.8
-
A2QL72
-
2
2.4
G5D7B5
-
2.7
3.5
-
isoenzyme I, p-nitrophenyl-alpha-N-acetylgalactosaminide
3
-
-
isozyme alpha-GalNAcase II
3.5
-
-
isozyme alpha-GalNAcase I
3.8
-
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
3.8
-
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
3.9
-
-
forssman hapten
4
4.5
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
4
6.8
-
-
4
-
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
4.2
-
-
isoenzyme II, p-nitrophenyl-alpha-N-acetylgalactosaminide
4.2
-
-
-
4.3
4.7
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
4.3
4.7
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
4.3
-
-
constitutive lung enzyme
4.5
-
-
4-methylumbelliferyl-alpha-galactopyranoside
4.5
-
-
N-acetyl-alpha-D-galactosaminide
4.8
-
-
4-methylumbelliferyl-alpha-galactopyranoside
5.8
6.8
-
three isoforms
6
-
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
6
-
-
assay at
6.1
-
-
; enzyme from HIV patient serum
6.5
7
-
recombinant enzyme
6.5
-
-
assay at
7
8
-
pH 7.2, 36C
additional information
-
-
other substrates
additional information
-
-
more values of isoenzymes
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.5
8
-
p-nitrophenyl-alpha-N-acetylgalactosaminide
3
8
-
below pH 3.6 the activity declines rapidly and at pH 3.0 retains about 1% of the orginal activity, above pH 7.5 the activity declines rapidly and at pH 8.0 retains about 4% of the orginal activity
4
7
-
not active above, p-nitrophenyl-alpha-N-acetylgalactosaminide
6
8
-
27% decline in activity from pH 6.0-8.0 with no apparent optimum
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
-
37
-
-
assay at
50
55
G5D7B5
-
55
-
A2QL72
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.4
-
-
purified isozyme alpha-GalNAcase I, isoelectric focusing
4.4
-
G5D7B5
isoelectric focusing
4.58
-
-
recombinant enzyme
4.8
-
-
isoelectric focusing
4.8
-
-
purified enzyme, isoelectric focusing
4.8
-
A2QL72
isoelectric focusing
7.1
-
-
purified isozyme alpha-GalNAcase II
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
inducible enzyme
Manually annotated by BRENDA team
-
high levels, salivary gland and gingival
Manually annotated by BRENDA team
-
low levels, embryonic lung and gingival
Manually annotated by BRENDA team
-
from a patient with Fabry disease
Manually annotated by BRENDA team
-
299, low levels
Manually annotated by BRENDA team
-
cutaneous melanoma, specific enzymatic activity of serum alpha-N-acetylgalactosaminidase is significantly increased in stage III melanoma patients, but not in early stages
Manually annotated by BRENDA team
-
peripheral blood, inducible enzyme
Manually annotated by BRENDA team
-
specific enzymatic activity of serum alpha-N-acetylgalactosaminidase is significantly increased in stage III melanoma patients, but not in early stages
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
serum enzyme
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40000
-
-
pH 7.2, gel filtration
40000
-
-
isozyme alpha-GalNAcase II, gel filtration
48000
-
-
gel filtration
55000
-
-
gel filtration
70000
-
G5D7B5
and 130000, gel filtration
80000
-
-
pH 4.2, gel filtration
83000
-
A4Q8F7
gel filtration
84000
-
-
gel filtration
102000
-
-
gel filtration
115000
-
-
non-denaturating polyacrylamide gel electrophoresis
130000
-
G5D7B5
and 70000, gel filtration
430000
-
-
about, isozyme alpha-GalNAcase I, gel filtration
440000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q8XNK8
x * 70000, SDS-PAGE
?
-
x * 48000, SDS-PAGE
?
-
x * 72100 Da, SDS-PAGE
?
-
x * 719600, denatured recombinant enzyme, x * 724200, native recombinant enzyme, SDS-PAGE
?
-
x * 46000, native enzyme, SDS-PAGE
?
