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Information on EC 3.2.1.49 - alpha-N-acetylgalactosaminidase and Organism(s) Aspergillus niger and UniProt Accession A2QL72

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IUBMB Comments
The human lysosomal enzyme is involved in the degradation of blood type A epitope.
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This record set is specific for:
Aspergillus niger
UNIPROT: A2QL72
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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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-acetamido-2-deoxy-alpha-D-galactoside acetamidodeoxygalactohydrolase
-
-
-
-
4-nitrophenyl-alpha-N-acetylgalactosaminidase
-
-
-
-
alpha-acetylgalactosaminidase
-
-
-
-
alpha-galactosidase B
-
-
-
-
alpha-GalNAc-ase
-
exo-alpha-N-acetylgalactosaminidase
-
-
-
-
N-acetyl-alpha-D-galactosaminidase
-
-
-
-
N-acetyl-alpha-galactosaminidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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 hide
9075-63-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-nitrophenyl-alpha-D-galactoside + H2O
2-nitrophenol + alpha-D-galactose
show the reaction diagram
-
-
-
?
2-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
2-nitrophenol + alpha-N-acetylgalactosamine
show the reaction diagram
-
-
-
?
2-nitrophenyl 2-acetyl-2-deoxy-alpha-D-galactosamine + H2O
2-nitrophenol + 2-acetyl-2-deoxy-alpha-D-galactosamine
show the reaction diagram
-
-
-
?
2-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
2-nitrophenol + alpha-N-acetylgalactosamine
show the reaction diagram
4-nitrophenyl N-acetyl-alpha-D-galactosamine + H2O
4-nitrophenol + N-acetyl-alpha-D-galactosamine
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
p-nitrophenol + alpha-N-acetylgalactosamine
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
an exoglycosidase specific for the hydrolysis of terminal alpha-linked N-acetylgalactosamine in various sugar chains
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Hg2+
-
10 mM, 12% residual activity
Pb2+
-
10 mM, 30% residual activity
additional information
-
not inhibitory: Ca2+, Mg2+, Mn2+, Ag+
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
33.5
-
pH 3.0, 35°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 4
recombinant enzyme, substrate 2-nitrophenyl 2-acetyl-2-deoxy-alpha-D-galactosamine
2.6 - 3.2
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 55
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
isoelectric focusing
4.8
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional alpha-galactosidase and alpha-N-acetylgalactosaminidase
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
115000
-
non-denaturating polyacrylamide gel electrophoresis
130000
440000
-
gel filtration
54000
70000
76000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 54000, calculated, x * 76000, SDS-PAGE
dimer
2 * 70000, recombinant enzyme, SDS-PAGE
hexamer
-
6 * 76000, SDS-PAGE
monomer
1 * 76000, native enzyme, gel filtration, 1 * 54000, about, sequence calculation, 1 * 70000, recombinant enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.5 - 4
-
-
695797
2.5 - 8
-
-
208674
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
stable for at least 3 days
37
48 h, 35% loss of activity
50
-
not stable above
55
-
5 h, 50% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, about 5% loss of activity
-
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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme
-
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
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team