Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,4-dinitrophenyl beta-D-Gal-(1->3)-alpha-D-GalNAc + H2O
2,4-dinitrophenol + beta-D-Gal-(1->3)-alpha-D-GalNAc
-
-
-
?
2,4-dinitrophenyl-GalNAc-alpha-R + H2O
2,4-dinitrophenol + GalNAc-alpha-R
-
-
-
?
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]
4,6-dimethoxy-1,3,5-triazin-2-yl alpha-N-acetylgalactosaminide + H2O
?
-
-
-
?
4-nitrophenyl 2-(acetylamino)-2-deoxy-alpha-D-galactopyranoside + H2O
4-nitrophenol + N-acetyl-alpha-D-galactosamine
4-nitrophenyl 2-acetamido-2-deoxy-3-O-(beta-D-galactopyranosyl)-alpha-D-galactopyranoside + H2O
4-nitrophenol + 3-O-beta-D-galactopyranosyl-2-acetamido-2-deoxy-alpha-D-galactopyranose
-
-
-
-
?
4-nitrophenyl beta-D-Gal-(1->3)-alpha-D-GalNAc + H2O
4-nitrophenol + beta-D-Gal-(1->3)-alpha-D-GalNAc
4-nitrophenyl-N-acetyl-beta-D-galactosaminide + H2O
4-nitrophenol + N-acetyl-beta-D-galactosamine
-
-
-
?
4-nitrophenyl-N-acetyl-beta-D-galactosaminide + L-Ser
?
transglycosylation
-
-
?
asialo kappa-casein + H2O
Galbeta(1-3)GalNAc + ?
asialo-fetuin + H2O
?
-
almost complete removal of O-linked Galbeta1-3GalNAc, the product has a decreased trypsin inhibitory activity
-
?
asialo-kappa-casein + H2O
Galbeta(1-3)GalNAc + ?
asialofetuin + H2O
Galbeta(1-3)GalNAc + ?
asialoglycophorin + H2O
Galbeta(1-3)GalNAc + ?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + 1-butanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-butyl + p-nitrophenol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + 1-heptanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-heptyl + p-nitrophenol
-
transfer ratio in presence of sodium cholate is 22.7%
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + 1-hexanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-hexyl + p-nitrophenol
-
transfer ratio in presence of sodium cholate is 58.8%
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + 1-octanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-1-octyl + p-nitrophenol
-
transfer ratio in presence of sodium cholate is 14.9%
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + 1-pentanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-pentyl + p-nitrophenol
-
transfer ratio in presence of sodium cholate is 73.3%
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + 1-propanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-propyl + p-nitrophenol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + 2-benzyloxy-1-pentanol
?
-
transfer ratio in presence of sodium cholate is 56.3%
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + 2-benzyloxyethanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-(2-benzyloxyethyl) + p-nitrophenol
-
transfer ratio in presence of sodium cholate is 80.8%
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + allyl alcohol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-allyl + p-nitrophenol
-
transfer ratio in presence of sodium cholate is 86.8%
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + benzyloxycarbonyl-Leu-Ser-Gln-Val-His-Arg
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-(CBZ-Leu)-Ser-Gln-Val-His-Arg + p-nitrophenol
-
-
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + diethylene glycol monomethyl ether
?
-
transfer ratio in presence of sodium cholate is 78.6%
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + ethanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-ethyl + p-nitrophenol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + ethylene glycol monomethyl ether
?
-
transfer ratio in presence of sodium cholate is 79.4%
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + methanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-methyl + p-nitrophenol
dansyl-Ser-GalNAc-Gal + H2O
dansyl-Ser + GalNAc-Gal + H2O
-
-
-
?
dansyl-Thr-GalNAc-Gal + H2O
dansyl-Thr + GalNAc-Gal + H2O
-
-
-
?
Gal-beta-1,3-GalNAc-alpha-1p-nitrophenol + H2O
p-nitrophenol + Gal-beta-1,3-GalNAc
Galbeta(1,3)GalNAc-asialofetuin + H2O
Galbeta(1,3)GalNAc + asialofetuin
pH 5.0, 37°C
-
-
?
Galbeta(1,3)GalNAcalpha-1-p-nitrophenol + H2O
p-nitrophenol + Galbeta(1,3)GalNAc
Galbeta(1-3)GalNAcalpha(1-)OC6H4-o-NO2 + H2O
Galbeta(1-3)GalNAc + o-nitrophenol
-
-
-
-
?
Galbeta(1-3)GalNAcalpha(1-)OC6H4-p-NO2 + H2O
Galbeta(1-3)GalNAc + p-nitrophenol
-
-
-
-
?
Galbeta(1-3)GalNAcalpha(1-)OC6H5 + H2O
Galbeta(1-3)GalNAc + phenol
-
-
-
-
?
Galbeta(1-3)GalNAcalpha(1-)p-nitrophenyl + galactose
?
