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Information on EC 3.2.1.97 - endo-alpha-N-acetylgalactosaminidase and Organism(s) Bifidobacterium longum and UniProt Accession Q3T552
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3.2.1.97 endo-alpha-N-acetylgalactosaminidaseIUBMB 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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Word Map
- 3.2.1.97
-
o-linked
- neuraminidase
-
o-glycosidic
- n-acetylgalactosamine
- sialidase
-
mucin-type
- asialofetuin
-
o-glycanase
-
bifidobacterial
-
thomsen-friedenreich
- analysis
- galbeta1,3galnac
-
diplococcus
- synthesis
The taxonomic range for the selected organisms is: Bifidobacterium longum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
endo-alpha-n-acetylgalactosaminidase, engcp, engbf, nagbb, spgh101, endo-alpha-galnac-ase, endo-ef, endo-beta-n-acetylgalactosaminidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylgalactosaminidase, endo-alpha
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-
-
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D-galactosyl-N-acetyl-alpha-D-galactosamine D-galactosyl-N-acetylgalactosaminohydrolase
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-
-
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endo-alpha-acetylgalactosaminidase
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-
-
-
endo-alpha-N-acetylgalactosaminidase
additional information
-
the enzyme belongs to the glycoside hydrolase family 101, GH101
endo-alpha-N-acetylgalactosaminidase
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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-
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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
59793-96-3
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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
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-serine-[protein] + H2O
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-serine-[protein]
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-threonine-[protein] + H2O
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-threonine-[protein]
Galbeta(1,3)GalNAc-asialofetuin + H2O
Galbeta(1,3)GalNAc + asialofetuin
pH 5.0, 37°C
-
-
?
Galbeta(1-3)GalNAcalpha1-p-nitrophenol + H2O
Galbeta(1-3)GalNAc + p-nitrophenol
-
-
-
?
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-serine-[protein] + H2O
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-serine-[protein]
-
-
-
?
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-threonine-[protein] + H2O
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-threonine-[protein]
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-
-
?
4-nitrophenyl beta-D-Gal-(1->3)-alpha-D-GalNAc + H2O
4-nitrophenol + beta-D-Gal-(1->3)-alpha-D-GalNAc
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-
-
-
?
Gal-beta-1,3-GalNAc-alpha-1p-nitrophenol + H2O
p-nitrophenol + Gal-beta-1,3-GalNAc
pH 5.0, 37°C
-
-
?
gastric mucin + H2O
disaccharide + ?
-
EngBF does not release oligosaccharides from intact gastric mucin, but releases core 1 disaccharide from the gastric mucin pretreated with commercial sialidase and with the recombinant exo-alpha-N-acetylglucosamindase
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-
?
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-serine-[protein] + H2O
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-serine-[protein]
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-
-
?
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-serine-[protein] + H2O
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-serine-[protein]
-
-
-
?
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-threonine-[protein] + H2O
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-threonine-[protein]
-
-
-
?
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-threonine-[protein] + H2O
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-threonine-[protein]
-
-
-
?
Galbeta(1,3)GalNAcalpha-1-p-nitrophenol + H2O
p-nitrophenol + Galbeta(1,3)GalNAc
pH 5.0, 37°C
-
-
?
Galbeta(1,3)GalNAcalpha-1-p-nitrophenol + H2O
p-nitrophenol + Galbeta(1,3)GalNAc
pH 5.0, 37°C
-
-
?
additional information
?
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-
Galbeta(1,3)GalNAc disaccharide is liberated from asialofetuin and p-nitrophenol substrate containing the core 1 structure (Galbeta(1,3)GalNAcalpha-1), but not from sialofetuin or any p-nitrophenol substrate other than Galbeta(1,3)GalNAcalpha-1-p-nitrophenol
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-
?
additional information
?
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Galbeta(1,3)GalNAc disaccharide is liberated from asialofetuin and p-nitrophenol substrate containing the core 1 structure (Galbeta(1,3)GalNAcalpha-1), but not from sialofetuin or any p-nitrophenol substrate other than Galbeta(1,3)GalNAcalpha-1-p-nitrophenol
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-
?
additional information
?
-
no reaction with Galbeta(1,3)(GlcNAcbeta(1,6))GalNAcalpha-1-p-nitrophenol, GalNAcalpha-1-p-nitrophenol, GlcNAcbeta(1,3)GalNAcalpha-1-p-nitrophenol and Galbeta(1,3)GlcNAcalpha-1-p-nitrophenol
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-
?
additional information
?
