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IUBMB Comments The human lysosomal enzyme is involved in the degradation of blood type A epitope.
The taxonomic range for the selected organisms is: Aspergillus niger The enzyme appears in selected viruses and cellular organisms
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,
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2-acetamido-2-deoxy-alpha-D-galactoside acetamidodeoxygalactohydrolase
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4-nitrophenyl-alpha-N-acetylgalactosaminidase
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alpha-acetylgalactosaminidase
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alpha-galactosidase B
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exo-alpha-N-acetylgalactosaminidase
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N-acetyl-alpha-D-galactosaminidase
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N-acetyl-alpha-galactosaminidase
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hydrolysis of O-glycosyl bond
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alpha-N-acetyl-D-galactosaminide N-acetylgalactosaminohydrolase
The human lysosomal enzyme is involved in the degradation of blood type A epitope.
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2-nitrophenyl-alpha-D-galactoside + H2O
2-nitrophenol + alpha-D-galactose
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2-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
2-nitrophenol + alpha-N-acetylgalactosamine
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?
2-nitrophenyl 2-acetyl-2-deoxy-alpha-D-galactosamine + H2O
2-nitrophenol + 2-acetyl-2-deoxy-alpha-D-galactosamine
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?
2-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
2-nitrophenol + alpha-N-acetylgalactosamine
4-nitrophenyl N-acetyl-alpha-D-galactosamine + H2O
4-nitrophenol + N-acetyl-alpha-D-galactosamine
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?
p-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
p-nitrophenol + alpha-N-acetylgalactosamine
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?
additional information
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2-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
2-nitrophenol + alpha-N-acetylgalactosamine
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?
2-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
2-nitrophenol + alpha-N-acetylgalactosamine
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enzyme acts with retention of the anomeric configuration
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additional information
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preference for alpha-N-acetyl-D-galactosaminide over alpha-D-galactoside. alpha-N-acetylgalactosaminidase activity uses a retaining mechanism
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additional information
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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
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additional information
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an exoglycosidase specific for the hydrolysis of terminal alpha-linked N-acetylgalactosamine in various sugar chains
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additional information
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the enzyme also exhibits alpha-galactosidase activity
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additional information
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an exoglycosidase specific for the hydrolysis of terminal alpha-linked N-acetylgalactosamine in various sugar chains
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Hg2+
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10 mM, 12% residual activity
Pb2+
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10 mM, 30% residual activity
additional information
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not inhibitory: Ca2+, Mg2+, Mn2+, Ag+
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0.73
2-nitrophenyl-alpha-N-acetylgalactosaminide
pH not specified in the publication, temperature not specified in the publication
0.56 - 0.73
2-nitrophenyl-alpha-N-acetylgalactosaminide
0.23
p-nitrophenyl-alpha-N-acetylgalactosaminide
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0.56
2-nitrophenyl-alpha-N-acetylgalactosaminide
pH 3.5, 37°C
0.73
2-nitrophenyl-alpha-N-acetylgalactosaminide
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pH 3.0, 35°C
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3.1
substrate 2-nitrophenyl-alpha-D-galactoside, pH not specified in the publication, temperature not specified in the publication
33.5
substrate 2-nitrophenyl-alpha-N-acetylgalactosaminide, pH not specified in the publication, temperature not specified in the publication
42.3
pH 3.5, 37°C
42.3
purified recombinant enzyme, pH 3.5, 37°C
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2 - 4
recombinant enzyme, substrate 2-nitrophenyl 2-acetyl-2-deoxy-alpha-D-galactosamine
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50 - 55
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50 - 55
recombinant enzyme, substrate 2-nitrophenyl 2-acetyl-2-deoxy-alpha-D-galactosamine
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4.8
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isoelectric focusing
4.4
isoelectric focusing
4.4
isoelectric focusing, recombinant enzyme
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bifunctional alpha-galactosidase and alpha-N-acetylgalactosaminidase
UniProt
brenda
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brenda
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brenda
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115000
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non-denaturating polyacrylamide gel electrophoresis
130000
and 70000, gel filtration
130000
recombinant enzyme, analytical ultracentrifugation and dynamic light scattering, dimeric form
54000
x * 54000, calculated, x * 76000, SDS-PAGE
54000
1 * 76000, native enzyme, gel filtration, 1 * 54000, about, sequence calculation, 1 * 70000, recombinant enzyme, SDS-PAGE
70000
and 130000, gel filtration
70000
recombinant enzyme, analytical ultracentrifugation and dynamic light scattering, monomeric form
76000
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6 * 76000, SDS-PAGE
76000
x * 54000, calculated, x * 76000, SDS-PAGE
76000
1 * 76000, native enzyme, gel filtration, 1 * 54000, about, sequence calculation, 1 * 70000, recombinant enzyme, SDS-PAGE
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?
