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Information on EC 3.2.1.49 - alpha-N-acetylgalactosaminidase and Organism(s) Homo sapiens and UniProt Accession P17050
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3.2.1.49 alpha-N-acetylgalactosaminidaseIUBMB Comments
The human lysosomal enzyme is involved in the degradation of blood type A epitope.
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Word Map
- 3.2.1.49
- n-acetylgalactosamine
- sialidase
- fabry
-
schindler
-
exoglycosidase
-
neuroaxonal
-
d3-binding
-
gcmaf
- angiokeratoma
-
alpha-linked
-
beta-galnac
-
macrophage-activating
- pomatia
-
corporis
- diffusum
- biflorus
-
mucin-type
- medicine
-
alpha-n-acetylgalactosaminyltransferase
- alpha-n-acetylgalactosamine
-
asialo
- diagnostics
- biotechnology
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
alpha-n-acetylgalactosaminidase, alpha-galnac, nagalase, envelope glycoprotein gp160, alpha-naga, alpha-galactosidase b, alpha-nagalase, alpha-galnacase i, alpha-nagal, alpha-galnacase ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-acetamido-2-deoxy-alpha-D-galactoside acetamidodeoxygalactohydrolase
-
-
-
-
4-nitrophenyl-alpha-N-acetylgalactosaminidase
-
-
-
-
alpha-acetylgalactosaminidase
-
-
-
-
alpha-galactosidase B
exo-alpha-N-acetylgalactosaminidase
-
-
-
-
N-acetyl-alpha-D-galactosaminidase
-
-
-
-
N-acetyl-alpha-galactosaminidase
-
-
-
-
alpha-galactosidase B
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
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
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
the enzyme exhibits an endo-enzyme activity in addition to an exo-activity
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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.
CAS REGISTRY NUMBER
COMMENTARY
9075-63-2
-
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-alpha-D-galactopyranoside + H2O
4-methylumbelliferone + alpha-D-galactopyranose
substrate of engineered enzyme mutant S188E/A191L, not of the wild-type enzyme
-
-
?
4-nitrophenyl alpha-D-N-acetylgalactosaminide + H2O
4-nitrophenol + N-acetyl-D-galactosamine
substrate binding and active site structure, active-site interactions and ligand binding, overview. Inactive enzyme conformation, overview
-
-
?
globotriaosylceramide + H2O
?
wild-type and engineered mutant enzymes
-
-
?
2-nitrophenyl alpha-D-fucopyranoside + H2O
2-nitrophenol + alpha-D-fucopyranose
-
-
-
-
?
4-methylumbelliferyl-alpha-D-galactopyranoside + H2O
4-methylumbelliferone + alpha-D-galactopyranose
-
-
-
-
?
4-methylumbelliferyl-alpha-D-galactosaminide + H2O
4-methylumbelliferone + alpha-D-galactosamine
-
-
-
-
?
4-nitrophenyl alpha-D-N-acetylgalactosaminide + H2O
4-nitrophenol + N-acetyl-D-galactosamine
-
-
-
-
?
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
-
i.e. Forssman hapten glycolipid
-
-
?
o-nitrophenyl N-acetyl-alpha-D-galactosaminide + H2O
o-nitrophenol + N-acetyl-D-galactosamine
-
-
-
-
?
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
-
-
-
-
?
p-nitrophenyl alpha-D-galactopyranoside + H2O
p-nitrophenol + alpha-D-galactopyranose
-
-
-
-
?
p-nitrophenyl N-acetyl-alpha-D-galactosaminide + H2O
p-nitrophenol + N-acetyl-alpha-D-galactosamine
-
-
-
-
?
p-nitrophenyl N-acetyl-alpha-D-galactosaminide + H2O
p-nitrophenol + N-acetyl-D-galactosamine
-
-
-
-
?
p-nitrophenyl-2-deoxy-alpha-D-galactopyranoside + H2O
p-nitrophenol + 2-deoxy-alpha-D-galactopyranose
-
-
-
-
?
p-nitrophenyl-alpha-N-acetyl-D-galactoaminide + H2O
p-nitrophenol + alpha-N-acetyl-D-galactosamine
-
the Hep-G2 cell lysate hydrolyzes the exo-type substrate
-
-
?
serum vitamin D3-binding protein + H2O
?
-
i.e. Gc protein, human substrate, deglycosylation of the substrate
-
-
?
4-nitrophenyl N-acetyl-D-galactosamine + H2O
4-nitrophenol + N-acetyl-galactosamine
-
-
-
?
4-nitrophenyl N-acetyl-D-galactosamine + H2O
4-nitrophenol + N-acetyl-galactosamine
-
-
-
-
?
additional information
?