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no reaction with Galbeta(1,3)(GlcNAcbeta(1,6))GalNAcalpha-1-p-nitrophenol, GalNAcalpha-1-p-nitrophenol, GlcNAcbeta(1,3)GalNAcalpha-1-p-nitrophenol and Galbeta(1,3)GlcNAcalpha-1-p-nitrophenol
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-
?
additional information
?
-
the enzyme also exhibits transglycosylation activity towards various mono- and disaccharides and 1-alkanols. No activity with GalNAc-p-nitrophenol, Galbeta(1-3)(GlcNAcbeta(1-6))GalNAc-p-nitrophenol, GlcNAcbeta(1-3)GalNAc-p-nitrophenol, Galbeta(1-3)GlcNAc-p-nitrophenol. Does not release sialo-oligosaccharides from fetuin
-
-
?
additional information
?
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-
the enzyme also exhibits transglycosylation activity towards various mono- and disaccharides and 1-alkanols. No activity with GalNAc-p-nitrophenol, Galbeta(1-3)(GlcNAcbeta(1-6))GalNAc-p-nitrophenol, GlcNAcbeta(1-3)GalNAc-p-nitrophenol, Galbeta(1-3)GlcNAc-p-nitrophenol. Does not release sialo-oligosaccharides from fetuin
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-
?
additional information
?
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-
EngCP from Clostridium perfringens possesses broader substrate specificity than EngBF
-
-
?
additional information
?
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-
EngBF preferably releases Galbeta1-3GalNAc from the core 1-type O-glycan, i.e. Thomsen-Friedenreich antigen or T-antigen, of mucin glycoproteins. EngBF also shows transglycosylation activity of the released disaccharide to other mono- and disaccharides
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-
?
additional information
?
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the enzyme hydrolyses the O-glycosidic bonds in mucin-type O-glycan between alpha-GalNAc and Ser/Thr. EngBF is highly specific for the core 1-type O-glycan to release the disaccharide Galbeta1-3GalNAc
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-
?
additional information
?
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active site structure and substrate binding by the enzyme, important residues for substrate binding are Trp residues Trp748 and Trp750, appearing to form stacking interactions with the beta-faces of sugar rings of Galbeta1-3GalNAc by substrate-induced fit, substrate specificity for glycans, docking analysis, detailed overview
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-
?
additional information
?
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endo-alpha-N-acetylgalactosaminidase catalyzes the release of Galbeta1-3GalNAc from the core 1-type O-glycan, Galbeta1-3GalNAcalpha1-Ser/Thr, of mucin glycoproteins and synthetic 4-nitrophenyl alpha-linked substrates. The enzyme directly transfers Galbeta1-3GalNAc to serine or threonine residues of bioactive peptides such as PAMP-12, bradykinin, peptide-TandMUC1a when Galbeta1-3GalNAcalpha1-4NP was used as a donor substrate. The enzyme also catalyzes the reverse-hydrolysis reaction. EngBF synthesizes the core 1 disaccharide-containing oligosaccharides when the enzyme is incubated with either glucose or lactose and Galbeta1-3GalNAc
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-
?
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
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-serine-[protein] + H2O
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-serine-[protein]
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-threonine-[protein] + H2O
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-threonine-[protein]
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-serine-[protein] + H2O
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-serine-[protein]
-
-
-
?
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-threonine-[protein] + H2O
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-threonine-[protein]
-
-
-
?
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-serine-[protein] + H2O
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-serine-[protein]
-
-
-
?
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-serine-[protein] + H2O
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-serine-[protein]
-
-
-
?
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-threonine-[protein] + H2O
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-threonine-[protein]
-
-
-
?
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-threonine-[protein] + H2O
3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-threonine-[protein]
-
-
-
?
additional information
?
-
-
EngBF preferably releases Galbeta1-3GalNAc from the core 1-type O-glycan, i.e. Thomsen-Friedenreich antigen or T-antigen, of mucin glycoproteins. EngBF also shows transglycosylation activity of the released disaccharide to other mono- and disaccharides
-
-
?
additional information
?