-
transglycosylation
-
-
?
Galbeta(1-3)GalNAcalpha(1-)p-nitrophenyl + glucose
?
-
transglycosylation
-
-
?
Galbeta(1-3)GalNAcalpha(1-)p-nitrophenyl + H2O
Galbeta(1-3)GalNAc + p-nitrophenol
-
-
-
-
?
Galbeta(1-3)GalNAcalpha(1-)p-nitrophenyl + maltose
?
-
transglycosylation
-
-
?
Galbeta(1-3)GalNAcalpha(1-)p-nitrophenyl + mannitol
?
-
transglycosylation
-
-
?
Galbeta(1-3)GalNAcalpha(1-)p-nitrophenyl + mannose
?
-
transglycosylation
-
-
?
Galbeta(1-3)GalNAcalpha(1-)p-nitrophenyl + sorbitol
?
-
transglycosylation
-
-
?
Galbeta(1-3)GalNAcalpha(1-)p-nitrophenyl + sucrose
?
-
transglycosylation
-
-
?
Galbeta(1-3)GalNAcalpha1-p-nitrophenol + H2O
Galbeta(1-3)GalNAc + p-nitrophenol
-
-
-
?
Galbeta1-3(GlcNAcbeta1-6)GalNAcalpha1-pNP + H2O
?
Galbeta1-3GalNAcalpha-pNP + H2O
Galbeta1-3GalNAc + p-nitrophenol
Galbeta1-3GalNAcalpha1-pNP + H2O
?
Galbeta1-3[Galbeta1-3GlcNAcbeta1-6]GalNAcalpha-pNP + H2O
?
Galbeta1-3[GlcNAcbeta1-6]GalNAcalpha1-pNP + H2O
?
GalNAcbeta1-3GalNAcalpha1-pNP + H2O
?
gastric mucin + H2O
disaccharide + ?
Glc-NAcbeta1-3GalNAcalpha1-pNP + H2O
?
-
-
-
?
Glcbeta1-3GalNAcalpha1-pNP + H2O
?
GlcNAcbeta1-3GalNAcalpha1-pNP + H2O
?
glycopeptide + H2O
Galbeta(1-3)GalNAc + ?
glycoprotein + H2O
Galbeta(1-3)GalNAc + ?
mucin + H2O
Galbeta1-3GalNAc + ?
Tn antigen + H2O
?
i.e. N-acetyl-beta-D-galactosaminyl-L-Ser/Thr
-
-
?
asialofetuin + H2O
additional information
-
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-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-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-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-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]
-
-
-
-
?
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]
-
-
-
-
?
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]
-
-
-
?
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]
-
-
-
?
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]
-
-
-
-
?
4-nitrophenyl 2-(acetylamino)-2-deoxy-alpha-D-galactopyranoside + H2O
4-nitrophenol + N-acetyl-alpha-D-galactosamine
1.8% relative activity
-
-
?
4-nitrophenyl 2-(acetylamino)-2-deoxy-alpha-D-galactopyranoside + H2O
4-nitrophenol + N-acetyl-alpha-D-galactosamine
1.8% relative activity
-
-
?
4-nitrophenyl 2-(acetylamino)-2-deoxy-alpha-D-galactopyranoside + H2O
4-nitrophenol + N-acetyl-alpha-D-galactosamine
-
-
-
?
4-nitrophenyl 2-(acetylamino)-2-deoxy-alpha-D-galactopyranoside + H2O
4-nitrophenol + N-acetyl-alpha-D-galactosamine
-
-
-
?
4-nitrophenyl beta-D-Gal-(1->3)-alpha-D-GalNAc + H2O
4-nitrophenol + beta-D-Gal-(1->3)-alpha-D-GalNAc
-
-
-
-
?
4-nitrophenyl beta-D-Gal-(1->3)-alpha-D-GalNAc + H2O
4-nitrophenol + beta-D-Gal-(1->3)-alpha-D-GalNAc
-
-
-
-
?
4-nitrophenyl beta-D-Gal-(1->3)-alpha-D-GalNAc + H2O
4-nitrophenol + beta-D-Gal-(1->3)-alpha-D-GalNAc
-
-
-
?
asialo kappa-casein + H2O
Galbeta(1-3)GalNAc + ?
-
-
-
-
?
asialo kappa-casein + H2O
Galbeta(1-3)GalNAc + ?
-
-
-
-
?
asialo kappa-casein + H2O
Galbeta(1-3)GalNAc + ?
-
-
-
-
?
asialo kappa-casein + H2O
Galbeta(1-3)GalNAc + ?
-
-
-
-
?
asialo kappa-casein + H2O
Galbeta(1-3)GalNAc + ?
-
-
-
-
?
asialo-kappa-casein + H2O
Galbeta(1-3)GalNAc + ?
-
-
-
-
?
asialo-kappa-casein + H2O
Galbeta(1-3)GalNAc + ?
