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(2S)-3-(benzyloxy)butane-1,2,4-triol + sialylglycopeptide
?
-
transglycosylation
-
-
?
(dansyl)-labeled Man5GlcNAc2-Asn + H2O
?
(GlcNAc)2(Man)5(GlcNAc)2Asn + H2O
?
-
-
-
-
?
(GlcNAc)2(Man)6(GlcNAc)2 + H2O
GlcNAc + (GlcNAc)1(Man)6(GlcNAc)2
-
-
-
?
(Man)3(GlcNAc)2-N-Asn-dansyl + H2O
?
-
endo-beta-N-acetylglucosaminidase PII, no activity with endo-beta-N-acetylglucosaminidase PII
-
-
?
(Man)3(GlcNAc)2-N-dansyl-Asn + H2O
GlcNAc-N-dansyl-Asn + (Man)3-GlcNAc
-
-
-
?
(Man)3(GlcNAc)2Asn + H2O
(Man)3GlcNAc + GlcNAc-Asn
-
di-N-acetylchitobiosyl linkage is hydrolyzed faster than the linkage in the glycopeptides (Man)5(GlcNAc)3Asn and (Man)6(GlcNAc)2Asn by enzyme form F-I. No activity with the enzyme form F-II
-
-
?
(Man)3(GlcNAc)2Asn-Ac + H2O
(Man)3GlcNAc + GlcNAc-Asn-Ac
-
di-N-acetylchitobiosyl linkage is hydrolyzed faster than the linkage in the glycopeptides (Man)5(GlcNAc)3Asn and (Man)6(GlcNAc)2Asn by enzyme form F-I. No activity with the enzyme form F-II
-
-
?
(Man)3(Xyl)1(GlcNAc)2-pyridylamino + H2O
?
(Man)5(GlcNAc)2-Asn + H2O
?
-
-
-
?
(Man)5(GlcNAc)2-N-acetyl-Asn + H2O
(Man)5GlcNAc + GlcNAc-N-acetyl-Asn
(Man)5(GlcNAc)2-N-dansyl-Asn + H2O
GlcNAc-N-dansyl-Asn + (Man)5-GlcNAc
-
-
-
?
(Man)5(GlcNAc)2-pyridylamino + H2O
(Man)5(GlcNAc) + 2-(acetylamino)-2-deoxy-N-pyridin-2-yl-beta-D-glucopyranosylamine
(Man)5(GlcNAc)2Asn + H2O
(Man)5GlcNAc + GlcNAc-Asn
(Man)5(GlcNAc)2Asn-Ac + H2O
(Man)5GlcNAc + GlcNAc-Asn-Ac
-
di-N-acetylchitobiosyl linkage is hydrolyzed faster than the linkage in the glycopeptides (Man)5(GlcNAc)3Asn and (Man)6(GlcNAc)2Asn by enzyme form F-I
-
-
?
(Man)5GlcNAc2-pyridylamino + H2O
?
-
-
-
-
?
(Man)6(GlcNAc)2-Asn + D-glucose
(Man)6GlcNAcGlc + ?
-
-
-
?
(Man)6(GlcNAc)2-pyridylamidated + H2O
?
-
-
-
-
?
(Man)6(GlcNAc)2-pyridylamino + H2O
?
(Man)6(GlcNAc)2Asn + H2O
(Man)6GlcNAc + GlcNAc-Asn
(Man)6(GlcNAc)2Asn-Ac + H2O
(Man)6GlcNAc + GlcNAc-Asn-Ac
-
di-N-acetylchitobiosyl linkage is hydrolyzed faster than the linkage in the glycopeptides (Man)5(GlcNAc)3Asn and (Man)6(GlcNAc)2Asn by enzyme form F-I
-
-
?
(Man)6-GlcNAc-Glc-alpha-Glc + H2O
?
-
-
-
-
?
(Man)6GlcNAc2-pyridylamino + H2O
?
-
-
-
-
?
(Man)7(GlcNAc)2-pyridylamino + H2O
?
(Man)8(GlcNAc)2-pyridylamino + H2O
?
(Man)9(GlcNAc)2-pyridylamino + H2O
?