x * 54000, calculated, x * 76000, SDS-PAGE
dimer
2 * 70000, recombinant enzyme, SDS-PAGE
hexamer
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6 * 76000, SDS-PAGE
monomer
1 * 76000, native enzyme, gel filtration, 1 * 54000, about, sequence calculation, 1 * 70000, recombinant enzyme, SDS-PAGE
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glycoprotein
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enzyme may be deglycosylated without loss of activity
glycoprotein
sequence contains eight potential N-glycosylation sites. Six asparagines located at residues 14, 52, 58, 88, 320 and 456 are glycosylated
glycoprotein
N-glycosylation occurs at six of the eight potential N-glycosylation sites in both wild-type and recombinant enzyme, i.e. residues 14, 52, 58, 88, 320 and 456
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35
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stable for at least 3 days
37
48 h, 35% loss of activity
55
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5 h, 50% loss of activity
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-20°C, about 5% loss of activity
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4°C, 50 mM citrate-phosphate buffer within the pH range 2-4, stable for several weeks
4°C, pH 1.5-4.0, stable for several months
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native enzyme from cell culture supernatant by three chromatographic steps to homogeneity, recombinant enzyme from Saccharomyces cerevisiae to homogeneity 105.9fold by hydrophobic interaction chromatography, ultrafiltration, cation exchange chromatography, gel filtration, and anion exchange chromatography
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DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3) as inactive enzyme in inclusion bodies, expression in Pichia pastoris strain X33 is not successful, heterologous overexpression in Saccharomyces cerevisiae strain W303-1A without enzyme secretion
expression in Saccharomyces cerevisiae
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Naundorf, A.; Ajisaka, K.
Purification of alpha-N-acetylgalactosaminidase from Aspergillus niger and its use in the synthesis of GalNAc-alpha-(1 O)-serine
Enzyme Microb. Technol.
25
483-488
1999
Aspergillus niger
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brenda
Weignerova, L.; Filipi, T.; Manglova, D.; Kren, V.
Induction, purification and characterization of alpha-N-acetylgalactosaminidase from Aspergillus niger
Appl. Microbiol. Biotechnol.
79
769-774
2008
Aspergillus niger, Aspergillus niger CCIM K2
brenda
Weignerova, L.; Pelantova, H.; Manglova, D.; Michalkova, K.; Kren, V.
Condensation reactions catalyzed by alpha-N-acetylgalactosaminidase from Aspergillus niger yielding alpha-N-acetylgalactosaminides
Biocatal. Biotransform.
28
150-155
2010
Aspergillus niger
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brenda
Kulik, N.; Weignerova, L.; Filipi, T.; Pompach, P.; Novak, P.; Mrazek, H.; Slamova, K.; Bezouska, K.; Kren, V.; Ettrich, R.
The alpha-galactosidase type A gene aglA from Aspergillus niger encodes a fully functional alpha-N-acetylgalactosaminidase
Glycobiology
20
1410-1419
2010
Aspergillus niger (A2QL72)
brenda
Mrazek, H.; Benada, O.; Man, P.; Vanek, O.; K?en, V.; Bezouska, K.; Weignerova, L.
Facile production of Aspergillus niger alpha-N-acetylgalactosaminidase in yeast
Protein Expr. Purif.
81
106-114
2011
Aspergillus niger (G5D7B5), Aspergillus niger CCIM K2 (G5D7B5)
brenda