-
-
the enzyme hydrolyses the O-glycosidic bonds in mucin-type O-glycan between alpha-GalNAc and Ser/Thr. EngBF is highly specific for the core 1-type O-glycan to release the disaccharide Galbeta1-3GalNAc
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
EngBF is not significantly inhibited by divalent cations
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0218
Galbeta(1,3)GalNAcalpha-1-p-nitrophenol
wild-type, pH 5.0, 37°C
0.0384
Galbeta(1,3)GalNAcalpha-1-p-nitrophenol
mutant D762A, pH 5.0, 37°C
0.107
Galbeta(1,3)GalNAcalpha-1-p-nitrophenol
mutant E822A, pH 5.0, 37°C
0.0384
Galbeta(1-3)GalNAcalpha1-p-nitrophenol
mutant enzyme D762A
0.107
Galbeta(1-3)GalNAcalpha1-p-nitrophenol
mutant enzyme E822A
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.23
Galbeta(1,3)GalNAcalpha-1-p-nitrophenol
mutant E822A, pH 5.0, 37°C
8.17
Galbeta(1,3)GalNAcalpha-1-p-nitrophenol
mutant D762A, pH 5.0, 37°C
0.23
Galbeta(1-3)GalNAcalpha1-p-nitrophenol
mutant enzyme E822A
8.17
Galbeta(1-3)GalNAcalpha1-p-nitrophenol
mutant enzyme D762A
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
optimal pH between pH 5-6 for all hydrolyzable substrates of EngBF
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
docking analysis and structural model building, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme, X-ray diffraction structure analysis at 2.0-2.5 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D1058N
activity in cell-free extracts of Escherichia coli almost comparable to wild-type
D1106N
D601N
D605N
D612N
D655N
D665N
D682N
D700N
D762A
D762N
D789N
D839N
D864N
D898N
E1276Q
E1302Q
E1350Q
E679Q
E723Q
E822A
E828Q
E882Q
Escherichia coli cells expressing the mutant enzyme exhibit less than 2% of the wild-type endo-alpha-GalNAc activity
S1248N
Escherichia coli cells expressing the mutant enzyme exhibit 10-30% of the wild-type endo-alpha-GalNAc activity
D1295A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the truncated wild-type enzyme
D682A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the truncated wild-type enzyme
D789A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the truncated wild-type enzyme
E822A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the truncated wild-type enzyme
K1199A
-
site-directed mutagenesis, the mutant shows increased activity compared to the truncated wild-type enzyme
N720A
-
site-directed mutagenesis, the mutant shows increased activity compared to the truncated wild-type enzyme
Q894A
-
site-directed mutagenesis, the mutant shows increased activity compared to the truncated wild-type enzyme
W748A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the truncated wild-type enzyme
W748F
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the truncated wild-type enzyme
W748Y
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the truncated wild-type enzyme
W750A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the truncated wild-type enzyme
W750F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the truncated wild-type enzyme
W750Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the truncated wild-type enzyme
Y787F
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the truncated wild-type enzyme
D1106N
Escherichia coli cells expressing the mutant enzyme exhibit 10-30% of the wild-type endo-alpha-GalNAc activity
D601N
activity in cell-free extracts of Escherichia coli almost comparable to wild-type
D601N
Escherichia coli cells expressing the mutant enzyme exhibit endo-alpha-GalNAc activity almost comparable with that of the cells carrying wild-type
D605N
Escherichia coli cells expressing the mutant enzyme exhibit 10-30% of the wild-type endo-alpha-GalNAc activity
D612N
activity in cell-free extracts of Escherichia coli almost comparable to wild-type
D612N
Escherichia coli cells expressing the mutant enzyme exhibit endo-alpha-GalNAc activity almost comparable with that of the cells carrying wild-type
D655N
Escherichia coli cells expressing the mutant enzyme exhibit 10-30% of the wild-type endo-alpha-GalNAc activity
D665N
activity in cell-free extracts of Escherichia coli almost comparable to wild-type
D665N
Escherichia coli cells expressing the mutant enzyme exhibit endo-alpha-GalNAc activity almost comparable with that of the cells carrying wild-type
D682N
Escherichia coli cells expressing the mutant enzyme exhibit less than 2% of the wild-type endo-alpha-GalNAc activity
D700N
activity in cell-free extracts of Escherichia coli almost comparable to wild-type
D700N
Escherichia coli cells expressing the mutant enzyme exhibit endo-alpha-GalNAc activity almost comparable with that of the cells carrying wild-type
D762N
Escherichia coli cells expressing the mutant enzyme exhibit less than 2% of the wild-type endo-alpha-GalNAc activity
D789N