(Man)9GlcNAc2-pyridylamino + H2O
?
-
-
-
-
?
1,3-di-O-benzyl-D-erythritol + sialylglycopeptide
?
-
transglycosylation
-
-
?
2-methyl-[alpha-D-mannopyranosyl-(1,3)-beta-D-mannopyranosyl-(1,4)-alpha-D-glucopyrano]-[2,1-d]-oxazoline + N4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-1-methyl-N2-(benzyloxycarbonyl)-L-asparagine
(N4-(alpha-D-mannopyranosyl)-(1,3)-beta-D-mannopyranosyl-(1,4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-1-methyl-N2-benzyloxycarbonyl)-L-asparagine + ?
-
-
yield 81%
-
?
4-methylumbelliferyl di-N-acetyl-beta-chitobioside + H2O
?
-
-
-
-
?
4-methylumbelliferyl N,N',N''-triacetyl-beta-D-glucosaminide + H2O
4-methylumbelliferone + N,N',N''-triacetyl-beta-D-glucosaminide
-
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferol + alpha-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
4-methylumbelliferyl-beta-D-mannopyranoside + H2O
4-methylumbelliferone + beta-D-mannopyranose
4-methylumbelliferyl-beta-D-N-acetylglucosaminide + H2O
4-methylumbelliferone + beta-D-N-acetylglucosamine
-
-
-
-
?
4-methylumbelliferyl-beta-mannopyranoside + H2O
4-methylumbelliferol + beta-D-mannopyranose
-
-
-
-
?
4-nitrophenyl beta-N-acetyl-D-glucosamine + H2O
4-nitrophenol + N-acetyl-D-glucosamine
-
-
-
-
?
4-nitrophenyl-GlcNAc + Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-ManGlcNAc2]-Lys-Thr
?
-
-
-
-
?
9-fluorenylmethyloxycarbonyl-labeled asparagine-linked agalactobiantennary oligosaccharide + 4-nitrophenyl-beta-D-glucopyranoside
?
transglycosylation activity
-
-
?
9-fluorenylmethyloxycarbonyl-labeled asparagine-linked agalactobiantennary oligosaccharide + H2O
9-fluorenylmethyloxycarbonyl-labeled asparagine-linked N-acetylglucosamine (GlcNAc) + ?
-
-
-
?
9H-fluoren-9-ylmethyl [(3R)-1,3-dihydroxybutan-2-yl]carbamate + H2O
?
-
transglycosylation
-
-
?
acetyl-Asn(GlcNAc)2(Man)6 + H2O
acetyl-AsnGlcNAc
alpha-NeuAc-(2->6)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)[alpha-NeuAc-(2->6)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)]beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-Asn + H2O
?
alpha1-acid glycoprotein + H2O
?
-
-
-
-
?
asialo-N-acetyl-lactosaminic-type glycoasparagine + H2O
GlcNAc-Asn + ?
-
-
-
?
Asn(GlcNAc)2(Man)3 + H2O
?
Asn(GlcNAc)2(Man)3(Fuc)1 + H2O
?
-
-
-
-
?
Asn(GlcNAc)2-(Man)5 + H2O
AsnGlcNAc + Man5(GlcNAc)
Asn(GlcNAc)2-(Man)6 + H2O
AsnGlcNAc + (GlcNAc)1-(Man)6
Asn(GlcNAc)2-(Man)6(GlcNAc)2 + H2O
AsnGlcNAc + (GlcNAC)1-(Man)6(GlcNAc)2
Asn(GlcNAc)4(Man)6 + H2O
?
-
-
-
-
?
Asn(Man4GlcNAc4) + H2O
?
-
-
-
?
Asn-(GlcNAc)2(Man)6 + gentiobiose
?
Asn-(GlcNAc)2(Man)6 + glucose
?