-
alpha-NAGAL is a lysosomal exoglycosidase that cleaves terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids
-
-
?
additional information
?
-
-
alpha-NAGAL is a lysosomal exoglycosidase that cleaves terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids
-
-
?
additional information
?
-
Ser188 and Ala191 play important roles in the recognition of an N-acetylgalactosamine residue in NAGA
-
-
?
additional information
?
-
-
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 also shows activity with 4-nitrophenyl alpha-D-galactosaminide
-
-
?
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 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
?
-
-
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 hydrolyzes alpha-N-acetylgalactosyl residues from glycolipids and glycoproteins
-
-
?
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
additional information
?
-
alpha-NAGAL is a lysosomal exoglycosidase that cleaves terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids
-
-
?
additional information
?
-
-
alpha-NAGAL is a lysosomal exoglycosidase that cleaves terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids
-
-
?
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 hydrolyzes alpha-N-acetylgalactosyl residues from glycolipids and glycoproteins
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme is inducible in patients peripheral blood mononuclear cells by HIV-1 provirus-inducing agent, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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, 37°C
0.7
4-nitrophenyl alpha-D-N-acetylgalactosaminide
recombinant wild-type enzyme
0.89
4-nitrophenyl alpha-D-N-acetylgalactosaminide
recombinant mutant N201Q
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
additional information
additional information
kinetics, recombinant wild-type and mutant enzymes
-
additional information
additional information
-
kinetics, recombinant wild-type and mutant enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
6.1
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 6
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 - 6
the enzyme is more than 50% active between pH 4.0 and pH 5.5, at pH 6, the enzyme retains almost 40% of activity
4 - 6
-
the enzyme is more than 50% active between pH 4.0 and pH 5.5, at pH 6, the enzyme retains almost 40% of activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 68
37 - 68
37°C: about 50% of maximal activity, 68°C: about 50% of maximal activity
37 - 68
-
37°C: about 50% of maximal activity, 68°C: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cutaneous melanoma, specific enzymatic activity of serum alpha-N-acetylgalactosaminidase is significantly increased in stage III melanoma patients, but not in early stages
-
specific enzymatic activity of serum alpha-N-acetylgalactosaminidase is significantly increased in stage III melanoma patients, but not in early stages
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
malfunction
deficiency of alpha-NAGAL activity results in the lysosomal storage disorders Schindler disease and Kanzaki disease, molecular basis, overview
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
Schindler disease is a lysosomal storage disorder caused due to deficiency or defective activity of alpha-N-acetylgalactosaminidase
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NAGAB_HUMAN
411
0
46565
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55600
48000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
-
study of oligosaccharide structure, the first five: N124, N177, N201, N359 and N385, of six potential N-glycosylation sites are occupied
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
the enzyme contains five N-linked glycosylation sites. The N201 glycosylation is critical for enzyme stability and activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
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
E367K
a naturally occuring Schindler disease and/or Kanzaki disease mutation
N201Q
site-directed mutagenesis, one of the proteins with the third N-linked carbohydrate attachment site is removed
R329Q
R329W
S160C
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
R329Q
R329W
additional information
E325K
a naturally occuring Schindler disease and/or Kanzaki disease mutation
E325K
less favourable binding energy compared to native enzyme. The mutant enzyme possesses reduced volume in the catalytic cleft as compared to native enzyme resulting in the change in substrate pose. Changes in root mean square fluctuation of residues involved in catalytic activity affects the active site in terms of conformational space, thereby resulting in the change in catalytic volume that eventually lead to altered substrate pose. The proximity of substrate (electrophilic C1 of hexose ring) towards the enzyme (O2 of ASP139) is inconsistent for the mutant as compared to native enzyme resulting in less favourable binding energy of substrate. The mutants has detrimental effects contributing to the pathogenesis of the disease
R329Q
a naturally occuring Schindler disease and/or Kanzaki disease mutation
R329Q
less favourable binding energy compared to native enzyme. The mutant enzyme possesses reduced volume in the catalytic cleft as compared to native enzyme resulting in the change in substrate pose. Changes in root mean square fluctuation of residues involved in catalytic activity affects the active site in terms of conformational space, thereby resulting in the change in catalytic volume that eventually lead to altered substrate pose. The proximity of substrate (electrophilic C1 of hexose ring) towards the enzyme (O2 of ASP139) is inconsistent for the mutant as compared to native enzyme resulting in less favourable binding energy of substrate. The mutants has detrimental effects contributing to the pathogenesis of the disease