Escherichia coli cells expressing the mutant enzyme exhibit less than 2% of the wild-type endo-alpha-GalNAc activity
D839N
activity in cell-free extracts of Escherichia coli almost comparable to wild-type
D839N
Escherichia coli cells expressing the mutant enzyme exhibit endo-alpha-GalNAc activity almost comparable with that of the cells carrying wild-type
D864N
activity in cell-free extracts of Escherichia coli almost comparable to wild-type
D864N
Escherichia coli cells expressing the mutant enzyme exhibit endo-alpha-GalNAc activity almost comparable with that of the cells carrying wild-type
D898N
activity in cell-free extracts of Escherichia coli almost comparable to wild-type
D898N
Escherichia coli cells expressing the mutant enzyme exhibit endo-alpha-GalNAc activity almost comparable with that of the cells carrying wild-type
E1276Q
Escherichia coli cells expressing the mutant enzyme exhibit 10-30% of the wild-type endo-alpha-GalNAc activity
E1302Q
activity in cell-free extracts of Escherichia coli almost comparable to wild-type
E1302Q
Escherichia coli cells expressing the mutant enzyme exhibit endo-alpha-GalNAc activity almost comparable with that of the cells carrying wild-type
E1350Q
activity in cell-free extracts of Escherichia coli almost comparable to wild-type
E1350Q
Escherichia coli cells expressing the mutant enzyme exhibit endo-alpha-GalNAc activity almost comparable with that of the cells carrying wild-type
E679Q
activity in cell-free extracts of Escherichia coli almost comparable to wild-type
E679Q
Escherichia coli cells expressing the mutant enzyme exhibit endo-alpha-GalNAc activity almost comparable with that of the cells carrying wild-type
E723Q
Escherichia coli cells expressing the mutant enzyme exhibit 10-30% of the wild-type endo-alpha-GalNAc activity
E828Q
Escherichia coli cells expressing the mutant enzyme exhibit 10-30% of the wild-type endo-alpha-GalNAc activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
37
the enzyme is stable up to 37°C and retains 73% activity after incubation at 45°C for 30 min in 50 mM acetate buffer (pH 5.0)
37
the enzyme is stable up to 37°C and retains 73% activity after incubation at 45°C for 30 min in 50 mM acetate buffer (pH 5.0)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged EngBF from Escherichia coli strain BL21(DE3) by affinity chromatography and gel filtration
-
recombinant His-tagged EngBF truncation and point mutants from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, wild-type and mutants D601N, D605N, D612N, D655N, D665N, E679Q, D682N, D682A, D700N, E723Q, D762N, D762A, D789N, D789A, E822Q, E822A, E828Q, D839N, D864N, D898N, D1058N, D1106N, D1248N, E1276Q, E1302Q, E1350Q
expression of His-tagged truncated EngBF mutants, comprising residues 340-1528 and 340-1694, respectively, and point mutants in Escherichia coli strain BL21(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujita, K.; Oura, F.; Nagamine, N.; Katayama, T.; Hiratake, J.; Sakata, K.; Kumagai, H.; Yamamoto, K.
Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-glycan-specific endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum
J. Biol. Chem.
280
37415-37422
2005
Bifidobacterium longum (Q3T552), Bifidobacterium longum, Bifidobacterium longum JCM 1217 (Q3T552)
Katayama, T.; Fujita, K.; Yamamoto, K.
Novel bifidobacterial glycosidases acting on sugar chains of mucin glycoproteins
J. Biosci. Bioeng.
99
457-465
2005
Bifidobacterium bifidum, Bifidobacterium bifidum ATCC 29521, Bifidobacterium bifidum JCM 7004, Bifidobacterium breve, Bifidobacterium breve JCM 1192, Bifidobacterium longum, Bifidobacterium longum (Q3T552), Bifidobacterium longum JCM 1217 (Q3T552), Bifidobacterium longum JCM 7054
Ashida, H.; Maki, R.; Ozawa, H.; Tani, Y.; Kiyohara, M.; Fujita, M.; Imamura, A.; Ishida, H.; Kiso, M.; Yamamoto, K.
Characterization of two different endo-alpha-N-acetylgalactosaminidases from probiotic and pathogenic enterobacteria, Bifidobacterium longum and Clostridium perfringens
Glycobiology
18
727-734
2008
Bifidobacterium longum, Clostridium perfringens (Q8XMJ5), Clostridium perfringens, Clostridium perfringens 13 (Q8XMJ5)
Ashida, H.; Ozawa, H.; Fujita, K.; Suzuki, S.; Yamamoto, K.
Syntheses of mucin-type O-glycopeptides and oligosaccharides using transglycosylation and reverse-hydrolysis activities of Bifidobacterium endo-alpha-N-acetylgalactosaminidase
Glycoconj. J.
27
125-132
2010
Bifidobacterium longum, Bifidobacterium longum JCM 1217
Suzuki, R.; Katayama, T.; Kitaoka, M.; Kumagai, H.; Wakagi, T.; Shoun, H.; Ashida, H.; Yamamoto, K.; Fushinobu, S.
Crystallographic and mutational analyses of substrate recognition of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum
J. Biochem.
146
389-398
2009
Bifidobacterium longum
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