Asn-Tyr-Asn(GlcNAc)2(Man)3(GlcNAc)2-(Gal)2-Lys + H2O
Asn-Tyr-Asn(GlcNAc)Lys + (Gal)2(GlcNAc)2(Man)3(GlcNAc)
-
-
-
?
beta-D-GlcNAc-(1-2)-alpha-D-Man-(1-3)-[alpha-D-Man-(1-3)-[alpha-D-Man-(1-6)]-alpha-D-Man-(1,6)]-beta-D-Man-(1-4)-beta-D-GlcNAc-(1-4)-beta-D-GlcNAc-pyridylamino
?
beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-Asn
beta-D-Man-(1->4)-beta-D-GlcNAc + beta-D-GlcNAc-Asn
-
-
-
-
?
beta-Glcp-(1-4)-GlcpNAc-oxazoline
?
-
Endo-A shows only marginal activity for transglycosylation with the disaccharide oxazoline. When used in a relatively large quantity, Endo-A can promote the transglycosylation of the disaccharide oxazoline to a GlcpNAc-Asn acceptor (it catalyzes the transfer of alpha-Manp-(1-3)-beta-Glcp-(1-4)-GlcpNAc-oxazoline to the acceptor). Endo-A promotes polymerization of beta-Glcp-(1-4)-GlcpNAc-oxazoline
-
-
?
bovine colostrum whey glycoproteins + H2O
?
bovine lactoferrin + H2O
?
calf fetuin + 4-nitrophenyl-beta-D-glucoside
?
-
-
transfer of triantennary complex type oligosaccharide, yield 3.4%
-
?
carboxypeptidase Y + Lys-Val-Ala-Asn((NeuAc-Gal-GlcNAc-Man)2Man-GlcNAc2)-Lys-Thr
?
-
-
change of hyperglycosylated protein to a sialyl complex type glycoprotein
-
?
complex-type aspargine-linked oligosaccharide + H2O
?
-
hydrolysis of the di-N-acetylchitobiose structure. The specificity for complex type oligosaccharides is probably defined by multiple domains in Endo D structure
-
-
?
dansyl asialotransferrin glycopeptide + H2O
?
dansyl derivative of Taka-amylase A glycopeptide + H2O
?
-
-
-
-
?
dansyl-Asn-(GlcNAc)2(Man)5 + H2O
dansyl-Asn-GlcNAc + ?
-
-
-
-
?
dansyl-Asn-(GlcNAc)2(Man)6 + H2O
dansyl-Asn-GlcNAc + (Man)6GlcNAc
dansyl-Asn-(GlcNAc)2(Man)6(GlcNAc)2 + H2O
?
-
-
-
-
?
dansyl-Asn-(GlcNAc)4(Man)6 + H2O
dansyl-Asn-GlcNAc + ?
dansyl-Lys-Val-Ala-Asn((NeuAc-Gal-GlcNAc-Man)2Man-GlcNAc2)-Lys-Thr + H2O
?
-
-
-
-
?
dansyl-ovalbumin-glycoprotein + H2O
?
-
-
-
-
?
dansyl-ovomucoid + H2O
?
-
-
-
-
?
dansyl-ovomucoid-glycoprotein + H2O
dansyl asparaginyl N-acetylglucosamine + ?
-
-
-
-
?
denatured RNase B + H2O
?
-
-
-
-
?
dolichyl pyrophosphoryl oligosaccharides + H2O
?
-
both glucosylated and unglucosylated polymannose oligosaccharides are released by the enzyme through cleavage of the di-N-acetylchitobiose squence
-
-
?
fluoresceinyl 2-acetamido-2-deoxy-beta-D-glucopyranoside + H2O
fluorescein + ?
-
-
-
?
fluoresceinyl di-N-acetyl-beta-chitobioside + H2O
fluorescein + ?
-
-
-
?
GlcNAc-Asn + Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAc
Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-Asn
Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAc-thiazoline is a transition state mimic and is resistant to Endo-A hydrolysis
-
-
?
GlcNAcAsn + H2O
N-acetyl-D-glucosamine + L-asparagine
glycosylated ascorbate oxidase + H2O
?
-
-
-
-
?
glycosylated human apo-transferrin + H2O
?
-
-
-
-
?
glycosylated mAb 2G12 + H2O
?
-
-
-
-
?
glycosylated type VI-A horseraddish peroxidase + H2O
?
-
-
-
-
?