R329W
a naturally occuring Schindler disease and/or Kanzaki disease mutation
R329W
less favourable binding energy compared to native enzyme. The mutant enzyme possesses reduced volume in the catalytic cleft as compared to native enzyme resulting in the change in substrate pose. Changes in root mean square fluctuation of residues involved in catalytic activity affects the active site in terms of conformational space, thereby resulting in the change in catalytic volume that eventually lead to altered substrate pose. The proximity of substrate (electrophilic C1 of hexose ring) towards the enzyme (O2 of ASP139) is inconsistent for the mutant as compared to native enzyme resulting in less favourable binding energy of substrate. The mutants has detrimental effects contributing to the pathogenesis of the disease
S160C
a naturally occuring Schindler disease and/or Kanzaki disease mutation
S160C
less favourable binding energy compared to native enzyme. The mutant enzyme possesses reduced volume in the catalytic cleft as compared to native enzyme resulting in the change in substrate pose. Changes in root mean square fluctuation of residues involved in catalytic activity affects the active site in terms of conformational space, thereby resulting in the change in catalytic volume that eventually lead to altered substrate pose. The proximity of substrate (electrophilic C1 of hexose ring) towards the enzyme (O2 of ASP139) is inconsistent for the mutant as compared to native enzyme resulting in less favourable binding energy of substrate. The mutants has detrimental effects contributing to the pathogenesis of the disease
R329Q
-
site-specific mutagenesis, construction of the naturally occurring mutation at R329 in Kanzaki disease, less severe phenotype compared to R329W
R329W
-
site-specific mutagenesis, construction of the naturally occurring mutation at R329 in Kanzaki disease, more severe phenotype compared to R329Q
additional information
construction of mutants of each of the five N-linked glycosylation sites
additional information
-
construction of mutants of each of the five N-linked glycosylation sites
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
comparison of activity at pH 5.0, 6.0 and 7.0 from Hep-G2 cells, HCT116 cells and Chang liver cells
655254
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
37
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the purified preparation of the enzyme can be stored frozen for a month and retains 100% of its activity after thawing
the purified preparation of the enzyme can be stored frozen for a month and retains 100% of its activity after thawing
the purified preparation of the enzyme can be stored frozen for a month and retains 100% of its activity after thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
the purified preparation of the enzyme can be stored frozen for a month and retains 100% of its activity after thawing
the purified wild-type and N201Q mutant proteins expressed in insect cells retain nearly full activity for months at 4°C, but the CHO-expressed material loses most of its activity within 72 h
the purified preparation of the enzyme can be stored frozen for a month and retains 100% of its activity after thawing
the purified preparation of the enzyme can be stored frozen for a month and retains 100% of its activity after thawing
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
ORGANISM
UNIPROT
LITERATURE
fucoidan reduces the expression of the enzyme in the DLD-1 cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
use of a modified alpha-N-acetylgalactosaminidase in the development of enzyme replacement therapy for Fabry disease
medicine
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dean, K.J.; Sweeley, C.C.
Studies on human liver alpha-galactosidase. II Purification and enzymatic properties of alpha-Galactosidas B (alpha-N-acetylgalactosaminidase)
J. Biol. Chem.
254
10001-10005
1979
Homo sapiens
Dean, K.J.; Sweeley, C.C.
Studies on human liver alpha-galactosidases. III. Partial characterization of carbohydrate-binding specificities
J. Biol. Chem.
254
10006-10010
1979
Homo sapiens
Salvayre, R.; Maret, A.; Negre, A.; Douste-Blazy, L.
Properties of multiple molecular forms of alpha-galactosidase and alpha-N-acetylgalactosaminidase from normal and fabry leukocytes
Eur. J. Biochem.
100
377-383
1979
Homo sapiens
Sweeley, C.C.; Ledonne, N.C.; Robbins, P.W.
Post-translational processing reactions involved in the biosynthesis of lysosomal alpha-N-acetylgalactosaminidase in cultured human fibroblasts
Arch. Biochem. Biophys.
223
158-165
1983
Homo sapiens
Salvayre, R.; Negre, A.; Maret, A.; Lenoir, G.; Douste-Blazy, L.
Separation and properties of molecular forms of alpha-galactosidase and alpha-N-acetylgalactosaminidase from blood lymphocytes and lymphoid cell lines transformed by Epstein-Barr virus
Biochim. Biophys. Acta
659
445-456
1981
Homo sapiens
Dean, K.J.; Sung, S.S.J.; Sweeley, C.C.
The identification of alpha-galactosidase B from human liver as an alpha-N-acetylgalactosaminidase
Biochem. Biophys. Res. Commun.
77
1411-1417
1977
Homo sapiens
Callahan, J.W.; Lassila, E.L.; den Tandt, W.; Philippart, M.
alpha-N-Acetylgalactosaminidase: isolation, properties and distribution of the human enzyme
Biochem. Med.