-
-
-
-
?
asialofetuin + H2O
?
-
-
-
?
asialofetuin + H2O
?
-
-
-
?
asialofetuin + H2O
Galbeta(1-3)GalNAc + ?
-
-
-
?
asialofetuin + H2O
Galbeta(1-3)GalNAc + ?
-
-
-
?
asialoglycophorin + H2O
Galbeta(1-3)GalNAc + ?
-
-
-
-
?
asialoglycophorin + H2O
Galbeta(1-3)GalNAc + ?
-
-
-
?
asialoglycophorin + H2O
Galbeta(1-3)GalNAc + ?
-
-
-
-
?
asialoglycophorin + H2O
Galbeta(1-3)GalNAc + ?
-
asialoglycophorin A
-
-
?
asialoglycophorin + H2O
Galbeta(1-3)GalNAc + ?
-
-
-
-
?
asialoglycophorin + H2O
Galbeta(1-3)GalNAc + ?
-
-
-
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + 1-butanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-butyl + p-nitrophenol
-
transfer ratio in presence of sodium cholate is 85.6%
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + 1-butanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-butyl + p-nitrophenol
-
transfer ratio in presence of sodium cholate is 85.6%
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + 1-propanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-propyl + p-nitrophenol
-
transfer ratio in presence of sodium cholate is 76.8%
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + 1-propanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-propyl + p-nitrophenol
-
transfer ratio in presence of sodium cholate is 76.8%
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + ethanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-ethyl + p-nitrophenol
-
transfer ratio in presence of sodium cholate is 65.0%
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + ethanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-ethyl + p-nitrophenol
-
transfer ratio in presence of sodium cholate is 65.0%
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + methanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-methyl + p-nitrophenol
-
transfer ratio in presence of sodium cholate is 70.8%
-
?
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-p-nitrophenyl + methanol
beta-D-Gal-(1-3)-alpha-D-GalNAc-(1-O)-methyl + p-nitrophenol
-
transfer ratio in presence of sodium cholate is 70.8%
-
?
fetuin + H2O
?
the enzyme catalyzes the cleavage of core 1 and core 3 type O-linked disaccharides between GalNAc and serine or threonine residues from glycoproteins
-
-
?
fetuin + H2O
?
-
hydrolysis of the O-glycosidic linkage between GalNAc and Ser or Thr
-
-
?
fetuin + H2O
?
-
hydrolysis of the O-glycosidic linkage between GalNAc and Ser or Thr
-
-
?
Gal-beta-1,3-GalNAc-alpha-1p-nitrophenol + H2O
p-nitrophenol + Gal-beta-1,3-GalNAc
pH 5.0, 37°C
-
-
?
Gal-beta-1,3-GalNAc-alpha-1p-nitrophenol + H2O
p-nitrophenol + Gal-beta-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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
Galbeta(1,3)GalNAcalpha-1-p-nitrophenol + H2O
p-nitrophenol + Galbeta(1,3)GalNAc
pH 5.0, 37°C
-
-
?
Galbeta1-3(GlcNAcbeta1-6)GalNAcalpha1-pNP + H2O
?
2.3% relative activity
-
-
?
Galbeta1-3(GlcNAcbeta1-6)GalNAcalpha1-pNP + H2O
?
2.3% relative activity
-
-
?
Galbeta1-3GalNAcalpha-pNP + H2O
Galbeta1-3GalNAc + p-nitrophenol
-
-
-
?
Galbeta1-3GalNAcalpha-pNP + H2O
Galbeta1-3GalNAc + p-nitrophenol
-
-
-
?
Galbeta1-3GalNAcalpha1-pNP + H2O
?
-
100% relative activity
-
-
?
Galbeta1-3GalNAcalpha1-pNP + H2O
?
100% relative activity
-
-
?
Galbeta1-3GalNAcalpha1-pNP + H2O
?
100% relative activity
-
-
?
Galbeta1-3[Galbeta1-3GlcNAcbeta1-6]GalNAcalpha-pNP + H2O
?
-
-
-
?
Galbeta1-3[Galbeta1-3GlcNAcbeta1-6]GalNAcalpha-pNP + H2O
?
-
-
-
?
Galbeta1-3[GlcNAcbeta1-6]GalNAcalpha1-pNP + H2O
?
-
-
-
?
Galbeta1-3[GlcNAcbeta1-6]GalNAcalpha1-pNP + H2O
?
-
-
-
?
GalNAcbeta1-3GalNAcalpha1-pNP + H2O
?
-
17.3% relative activity
-
-
?
GalNAcbeta1-3GalNAcalpha1-pNP + H2O
?
21% relative activity
-
-
?
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
-
-
?
gastric mucin + H2O
disaccharide + ?
EngCP 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 cloned from the same strain of Clostridium perfringens. It does not release core 2 trisaccharide from the mucin
-
-
?