H-Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-Man-GlcNAc2]-Lys-Thr-OH + (1S)-1,5-anhydro-1-(2,4,6-trimethoxyphenyl)-D-glucitol
?
-
-
-
-
?
H-Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-Man-GlcNAc2]-Lys-Thr-OH + 1-deoxy-1-phenyl-alpha-D-gluco-2-heptulopyranose
?
-
-
-
-
?
H-Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-Man-GlcNAc2]-Lys-Thr-OH + 2-benzamido-2-deoxy-D-glucopyranose
?
-
-
-
-
?
H-Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-Man-GlcNAc2]-Lys-Thr-OH + 2-benzoylcarbonylamino-2-deoxy-D-glucopyranose
?
-
-
-
-
?
H-Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-Man-GlcNAc2]-Lys-Thr-OH + 2-deoxy-2-naphthoamido-D-glucopyranose
?
-
-
-
-
?
H-Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-Man-GlcNAc2]-Lys-Thr-OH + 2-deoxy-2-phenoxyacetamido-D-glucopyranose
?
-
-
-
-
?
H-Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-Man-GlcNAc2]-Lys-Thr-OH + 2-deoxy-2-phthalimido-D-glucopyranose
?
-
-
-
-
?
H-Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-Man-GlcNAc2]-Lys-Thr-OH + benzyl beta-D-glucopyranoside
?
-
-
-
-
?
haptoglobin + H2O
?
-
-
-
-
?
hen egg glycopeptide + 4-nitrophenyl-beta-D-glucose
?
-
-
transfer of asparagine-linked oligosaccharide
-
?
human alpha1-acid glycoprotein + 4-nitrophenyl-beta-D-glucose
?
-
-
transfer of bi-, tri- and tetraantennary complex type oligosaccharide, yield 1.7%
-
?
invertase + Lys-Val-Ala-Asn((NeuAc-Gal-GlcNAc-Man)2Man-GlcNAc2)-Lys-Thr
?
-
-
change of hyperglycosylated protein to a sialyl complex type glycoprotein
-
?
Lys-Val-Ala-Asn((NeuAc-Gal-GlcNAc-Man)2Man-GlcNAc2)-Lys-Thr + 4-methylumbelliferyl-beta-D-N-acetylglucosaminide
?
-
-
-
-
?
Man(GlcNAc)2Asn-dansyl + H2O
?
-
-
-
-
?
Man3GlcNAc-oxazoline + Fmoc-Asn(Fucalpha(1->6)GlcNAc)-OH
?
-
-
-
?
Man3GlcNAc-oxazoline + Fmoc-Asn(GlcNAc)-OH
?
-
-
-
?
Manalpha1-2Manalpha1-6(Manalpha1-2Manalpha1-3)Manalpha1-6(Manalpha1-2Manalpha1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-PA + H2O
Manalpha1-2Manalpha1-6(Manalpha1-2Manalpha1-3)Manalpha1-6(Manalpha1-2Manalpha1-2Manalpha1-3)Manbeta1-4GlcNAc + 2-(acetylamino)-2-deoxy-N-pyridin-2-yl-beta-D-glucopyranosylamine
-
-
-
-
?
Manalpha1-2Manalpha1-6(Manalpha1-3)Manalpha1-6(Manalpha1-2Manalpha1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-PA + H2O
Manalpha1-2Manalpha1-6(Manalpha1-3)Manalpha1-6(Manalpha1-2Manalpha1-2Manalpha1-3)Manbeta1-4GlcNAc + 2-(acetylamino)-2-deoxy-N-pyridin-2-yl-beta-D-glucopyranosylamine
-
-
-
-
?
Manalpha1-2Manalpha1-6(Manalpha1-3)Manalpha1-6(Manalpha1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-PA + H2O
?
-
-
-
-
?
Manalpha1-3Manalpha1-6(Manalpha1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-PA + H2O
?
-
-
-
-
?
Manalpha1-6(Manalpha1-3)Manalpha1-6(Manalpha1-2Manalpha1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-PA + H2O
Manalpha1-6(Manalpha1-3)Manalpha1-6(Manalpha1-2Manalpha1-2Manalpha1-3)Manbeta1-4GlcNAc + 2-(acetylamino)-2-deoxy-N-pyridin-2-yl-beta-D-glucopyranosylamine
-
-
-
-
?