7
424-431
1973
Homo sapiens
Yagi, F.; Eckhardt, A.E.; Goldstein, I.J.
Gycosidases of Ehrlich ascites tumor cells and ascitic fluid-purification and substrate specificity of alpha-N-acetylgalactosaminidase and alpha-galactosidase: comparison with coffee bean alpha galactosidase
Arch. Biochem. Biophys.
280
61-67
1990
Homo sapiens
Den Tandt, W.R.; Scharpe, S.
Micromethod for the fluorimetric determination of plasma N-acetyl-alpha-galactosaminidase and study of some of its characteristics
Enzyme Protein
49
273-280
1996
Homo sapiens
Mohamad, S.B.; Nagasawa, H.; Uto, Y.; Hori, H.
Tumor cell alpha-N-acetylgalactosaminidase activity and its involvement in GcMAF-related macrophage activation
Comp. Biochem. Physiol. A
132
1-8
2002
Homo sapiens
Ohta, M.; Ohnishi, T.; Ioannou, Y.A.; Hodgson, M.E.; Matsuura, F.; Desnick, R.J.
Human alpha-N-acetylgalactosaminidase: site occupancy and structure of N-linked oligosaccharides
Glycobiology
10
251-261
2000
Homo sapiens
Matsuura, T.; Uematsu, T.; Yamaoka, M.; Furusawa, K.
Effect of salivary gland adenocarcinoma cell-derived alpha-N-acetylgalactosaminidase on the bioactivity of macrophage activating factor
Int. J. Oncol.
24
521-528
2004
Homo sapiens
Yamamoto, N.
Pathogenic significance of alpha-N-acetylgalactosaminidase activity found in the envelope glycoprotein gp160 of human immunodeficiency virus Type 1
AIDS Res. Hum. Retroviruses
22
262-271
2006
Homo sapiens, Human immunodeficiency virus 1
Kanekura, T.; Sakuraba, H.; Matsuzawa, F.; Aikawa, S.; Doi, H.; Hirabayashi, Y.; Yoshii, N.; Fukushige, T.; Kanzaki, T.
Three dimensional structural studies of alpha-N-acetylgalactosaminidase (alpha-NAGA) in alpha-NAGA deficiency (Kanzaki disease): different gene mutations cause peculiar structural changes in alpha-NAGAs resulting in different substrate specificities and clinical phenotypes
J. Dermatol. Sci.
37
15-20
2005
Homo sapiens
Tajima, Y.; Kawashima, I.; Tsukimura, T.; Sugawara, K.; Kuroda, M.; Suzuki, T.; Togawa, T.; Chiba, Y.; Jigami, Y.; Ohno, K.; Fukushige, T.; Kanekura, T.; Itoh, K.; Ohashi, T.; Sakuraba, H.
Use of a modified alpha-N-acetylgalactosaminidase in the development of enzyme replacement therapy for Fabry disease
Am. J. Hum. Genet.
85
569-580
2009
Homo sapiens (P17050), Homo sapiens
Harun-Or-Rashid, M.; Matsuzawa, T.; Satoh, Y.; Shiraishi, T.; Ando, M.; Sadik, G.; Uda, Y.
Purification and characterization of alpha-N-acetylgalactosaminidases I and II from the starfish Asterina amurensis
Biosci. Biotechnol. Biochem.
74
256-261
2010
Asterina amurensis, Homo sapiens
Greco, M.; Mitri, M.D.; Chiriaco, F.; Leo, G.; Brienza, E.; Maffia, M.
Serum proteomic profile of cutaneous malignant melanoma and relation to cancer progression: association to tumor derived alpha-N-acetylgalactosaminidase activity
Cancer Lett.
283
222-229
2009
Homo sapiens
Clark, N.E.; Garman, S.C.
The 1.9 A structure of human alpha-N-acetylgalactosaminidase: The molecular basis of Schindler and Kanzaki diseases
J. Mol. Biol.
393
435-447
2009
Homo sapiens (P17050), Homo sapiens
Meshach Paul, D.; Rajasekaran, R.
Exploration of structural and functional variations owing to point mutations in alpha-NAGA
Interdiscip. Sci.
10
81-92
2018
Homo sapiens (P17050)
Cao, H.T.T.; Mikkelsen, M.D.; Lezyk, M.J.; Bui, L.M.; Tran, V.T.T.; Silchenko, A.S.; Kusaykin, M.I.; Pham, T.D.; Truong, B.H.; Holck, J.; Meyer, A.S.
Novel enzyme actions for sulphated galactofucan dpolymerisation and a new engineering strategy for molecular stabilisation of fucoidan degrading enzymes
Mar. Drugs
16
422
2018
Homo sapiens (P17050)
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