G5D7B5
x * 54000, calculated, x * 76000, SDS-PAGE
dimer
-
2 * 35000, monomers associate to dimers at pH 4.2, SDS-PAGE
dimer
-
2 * 52000, probably two subunits with identical molecular weight, SDS-PAGE
dimer
A4Q8F7
2 * 48500, SDS-PAGE
hexamer
-
6 * 76000, SDS-PAGE
hexamer
Aspergillus niger CCIM
-
6 * 76000, SDS-PAGE
-
homodimer
-
alpha-NAGAL is a homodimer with each monomer divided into two domains. Domain 1 forms a (beta/alpha)8 barrel, and domain 2 contains eight antiparallel beta strands in two beta sheets
monomer
-
57000, SDS-PAGE
monomer
-
43000, SDS-PAGE
monomer
-
1 * 43000, isozyme alpha-GalNAcase II, SDS-PAGE
multimer
-
x * 49100, SDS-PAGE
multimer
-
160000-200000, SDS-PAGE, three isoforms
polymer
-
x * 47000, isozyme alpha-GalNAcase I, SDS-PAGE
tetramer
-
4 * 50000, SDS-PAGE
monomer
A4Q8F7
1 * 48500, SDS-PAGE
additional information
-
study of oligosaccharide structure, the first five: N124, N177, N201, N359 and N385, of six potential N-glycosylation sites are occupied
additional information
-
isozyme alpha-GalNAcase I and alpha-GalNAcase II peptide mapping and amino acid sequence comparisons, overview
additional information
A4Q8F7
enzyme may exist both in the monomeric and dimeric form, depending on the salt concentration of the buffer solution
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
enzyme may be deglycosylated without loss of activity
glycoprotein
G5D7B5
sequence contains eight potential N-glycosylation sites. Six asparagines located at residues 14, 52, 58, 88, 320 and 456 are glycosylated
glycoprotein
Aspergillus niger CCIM
-
enzyme may be deglycosylated without loss of activity
-
glycoprotein
-
precursor is processed to the mature protein
glycoprotein
-
the enzyme contains five N-linked glycosylation sites. The N201 glycosylation is critical for enzyme stability and activity
glycoprotein
-
7.0% neutral sugars
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native enzyme and in complex with alpha-N-acetylgalactosamine, to 2.3 and 2.4 A resolution, respectively. Each monomer of NagA consists of two closely associated domains, forming a narrow tunnel in which the NAD+ molecule is anchored. The NAD+ is embedded within a narrow tunnel, almost exclusively shielded from solvent. It is bound with its diphosphate group oriented towards the N-terminus of the first alpha-helix of the N-terminal dinucleotide-binding domain and has both the adenine ring and the nicotinamide ring in the anti conformation. No major structural changes are observed in NagA upon product binding
A4Q8F7
X-ray crystallography
-
purified recombinant wild-type and mutant enzymes in complexes with two catalytic products, the alpha-galactose and alpha-GalNAc monosaccharides, and a covalent intermediate bound in the enzyme active site, X-ray diffraction structure determination and analysis at 1.9 A resolution
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.3
6.5
-
purified isozyme alpha-GalNAcase II, stable at 4C
2.7
4.5
-
purified isozyme alpha-GalNAcase I, stable at 4C
3.5
8.5
-
purified enzyme, stable at 4C
3.6
6.8
-
-
4.5
5.5
-
isoenzyme I
4.5
6.5
-
isoenzyme II
additional information
-
-
comparison of activity at pH 5.0, 6.0 and 7.0 from Hep-G2 cells, HCT116 cells and Chang liver cells
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
24
-
active and stable at
4
37
-
the enzyme hydrolyses A2 epitopes at 4C with 42% of the efficiency of that at 37C
35
-
-
stable for at least 3 days
37
-
-
stable for 6 h in 0.05 sodium citrate buffer, pH 4.2
37
-
-
pH 4.0,m 60 min, purified isozyme alpha-GalNAcase I shows 50% remaining activity, purified isozyme alpha-GalNAcase II 92%
37
-
-
purified enzyme, 60 min, pH 4.0, 98% activity remaining
37
-
G5D7B5
48 h, 35% loss of activity
40
-
-
not stable above
40
-
-
40% loss of activity after 30 min
42
-
-
comparison of stability at 42C of mutant and wild-type enzymes
45
-
-
55% loss of activity after 10 min
50
-
-
isoenzyme I stable for 30 min, isoenzyme II loses activity
50
-
-
not stable above
50
-
-
at heating during 30 min retains 100% of the activity
55
-
-
not stable above
55
-
-
5 h, 50% loss of activity
additional information
-
-
the enzyme does not withstand freezing
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0C, 1 month
-
20C, stable for 1 week
-
4C, sterile condition, stable for any length of time
-
-20C, about 5% loss of activity
-
4C, 50 mM citrate-phosphate buffer within the pH range 2-4, stable for several weeks
G5D7B5
4C, pH 1.5-4.0, stable for several months
-
-20C, lyophilized, several years
-
-20C, 6 months
-
-20C, acidified plasma, at least one year
-
-20C, lyophilized, several years
-
the purified wild-type and N201Q mutant proteins expressed in insect cells retain nearly full activity for months at 4C, but the CHO-expressed material loses most of its activity within 72 h
-
-20C, lyophilized, several years
-
0C, sodium citrate buffer, bovine serum albumin, 2 weeks, pH 4.2
-
4C, enzyme separation buffer containing 3 mM sodium azide, 25-31 months
-