Manalpha1-6(Manalpha1-3)Manalpha1-6(Manalpha1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-PA + H2O
?
-
-
-
-
?
Manalpha1-6(Manalpha1-3)Manalpha1-6(Manalpha1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-pyridylamino + H2O
?
-
-
-
-
?
Manalpha1-6(Manalpha1-3)Manalpha1-6(Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-PA + H2O
?
-
-
-
-
?
Manalpha1->6(Manalpha1->3)Manalpha1->6(Manalpha1->2Manalpha1->3)Manbeta1->4GlcNAcbeta1->4GlcNAcAsn + H2O
Manalpha1->6(Manalpha1->3)Manalpha1->6(Manalpha1->2Manalpha1->3)Manbeta1->4GlcNAcbeta1 + GlcNAcAsn
Manalpha1->6(Manalpha1->3)Manbeta1->4GlcNAcbeta1->4(Fucalpha1->6)GlcNAc->N-acetylAsn + H2O
Manalpha1->6(Manalpha1->3)Manbeta1->4GlcNAc + Fucalpha1-6GlcNAc-N-acetylAsn
N,N',N'',N'''-tetraacetylchitotetraose + H2O
2 N,N'-diacetylchitobiose
-
-
-
?
N,N',N''-triacetylchitotriose + H2O
N-acetyl-D-glucosamine + N,N'-diacetylchiotobiose
-
-
-
?
N-acetyl-beta-D-hexosaminides + H2O
N-acetyl-D-hexosamines
-
-
-
?
N-glycosylated bovine lactoferrin + H2O
?
N-glycosylated bovine serum albumin + H2O
?
N-glycosylated human lactoferrin + H2O
?
N-glycosylated human serum + H2O
Man5GlcNAc + ?
-
-
main product
-
?
N-glycosylated human transferrin + H2O
?
N-glycosylated immunglobuline G + H2O
?
N-glycosylated immunoglobulin A + H2O
?
N-glycosylated immunoglobulin G + H2O
?
N-glycosylated lactoferrin + H2O
?
N-glycosylated orosomucoid + H2O
?
the enzyme cleaves only biantennary and sialylated structures of orosomucoid
-
-
?
N-glycosylated ovalbumin + H2O
?
-
-
-
-
?
N-glycosylated RNase B + H2O
?
N-glycosylated RNase B + H2O
Man5GlcNAc + ?
-
-
main product
-
?
N-glycosylated silkworm hemolymph glycoproteins + H2O
?
-
-
-
-
?
N-glycosylated storage protein 2 + H2O
?
-
-
-
-
?
N-glycosylated transferrin + H2O
?
-
-
-
?
N-glycosylated yeast invertase + H2O
?
-
-
-
-
?
N4-(2-acetamido-3-O-benzyl-2-deoxy-beta-D-glucopyranosyl)-N2-(9-fluorenylmethoxycarbonyl)asparagine + H2O
?
N4-(2-acetamido-4-O-benzyl-2-deoxy-beta-D-glucopyranosyl)-N2-(9-fluorenylmethoxycarbonyl)-L-asparagine + H2O
?
N4-(2-acetamido-6-O-benzyl-2-deoxy-beta-D-glucopyranosyl)-N2-(9-fluorenylmethoxycarbonyl)-L-asparagine + H2O
?
N4-(alpha-L-fucopyranosyl-(1 ->3)-2-acetamido-2-deoxy-beta-D-glucopyranosyl)-N2-(9-fluorenylmethoxycarbonyl)-L-asparagine + H2O
?
N4-(beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-N2-dansyl-L-Asn + H2O
beta-D-Man-(1->4)-beta-D-GlcNAc + N4-(beta-D-GlcNAc)-N2-dansyl-L-Asn
-
-
-
-
?
Nalpha-9-fluorenylmethoxycarbonyl-Nbeta-3-hydroxymetyl-4-hydroxy-cyclohexyl-L-asparagine + sialylglycopeptide
?
-
transglycosylation
-
-
?