Glcbeta1-3GalNAcalpha1-pNP + H2O
?
-
35.3% relative activity
-
-
?
Glcbeta1-3GalNAcalpha1-pNP + H2O
?
156.7% relative activity
-
-
?
GlcNAcbeta1-3GalNAcalpha1-pNP + H2O
?
-
0.3% relative activity
-
-
?
GlcNAcbeta1-3GalNAcalpha1-pNP + H2O
?
3.5% relative activity
-
-
?
glycopeptide + H2O
Galbeta(1-3)GalNAc + ?
-
specific requirement for an unsubstituted galactose at the nonreducing terminus and an alpha-linkage between N-acetylgalactosamine and the aglycone
-
-
?
glycopeptide + H2O
Galbeta(1-3)GalNAc + ?
-
glycopeptides from mouse myeloma, fetuin and pig submaxillary mucin
-
?
glycopeptide + H2O
Galbeta(1-3)GalNAc + ?
-
release of Galbeta(1-3)GalNAc from glycopeptides possesing Ser or Thr O-glycosidic linkages
-
-
?
glycoprotein + H2O
Galbeta(1-3)GalNAc + ?
-
release of Galbeta(1-3)GalNAc from glycoproteins possesing Ser or Thr O-glycosidic linkages
-
?
glycoprotein + H2O
Galbeta(1-3)GalNAc + ?
-
release of Galbeta(1-3)GalNAc from glycoproteins possesing Ser or Thr O-glycosidic linkages
-
?
glycoprotein + H2O
Galbeta(1-3)GalNAc + ?
-
hydrolyzes the O-glycosidic linkage between alpha-N-acetylgalactosamine and the hydroxyl group of Ser or Thr residues in mucus and mucin-type glycoproteins
-
-
?
glycoprotein + H2O
Galbeta(1-3)GalNAc + ?
-
hydrolyzes the O-glycosidic linkage between alpha-N-acetylgalactosamine and the hydroxyl group of Ser or Thr residues in mucus and mucin-type glycoproteins
-
-
?
glycoprotein + H2O
Galbeta(1-3)GalNAc + ?
-
digestion of nerve cell surface glycoproteins or their terminal N-acetylgalactosamines, no digestion of galactosamines associated with the collagenous ligands or perineuronal proteoglycan
-
-
?
glycoprotein + H2O
Galbeta(1-3)GalNAc + ?
-
specific requirement for an unsubstituted galactose in the nonreducing terminus and an alpha-linkage between N-acetylgalactosamine and the aglycone
-
?
glycoprotein + H2O
Galbeta(1-3)GalNAc + ?
-
disialized human erythrocyte membrane glycoprotein, porcine submaxillarry mucin
no oligosaccharides larger than trisaccharides are liberated from porcine submaxillarry mucin
?
glycoprotein + H2O
Galbeta(1-3)GalNAc + ?
-
bovine submaxillary mucin, no hydrolysis of remodelled antifreeze glycoprotein containing NeuAcalpha2-3Galbeta1-3GalNAc and Galbeta1-3(NeuAcalpha2-6)GalNAc
-
-
?
glycoprotein + H2O
Galbeta(1-3)GalNAc + ?
-
release of Galbeta(1-3)GalNAc from glycoproteins possesing Ser or Thr O-glycosidic linkages
-
-
?
glycoprotein + H2O
Galbeta(1-3)GalNAc + ?
-
release of Galbeta(1-3)GalNAc from glycoproteins possesing Ser or Thr O-glycosidic linkages
no oligosaccharides larger than trisaccharides are liberated from porcine submaxillarry mucin
?
glycoprotein + H2O
Galbeta(1-3)GalNAc + ?
-
liberates Galbeta(1-3)4GalNAc and also other larger oligosaccharides by hydrolysis of O-glycosidic linkage between GalNAc and Ser or Thr
-
?
glycoprotein + H2O
Galbeta(1-3)GalNAc + ?
-
purified pig gastric mucus glycoproteins
-
-
?
glycoprotein + H2O
Galbeta(1-3)GalNAc + ?
-
liberates Galbeta(1-3)4GalNAc and also other larger oligosaccharides by hydrolysis of O-glycosidic linkage between GalNAc and Ser or Thr
-
?
glycoprotein + H2O
Galbeta(1-3)GalNAc + ?
-
purified pig gastric mucus glycoproteins
-
-
?
mucin + H2O
Galbeta1-3GalNAc + ?
-
desialylated bovine submaxillary mucin
-
?
mucin + H2O
Galbeta1-3GalNAc + ?
-
release of Galbeta(1-3)GalNAc from mucins possesing Ser or Thr O-glycosidic linkages
-
-
?
mucin + H2O
Galbeta1-3GalNAc + ?
-
release of Galbeta(1-3)GalNAc from mucins possesing Ser or Thr O-glycosidic linkages
-
-
?
asialofetuin + H2O
additional information
-
-
-
Galbeta(1-3)GalNAc + ?
