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Information on EC 3.2.1.97 - endo-alpha-N-acetylgalactosaminidase and Organism(s) Streptococcus pneumoniae and UniProt Accession Q8DR60

for references in articles please use BRENDA:EC3.2.1.97
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IUBMB Comments
The enzyme catalyses the liberation of Gal-(1->3)-beta-GalNAc alpha-linked to serine or threonine residues of mucin-type glycoproteins. EngBF from the bacterium Bifidobacterium longum specifically acts on core 1-type O-glycan to release the disaccharide Gal-(1->3)-beta-GalNAc. The enzymes from the bacteria Clostridium perfringens, Enterococcus faecalis, Propionibacterium acnes and Alcaligenes faecalis show broader specificity (e.g. they can also release the core 2 trisaccharide Gal-(1->3)-beta-(GlcNAc-(1->6)-beta)-GalNAc or the core 3 disaccharide GlcNAc-(1->3)-beta-GalNAc) [1,2]. The enzyme may play an important role in the degradation and utilization of mucins having core 1 O-glycan.
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This record set is specific for:
Streptococcus pneumoniae
UNIPROT: Q8DR60
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The taxonomic range for the selected organisms is: Streptococcus pneumoniae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
endo-alpha-n-acetylgalactosaminidase, engcp, engbf, nagbb, spgh101, endo-alpha-galnac-ase, endo-ef, endo-beta-n-acetylgalactosaminidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylgalactosaminidase, endo-alpha
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D-galactosyl-N-acetyl-alpha-D-galactosamine D-galactosyl-N-acetylgalactosaminohydrolase
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endo-alpha-acetylgalactosaminidase
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endo-alpha-N-acetylgalactosaminidase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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SYSTEMATIC NAME
IUBMB Comments
glycopeptide-D-galactosyl-N-acetyl-alpha-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase
The enzyme catalyses the liberation of Gal-(1->3)-beta-GalNAc alpha-linked to serine or threonine residues of mucin-type glycoproteins. EngBF from the bacterium Bifidobacterium longum specifically acts on core 1-type O-glycan to release the disaccharide Gal-(1->3)-beta-GalNAc. The enzymes from the bacteria Clostridium perfringens, Enterococcus faecalis, Propionibacterium acnes and Alcaligenes faecalis show broader specificity (e.g. they can also release the core 2 trisaccharide Gal-(1->3)-beta-(GlcNAc-(1->6)-beta)-GalNAc or the core 3 disaccharide GlcNAc-(1->3)-beta-GalNAc) [1,2]. The enzyme may play an important role in the degradation and utilization of mucins having core 1 O-glycan.
CAS REGISTRY NUMBER
COMMENTARY hide
59793-96-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Galbeta(1-3)GalNAcalpha(1-)OC6H4-o-NO2 + H2O
Galbeta(1-3)GalNAc + o-nitrophenol
show the reaction diagram
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?
Galbeta(1-3)GalNAcalpha(1-)OC6H4-p-NO2 + H2O
Galbeta(1-3)GalNAc + p-nitrophenol
show the reaction diagram
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?
Galbeta(1-3)GalNAcalpha(1-)OC6H5 + H2O
Galbeta(1-3)GalNAc + phenol
show the reaction diagram
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?
glycopeptide + H2O
Galbeta(1-3)GalNAc + ?
show the reaction diagram
glycoprotein + H2O
Galbeta(1-3)GalNAc + ?
show the reaction diagram
mucin + H2O
Galbeta1-3GalNAc + ?
show the reaction diagram
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desialylated bovine submaxillary mucin
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?
asialofetuin + H2O
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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at a level twice the EDTA concentration completely restores enzyme activity
Mg2+
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at a level twice the EDTA concentration completely restores enzyme activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
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2.5 mM CaCl2, 3.3% inhibition
Cys
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2 mM, 12% inhibition
Hg2+
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2 mM, complete inhibition
L-Cys
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2 mM, 12% inhibition
p-chloromercuribenzenesulfonate
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1 mM, 60% inhibition
p-Nitrophenyl-2-acetamido-2-deoxy-3-O-beta-D-galactopyranosyl-beta-D-galactopyranoside
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Zn2+
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2.5 mM, 66% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
asialofetuin
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0.23
Galbeta(1-3)GalNAcalpha(1-)OC6H4-o-NO2
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0.25
Galbeta(1-3)GalNAcalpha(1-)OC6H4-p-NO2
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additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7
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about 50% of maximal activity at pH 5.5 and at pH 7.0
6 - 8.8
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pH 6.0: about 40% of maximal activity, pH 8.8: about 60% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
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gel filtration
190000
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x * 190000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 190000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 2 months, stable
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-20°C, stable for 3 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kobata, A.; Takasaki, S.
endo-beta-Galactosidase and endo-alpha-N-acetylgalactosaminidase from Diplococcus pneumoniae
Methods Enzymol.
50
560-584
1978
Streptococcus pneumoniae
Manually annotated by BRENDA team
Endo, Y.; Kobata, A.
Partial purification and characterization of an endo-alpha-N-acetylgalactosaminidase from the culture medium of Diplococcus pneumoniae
J. Biochem.
80
1-8
1976
Streptococcus pneumoniae
Manually annotated by BRENDA team
Umemoto, J.; Matta, K.L.; Barlow, J.J.; Bhavanandan, V.P.
Action of endo-alpha-N-acetyl-D-galactosaminidase on synthetic glycosides including chromogenic substrates
Anal. Biochem.
91
186-193
1978
Streptococcus pneumoniae
Manually annotated by BRENDA team
Umemoto, J.; Bhavanandan, V.P.; Davidson, E.A.
Purification and properties of an endo-alpha-N-acetyl-D-galactosaminidase from Diplococcus pneumoniae
J. Biol. Chem.
252
8609-8614
1977
Streptococcus pneumoniae
Manually annotated by BRENDA team
Bhavanandan, V.P.; Umemoto, J.; Davidson, E.A.
Characterization of an endo-alpha-N-acetyl galactosaminidase from Diplococcus pneumoniae
Biochem. Biophys. Res. Commun.
70
738-745
1976
Streptococcus pneumoniae
Manually annotated by BRENDA team
Glasgow, L.R.; Paulson, J.C.; Hill, R.L.
Systematic purification of five glycosidases from Streptococcus (Diplococcus) pneumoniae
J. Biol. Chem.
252
8615-8623
1977
Streptococcus pneumoniae
Manually annotated by BRENDA team
Fan, J.Q.; Yamamoto, K.; Matsumoto, Y.; Hirabayashi, Y.; Kumagai, H.; Tochikura, T.
Action of endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp. on amino acid-O-glycans: comparison with the enzyme from Diplococcus pneumoniae
Biochem. Biophys. Res. Commun.
169
751-757
1990
Alcaligenes sp., Streptococcus pneumoniae
Manually annotated by BRENDA team
Brooks, M.M.; Savage, A.V.
The substrate specificity of the enzyme endo-alpha-N-acetyl-D-galactosaminidase from Diplococcus pneumonia
Glycoconj. J.
14
183-190
1997
Streptococcus pneumoniae
Manually annotated by BRENDA team