Neu2Gal2GlcNAc2-Man3GlcNAc2-Asn + H2O
?
O-(alpha-D-mannopyranosyl)-(1,6)-[(alpha-D-mannopyranosyl)-(1,3)]-beta-D-mannopyranosyl-(1,4)-(1,2-dideoxy-alpha-D-glucopyrano)-[2,1-d]-2-oxazoline + benzyl alpha-D-mannopyranoside
2,3,4,6-tetra-O-acetyl-1-O-(2,2,2-trichloroethanimidoyl)-alpha-D-mannopyranose + ?
-
-
-
-
?
O-(beta-D-mannopyranosyl)-(1,4)-(1,2-dideoxy-alpha-D-glucopyrano)-[2,1-d]-2-oxazoline + 2-O-acetyl-3,4,6-tri-O-benzyl-alpha-D-mannopyranosyl trichloroacetimidate
ethyl 2-O-acetyl-3,4,6-tri-O-benzyl-alpha-D-mannopyranosyl-(1-3)-4,6-O-benzylidene-2-O-levulinoyl-1-thio-beta-D-glucopyranoside + ?
-
-
yield of 98%
-
?
O-(beta-D-mannopyranosyl)-(1,4)-(1,2-dideoxy-alpha-D-glucopyrano)-[2,1-d]-2-oxazoline + benzyl alpha-D-mannopyranoside
benzyl 2,4-di-O-benzoyl-alpha-D-mannopyranoside + ?
-
-
-
-
?
ovalbumin + H2O
oligosaccharides + ?
p-nitrophenyl-beta-2-acetamido-2-deoxy-D-glucopyranoside + H2O
2-acetamido-2-deoxy-D-glucose + p-nitrophenol
-
-
-
?
phosphorylated oligosaccharide + H2O
?
presence of an alpha1,2-linked mannose residue facilitates the hydrolysis of phosphorylated oligosaccharides. The enzyme efficiently hydrolyzes phosphorylated oligosaccharides that are larger than Man4GlcNAc2-P, generating GlcNAc-1-P and neutral Gn1-type free oligosaccharides. It preferentially hydrolyzes phosphorylated oligosaccharides carrying the Manalpha1,2Manalpha1,3(Manalpha1,6)Manbeta1,4GlcNAcbeta1,4GlcNAc structure
-
-
?
Ricinus lectin + H2O
?
-
-
-
-
?
RNase B + Lys-Val-Ala-Asn((NeuAc-Gal-GlcNAc-Man)2Man-GlcNAc2)-Lys-Thr
?
-
-
change of high-mannose type oligosaccharide of Rnase B to a sialyl complex type
-
?
transferrin + 4-nitrophenyl-alpha-D-galactoside
?
-
-
transfer of asialobiantennary complex type oligosaccharide of human native transferrin
-
?
transferrin + 4-nitrophenyl-alpha-D-glucoside
?
-
-
transfer of asialobiantennary complex type oligosaccharide of human native transferrin
-
?
transferrin + 4-nitrophenyl-beta-D-galactoside
?
-
-
transfer of asialobiantennary complex type oligosaccharide of human native transferrin
-
?
transferrin + 4-nitrophenyl-beta-D-glucoside
?
-
-
transfer of asialobiantennary complex type oligosaccharide of human native transferrin with yield of 1.1%
-
?
transferrin + 4-nitrophenyl-beta-D-mannoside
?
-
-
transfer of asialobiantennary complex type oligosaccharide of human native transferrin
-
?
transferrin + 4-nitrophenyl-beta-D-xyloside
?
-
-
transfer of asialobiantennary complex type oligosaccharide of human native transferrin
-
?
transferrin + 4-nitrophenyl-glycerol
?
-
-
transfer of asialobiantennary complex type oligosaccharide of human native transferrin
-
?
transferrin + 4-nitrophenyl-N-acetyl-beta-D-glucosaminide
?
-
-
transfer of asialobiantennary complex type oligosaccharide of human native transferrin
-
?
transferrin + H2O
complex oligosaccharides + ?
-
-
-
?
yeast carboxypeptidase + H2O
?
-
-
-
-
?
yeast invertase + H2O
?