-20C, 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native isozymes alpha-GalNAcase I and alpha-GalNAcase II from liver
-
native enzyme
-
recombinant protein
G5D7B5
native isozymes alpha-GalNAcase I and II are isolated from liver homogenate by ammonium sulfate fractionation and separated from each other by gel filtration. Then they are further individually purified by cation exchange chromatography and gel filtration, and additionally by hydroxylapatite chromatography for isozyme alpha-GalNAcase II. Isozyme alpha-GalNAcase I is purified 440fold, isozyme alpha-GalNAcase II 544fold
-
partially
-
recombinant enzyme
-
enzyme from salivary gland cells
-
enzyme mutant from cell culture by dialysis, ammonium sulfate fractionation, hydrophobic interaction, cation exchange, and anion exchange chromatography
-
native enzyme from placenta by 4-aminophenyl thio-beta-D-galactose-ceramide hexoside-resin affinity
-
partially
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Saccharomyces cerevisiae
G5D7B5
expression of aagA gene in Escherichia coli, resulting in recombinants exhibiting high-level expression of the expected activity
Q8XNK8
the gene encoding the clostridial enzyme is cloned in an Escherichia coli T7 expression system
-
expression in Escherichia coli
A4Q8F7
expression in bacteria, rabbit reticulocyte lysate and yeast
-
expression in yeast Pichia pastoris
-
expression in Chines hamster ovary cells
-
expression in CHO and COS-1 cells. Expression of wild-type and mutant enzymes in Escherichia coli as insoluble proteins, and in Kluyveromyces lactis as soluble hyperglycosylated proteins. Expression of wild-type and mutant enzymes in Trichoplusia ni Tn5 insect cells using the baculovirus transfection system leads to suitable proteins
-
expression of the engineered enzyme in CHO cells
-
expression in B-lymphoblast cell line
-
expression in Cos-1 cells
-, Q9QWR8
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D217N
-
a naturally occuring Schindler disease and/or Kanzaki disease mutation
E193X
-
a naturally occuring Schindler disease and/or Kanzaki disease mutation
E325K
-
a naturally occuring Schindler disease and/or Kanzaki disease mutation
N124Q
-
35% activity in comparison to 100% activity of wild-type enzyme
N177Q
-
48% activity in comparison to 100% activity of wild-type enzyme
N201Q
-
28% activity in comparison to 100% activity of wild-type enzyme
N201Q
-
site-directed mutagenesis, one of the proteins with the third N-linked carbohydrate attachment site is removed
N359Q
-
57% activity in comparison to 100% activity of wild-type enzyme
N385Q
-
4% activity in comparison to 100% activity of wild-type enzyme
R329Q
-
mutation results in protein instability; site-specific mutagenesis, construction of the naturally occurring mutation at R329 in Kanzaki disease, less severe phenotype compared to R329W
R329Q
-
a naturally occuring Schindler disease and/or Kanzaki disease mutation
R329W
-
mutation results in protein instability; site-specific mutagenesis, construction of the naturally occurring mutation at R329 in Kanzaki disease, more severe phenotype compared to R329Q
R329W
-
a naturally occuring Schindler disease and/or Kanzaki disease mutation
S160C
-
a naturally occuring Schindler disease and/or Kanzaki disease mutation
S188E/A191L
-
Ser188 and Ala191 play important roles in the recognition of an N-acetylgalactosamine residue in NAGA, while lu203 and Leu206 play important roles in the recognition of a galactose residue in GLA. Construction of a modified alpha-N-acetylgalactosaminidase with alpha-galactosidase A-like substrate specificity. The enzyme acquires the ability to catalyze the degradation of 4-methylumbelliferyl-alpha-D-galactopyranoside, but retaines the wild-type NAGA's stability, overview
E367K
-
a naturally occuring Schindler disease and/or Kanzaki disease mutation
additional information
-
construction of mutants of each of the five N-linked glycosylation sites
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
The enzyme is able to remove at neutral pH alpha-1,3-bound residues of N-acetylgalactosamine from glycoproteins of blood group A-substances and A-erythrocytes, converting them into 0 group substances
medicine
Arenibacter latericius KMM 426
-
The enzyme is able to remove at neutral pH alpha-1,3-bound residues of N-acetylgalactosamine from glycoproteins of blood group A-substances and A-erythrocytes, converting them into 0 group substances
-
medicine
-
the enzyme may be useful for enzymic conversion of type A2 to universally transfusable type O red blood cells, potential application in the field of solid organ transplantation
medicine
-
potential application in the field of erythrocyte conversion technology
biotechnology
-
use of a modified alpha-N-acetylgalactosaminidase in the development of enzyme replacement therapy for Fabry disease
medicine
-
the enzyme can be employed as a diagnostic/prognostic tool for patients with salivary gland adenocarcima
medicine
-
use of a modified alpha-N-acetylgalactosaminidase in the development of enzyme replacement therapy for Fabry disease