?
asialofetuin + H2O
additional information
-
-
-
Galbeta(1-3)GalNAc + ?
?
asialofetuin + H2O
additional information
-
-
-
Galbeta(1-3)GalNAc + ?
?
asialofetuin + H2O
additional information
-
-
-
-
-
?
asialofetuin + H2O
additional information
-
-
-
-
-
?
asialofetuin + H2O
additional information
-
-
-
-
-
?
asialofetuin + H2O
additional information
-
-
-
-
-
?
asialofetuin + H2O
additional information
-
-
hydrolysis of the O-glycosidic linkage between GalNAc and Ser or Thr
Galbeta(1-3)GalNAc + Galbeta(1-3)(Galbeta(1-4)GlcNAcbeta(1-6))GalNAc
?
asialofetuin + H2O
additional information
-
-
hydrolysis of the O-glycosidic linkage between GalNAc and Ser or Thr
Galbeta(1-3)GalNAc + Galbeta(1-3)(Galbeta(1-4)GlcNAcbeta(1-6))GalNAc
?
asialofetuin + H2O
additional information
-
-
-
-
-
?
additional information
?
-
-
highly induced by porcine gastric mucin
-
-
?
additional information
?
-
-
highly induced by porcine gastric mucin
-
-
?
additional information
?
-
-
the enzyme also catalyzes the transfer of beta-D-Gal-(1-3)-alpha-D-GalNAc from asialofetuin to 1-alkanols
-
?
additional information
?
-
-
the enzyme also catalyzes the transfer of beta-D-Gal-(1-3)-alpha-D-GalNAc from asialofetuin to 1-alkanols
-
?
additional information
?
-
the expression of the gene is highly induced in the presence of mucin
-
-
?
additional information
?
-
-
the expression of the gene is highly induced in the presence of mucin
-
-
?
additional information
?
-
the enzyme acts very weakly on GalNAcalpha1-UDP and GalNAcalpha(1>3)Galbeta(1>4)Glc and not at all on Neu5Acalpha(2>6)GalNAcalpha1-L-Ser (sialyl Tn antigen)and GalNAcalpha(1>3)(Fucalpha(1>2))Gal (blood group A trisaccharide). In addition, the enzyme very slowly hydrolyzes core-3 (4-nitrophenyl-GlcNAcbeta(1>3)GalNAcalpha1) and core-8 (4-nitrophenyl-Galalpha(1>3)GalNAcalpha1)-type structures but not other core structures
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
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
-
-
?
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
-
-
?
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
?
-
-
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
?
-
-
EngCP from Clostridium perfringens possesses broader substrate specificity than EngBF
-
-
?
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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
?
-
-
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
-
-
?
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
-
-
?
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
?
-
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
-
-
?
additional information
?
-
EngCP possesses broader substrate specificity than EngBF of Bifidobacterium longum, which may contribute to the pathogenicity of Clostridium perfringens. EngCP does not act on sialyl core 1 O-glycans, e.g., fetuin
-
-
?
additional information
?
-
-
EngCP possesses broader substrate specificity than EngBF of Bifidobacterium longum, which may contribute to the pathogenicity of Clostridium perfringens. EngCP does not act on sialyl core 1 O-glycans, e.g., fetuin
-
-
?
additional information
?
-
EngCP possesses broader substrate specificity than EngBF of Bifidobacterium longum, which may contribute to the pathogenicity of Clostridium perfringens. EngCP does not act on sialyl core 1 O-glycans, e.g., fetuin
-
-
?
additional information
?
-
can not release the oligosaccharide from GlcNAcbeta1-6GalNAcalpha1-pNP
-
-
?
additional information
?
-
-
can not release the oligosaccharide from GlcNAcbeta1-6GalNAcalpha1-pNP
-
-
?
additional information
?
-
can not release the oligosaccharide from GlcNAcbeta1-6GalNAcalpha1-pNP
-
-
?
additional information
?
-
-
no action on phenyl alpha-N-acetyl-D-galactosaminide, asialo ovine submaxillary mucin or monosialoganglioside
-
-
?
additional information
?
-
-
no activity when the aglycone is methanol
-
-
?
additional information
?
-
SpGH101 specifically removes an O-linked disaccharide Gal-beta-1,3-GalNAc-alpha from glycoproteins
-
-
?
additional information
?
-
-
SpGH101 specifically removes an O-linked disaccharide Gal-beta-1,3-GalNAc-alpha from glycoproteins
-
-
?
additional information
?
-
the enzyme contains several putative carbohydrate binding modules, structure-function relationship, D764 and E796 are the nucleophile and general acid-base residues, respectively, overview
-
-
?
additional information
?
-
-
the enzyme contains several putative carbohydrate binding modules, structure-function relationship, D764 and E796 are the nucleophile and general acid-base residues, respectively, overview
-
-
?
additional information
?
-
-
the enzyme is responsible for catalyzing the liberation of galactosyl beta-1,3-N-acetyl-D-galactosamine linked to serine or threonine residues of mucin-type glycoproteins
-
-
?
additional information
?
-
-
highly induced by porcine gastric mucin
-
-
?
additional information
?
-
-
enzyme production is induced by mucin, the induction is inhibited by glucose and other easily assimilable carbon sources, as well as by complex nitrogen sources, addition of palmitate, lambda-carrageenan or crude mucin to a mucin-based production medium enhances enzyme production
-
-
?
additional information
?
-
-
highly induced by porcine gastric mucin
-
-
?
additional information
?
-
-
enzyme production is induced by mucin, the induction is inhibited by glucose and other easily assimilable carbon sources, as well as by complex nitrogen sources, addition of palmitate, lambda-carrageenan or crude mucin to a mucin-based production medium enhances enzyme production
-
-
?
additional information
?
-
-
induced when asialofetuin is the sole carbon source
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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]
Tn antigen + H2O
?
i.e. N-acetyl-beta-D-galactosaminyl-L-Ser/Thr
-
-
?
additional information
?
-
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-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-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-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-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]
-
-
-
-
?
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]
-
-
-
-
?
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]
-
-
-
?
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]
-
-
-
?
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
?
-
-
highly induced by porcine gastric mucin
-
-
?
additional information
?
-
-
highly induced by porcine gastric mucin
-
-
?
additional information
?
-
the expression of the gene is highly induced in the presence of mucin
-
-
?
additional information
?
-
-
the expression of the gene is highly induced in the presence of mucin
-
-
?
additional information
?
-
the enzyme acts very weakly on GalNAcalpha1-UDP and GalNAcalpha(1>3)Galbeta(1>4)Glc and not at all on Neu5Acalpha(2>6)GalNAcalpha1-L-Ser (sialyl Tn antigen)and GalNAcalpha(1>3)(Fucalpha(1>2))Gal (blood group A trisaccharide). In addition, the enzyme very slowly hydrolyzes core-3 (4-nitrophenyl-GlcNAcbeta(1>3)GalNAcalpha1) and core-8 (4-nitrophenyl-Galalpha(1>3)GalNAcalpha1)-type structures but not other core structures
-
-
?
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
-
-
?
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
?
-
SpGH101 specifically removes an O-linked disaccharide Gal-beta-1,3-GalNAc-alpha from glycoproteins
-
-
?
additional information
?
-
-
SpGH101 specifically removes an O-linked disaccharide Gal-beta-1,3-GalNAc-alpha from glycoproteins
-
-
?
additional information
?
-
-
the enzyme is responsible for catalyzing the liberation of galactosyl beta-1,3-N-acetyl-D-galactosamine linked to serine or threonine residues of mucin-type glycoproteins
-
-
?
additional information
?
-
-
highly induced by porcine gastric mucin
-
-
?
additional information
?
-
-
enzyme production is induced by mucin, the induction is inhibited by glucose and other easily assimilable carbon sources, as well as by complex nitrogen sources, addition of palmitate, lambda-carrageenan or crude mucin to a mucin-based production medium enhances enzyme production
-
-
?
additional information
?
-
-
highly induced by porcine gastric mucin
-
-
?
additional information
?
-
-
enzyme production is induced by mucin, the induction is inhibited by glucose and other easily assimilable carbon sources, as well as by complex nitrogen sources, addition of palmitate, lambda-carrageenan or crude mucin to a mucin-based production medium enhances enzyme production
-
-
?
additional information
?
-
-
induced when asialofetuin is the sole carbon source
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D1058N
activity in cell-free extracts of Escherichia coli almost comparable to wild-type
D1248N
10-30% activity compared to wild-type
D1295A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the truncated wild-type enzyme
E822Q
significant decrease in activity (below 2%)
E882Q
Escherichia coli cells expressing the mutant enzyme exhibit less than 2% of the wild-type endo-alpha-GalNAc activity
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
S1248N
Escherichia coli cells expressing the mutant enzyme exhibit 10-30% of the wild-type endo-alpha-GalNAc activity
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
D612N
-
activity in cell-free extracts of Escherichia coli almost comparable to wild-type
-
D658A
site-directed mutagenesis, the substrate specificity and activity is altered compared to the wild-type enzyme
D764A
site-directed mutagenesis, the substrate specificity and activity is altered compared to the wild-type enzyme
D764F
site-directed mutagenesis, the substrate specificity and activity is altered compared to the wild-type enzyme
E796A
site-directed mutagenesis, the substrate specificity and activity is altered compared to the wild-type enzyme
E796Q
site-directed mutagenesis, the substrate specificity and activity is altered compared to the wild-type enzyme
D1106N
10-30% activity compared to wild-type
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
10-30% activity compared to 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
10-30% activity compared to 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
D682A
no activity
D682A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the truncated wild-type enzyme
D682N
Escherichia coli cells expressing the mutant enzyme exhibit less than 2% of the wild-type endo-alpha-GalNAc activity
D682N
significant decrease in activity (below 2%)
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
D762A
activity almost comparable to wild-type
D762A
kcat/KM is 3.9fold lower than wild-type value
D762N
Escherichia coli cells expressing the mutant enzyme exhibit less than 2% of the wild-type endo-alpha-GalNAc activity
D762N
significant decrease in activity (below 2%)
D789A
no activity
D789A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the truncated wild-type enzyme
D789N
Escherichia coli cells expressing the mutant enzyme exhibit less than 2% of the wild-type endo-alpha-GalNAc activity
D789N
significant decrease in activity (below 2%)
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
10-30% activity compared to 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
10-30% activity compared to wild-type
E723Q
Escherichia coli cells expressing the mutant enzyme exhibit 10-30% of the wild-type endo-alpha-GalNAc activity
E822A
kcat/KM is 380fold lower than wild-type value
E822A
significant decrease in kcat and slight increase in Km
E822A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the truncated wild-type enzyme
E828Q
10-30% activity compared to wild-type
E828Q
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
-
D762N
-
Escherichia coli cells expressing the mutant enzyme exhibit less than 2% of the wild-type endo-alpha-GalNAc activity
-
D762N
-
significant decrease in activity (below 2%)
-
additional information
construction of a DELTA1-39 deletion and DELTA1-39,DELTA1568-1767 deletion mutants
additional information
-
construction of a DELTA1-39 deletion and DELTA1-39,DELTA1568-1767 deletion mutants
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Kobata, A.; Takasaki, S.
endo-beta-Galactosidase and endo-alpha-N-acetylgalactosaminidase from Diplococcus pneumoniae
Methods Enzymol.
50
560-584
1978
Streptococcus pneumoniae
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Fan, J.Q.; Kadowaki, S.; Yamamoto, K.; Kumagai, H.; Tochikura, T.
Purification and characterization of endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp.
Agric. Biol. Chem.
52
1715-1723
1988
Alcaligenes sp., Alcaligenes sp. F-1906
-
brenda
Iwase, H.; Ishii, I.; Ishihara, K.; Tanaka, Y.; Omura, S.; Hotta, K.
Release of oligosaccharides possessing reducing-end N-acetylgalactosamine from mucus glycoprotein in Streptomyces sp. OH-11242 culture medium through action of endo-type glycosidase
Biochem. Biophys. Res. Commun.
151
422-428
1988
Streptomyces sp., Streptomyces sp. OH-11242
brenda
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
brenda
Yoshimoto, T.; Takahashi, E.; Tsuru, D.
Purification and enzymatic properties of an endo-alpha-N-acetylgalactosaminidase from Bacillus laterosporus SS-16
J. Ferment. Bioeng.
70
348-350
1990
Brevibacillus laterosporus, Brevibacillus laterosporus SS-16
-
brenda
Fan, J.Q.; Yamamoto, K.; Kumagai, H.; Tochikura, T.
Unique production of a disaccharide, Galbeta1->3GalNAc, by endo-alpha-N-acetylgalactosaminidase of Alcaligenes sp.
J. Ferment. Bioeng.
72
92-95
1991
Alcaligenes sp.
-
brenda
Tanaka, Y.; Takahashi, Y.; Shinose, M.; Omura, S.; Karakasa, I.I.; Iwase, H.; Hotta, K.
Screening and fermentation of endo-alpha-N-acetylgalactosaminidase S, a mucin-hydrolyzing enzyme from Streptomyces acting on the GalNAc-O-Ser(Thr) linkage
J. Ferment. Bioeng.
85
381-387
1998
Streptomyces sp., Streptomyces sp. OH-11242
-
brenda
Ashida, H.; Yamamoto, K.; Murata, T.; Usui, T.; Kumagai, H.
Characterization of endo-alpha-N-acetylgalactosaminidase from Bacillus sp. and syntheses of neo-oligosaccharides using its transglycosylation activity
Arch. Biochem. Biophys.
373
394-400
2000
Bacillus sp. (in: Bacteria)
brenda
Fan, J.Q.; Kanatani, K.; Andoh, N.; Yamamoto, K.; Kumagai, H.; Tochikura, T.
Release of T-antigen, a carcinoma marker from native human cells by endo-alpha-N-acetylgalactosaminidase of Alcaligenes sp.
Biochem. Biophys. Res. Commun.
172
341-347
1990
Alcaligenes sp.
brenda
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
brenda
Prasad, V.P.; Devaraj, H.
Production of endo-N-acetyl-galactosaminidase from a mycoparasitic fungus Gliocladium virens
Indian J. Exp. Biol.
35
405-407
1997
Trichoderma virens
-
brenda
Ishii-Karakasa, I.; Iwase, H.; Hotta, K.
Structural determination of the O-linked sialyl oligosaccharides liberated from fetuin with endo-alpha-N-acetylgalactosaminidase-S by HPLC analysis and 600-MHz 1H-NMR spectroscopy
Eur. J. Biochem.
247
709-715
1997
Streptomyces sp., Streptomyces sp. OH-11242
brenda
Ishii-Karakasa, I.; Iwase, H.; Hotta, K.; Tanaka, Y.; Omura, S.
Partial purification and characterization of an endo-alpha-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242
Biochem. J.
288
475-482
1992
Streptomyces sp., Streptomyces sp. OH-11242
brenda
Murakami, T.; Ohtsuka, A.; Su, W.D.; Taguchi, T.; Oohashi, T.; Murakami, T.; Abe, K.; Ninomiya, Y.
The extracellular matrix in the mouse brain: its reactions to endo-alpha-N-acetylgalactosaminidase and certain other enzymes
Arch. Histol. Cytol.
62
273-281
1999
Mus musculus
brenda
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
brenda
Ashida, H.; Yamamoto, K.; Kumagai, H.
Trypsin inhibitory activity of bovine fetuin de-O-glycosylated by endo-alpha-N-acetylgalactosaminidase
Biosci. Biotechnol. Biochem.
64
2266-2268
2000
Bacillus sp. (in: Bacteria)
brenda
Ajisaka, K.; Miyasato, M.; Ishii-Karakasa, I.
Efficient synthesis of O-linked glycopeptide by a transglycosylation using endo alpha-N-acetylgalactosaminidase from Streptomyces sp
Biosci. Biotechnol. Biochem.
65
1240-1243
2001
Streptomyces sp.
brenda
Ashida, H.; Yamamoto, K.; Kumagai, H.
Enzymatic syntheses of T antigen-containing glycolipid mimicry using the transglycosylation activity of endo-alpha-N-acetylgalactosaminidase
Carbohydr. Res.
330
487-493
2001
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) A198
brenda
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)
brenda
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 breve, Bifidobacterium longum, Bifidobacterium longum (Q3T552), Bifidobacterium breve JCM 1192, Bifidobacterium bifidum ATCC 29521, Bifidobacterium longum JCM 7054, Bifidobacterium longum JCM 1217 (Q3T552), Bifidobacterium bifidum JCM 7004
brenda
Ruas-Madiedo, P.; Gueimonde, M.; Fernandez-Garcia, M.; de los Reyes-Gavilan, C.G.; Margolles, A.
Mucin degradation by Bifidobacterium strains isolated from the human intestinal microbiota
Appl. Environ. Microbiol.
74
1936-1940
2008
Bifidobacterium bifidum (B2C4H5), Bifidobacterium bifidum
brenda
Goda, H.M.; Ushigusa, K.; Ito, H.; Okino, N.; Narimatsu, H.; Ito, M.
Molecular cloning, expression, and characterization of a novel endo-alpha-N-acetylgalactosaminidase from Enterococcus faecalis
Biochem. Biophys. Res. Commun.
375
541-546
2008
Enterococcus faecalis (Q833X5), Enterococcus faecalis, Enterococcus faecalis NBRC3971 (Q833X5)
brenda
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)
brenda
Gregg, K.J.; Boraston, A.B.
Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of a family 101 glycoside hydrolase from Streptococcus pneumoniae
Acta Crystallogr. Sect. F
65
133-135
2009
Streptococcus pneumoniae TIGR4
brenda
Willis, L.M.; Zhang, R.; Reid, A.; Withers, S.G.; Wakarchuk, W.W.
Mechanistic investigation of the endo-alpha-N-acetylgalactosaminidase from Streptococcus pneumoniae R6
Biochemistry
48
10334-10341
2009
Streptococcus pneumoniae R6 (Q8DR60), Streptococcus pneumoniae R6
brenda
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
brenda
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
brenda
Kiyohara, M.; Nakatomi, T.; Kurihara, S.; Fushinobu, S.; Suzuki, H.; Tanaka, T.; Shoda, S.; Kitaoka, M.; Katayama, T.; Yamamoto, K.; Ashida, H.
alpha-N-acetylgalactosaminidase from infant-associated bifidobacteria belonging to novel glycoside hydrolase family 129 is implicated in alternative mucin degradation pathway
J. Biol. Chem.
287
693-700
2012
Bifidobacterium bifidum (G5ELM1)
brenda
Morio, A.; Xu, J.; Masuda, A.; Kinoshita, Y.; Hino, M.; Morokuma, D.; Goda, H.; Okino, N.; Ito, M.; Mon, H.; Fujita, R.; Kusakabe, T.; Lee, J.
Expression, purification, and characterization of highly active endo-alpha-N-acetylgalactosaminidases expressed by silkworm-baculovirus expression system
J. Asia Pac. Entomol.
22
404-408
2019
Enterococcus faecalis (B5UB72)
-
brenda