-
-
-
-
?
additional information
?
-
(dansyl)-labeled Man5GlcNAc2-Asn + H2O
?
hydrolytic activity of endo-beta-N-acetylglucosaminidase Endo-CC1 is higher than that of Endo-CC2
-
-
?
(dansyl)-labeled Man5GlcNAc2-Asn + H2O
?
hydrolytic activity of endo-beta-N-acetylglucosaminidase Endo-CC1 on (dansyl)-labeled Man5GlcNAc2-Asn is higher than that of Endo-CC2
-
-
?
(dansyl)-labeled Man5GlcNAc2-Asn + H2O
?
hydrolytic activity of endo-beta-N-acetylglucosaminidase Endo-CC1 is higher than that of Endo-CC2
-
-
?
(dansyl)-labeled Man5GlcNAc2-Asn + H2O
?
hydrolytic activity of endo-beta-N-acetylglucosaminidase Endo-CC1 on (dansyl)-labeled Man5GlcNAc2-Asn is higher than that of Endo-CC2
-
-
?
(Man)3(Xyl)1(GlcNAc)2-pyridylamino + H2O
?
-
-
-
-
?
(Man)3(Xyl)1(GlcNAc)2-pyridylamino + H2O
?
-
-
-
-
?
(Man)5(GlcNAc)2-N-acetyl-Asn + H2O
(Man)5GlcNAc + GlcNAc-N-acetyl-Asn
-
-
-
?
(Man)5(GlcNAc)2-N-acetyl-Asn + H2O
(Man)5GlcNAc + GlcNAc-N-acetyl-Asn
-
-
-
-
?
(Man)5(GlcNAc)2-N-acetyl-Asn + H2O
(Man)5GlcNAc + GlcNAc-N-acetyl-Asn
-
-
-
?
(Man)5(GlcNAc)2-pyridylamino + H2O
(Man)5(GlcNAc) + 2-(acetylamino)-2-deoxy-N-pyridin-2-yl-beta-D-glucopyranosylamine
-
-
-
-
?
(Man)5(GlcNAc)2-pyridylamino + H2O
(Man)5(GlcNAc) + 2-(acetylamino)-2-deoxy-N-pyridin-2-yl-beta-D-glucopyranosylamine
-
-
-
-
?
(Man)5(GlcNAc)2-pyridylamino + H2O
(Man)5(GlcNAc) + 2-(acetylamino)-2-deoxy-N-pyridin-2-yl-beta-D-glucopyranosylamine
-
-
-
-
?
(Man)5(GlcNAc)2-pyridylamino + H2O
(Man)5(GlcNAc) + 2-(acetylamino)-2-deoxy-N-pyridin-2-yl-beta-D-glucopyranosylamine
-
-
-
-
?
(Man)5(GlcNAc)2Asn + H2O
(Man)5GlcNAc + GlcNAc-Asn
-
di-N-acetylchitobiosyl linkage is hydrolyzed faster than the linkage in the glycopeptides (Man)5(GlcNAc)3Asn and (Man)6(GlcNAc)2Asn by enzyme form F-I
-
-
?
(Man)5(GlcNAc)2Asn + H2O
(Man)5GlcNAc + GlcNAc-Asn
-
-
-
-
?
(Man)5(GlcNAc)2Asn + H2O
(Man)5GlcNAc + GlcNAc-Asn
-
-
-
-
?
(Man)6(GlcNAc)2-pyridylamino + H2O
?
-
-
-
-
?
(Man)6(GlcNAc)2-pyridylamino + H2O
?
-
-
-
-
?
(Man)6(GlcNAc)2-pyridylamino + H2O
?
-
-
-
-
?
(Man)6(GlcNAc)2Asn + H2O
(Man)6GlcNAc + GlcNAc-Asn
-
-
-
-
?
(Man)6(GlcNAc)2Asn + H2O
(Man)6GlcNAc + GlcNAc-Asn
-
-
-
?
(Man)6(GlcNAc)2Asn + H2O
(Man)6GlcNAc + GlcNAc-Asn
-
di-N-acetylchitobiosyl linkage is hydrolyzed faster than the linkage in the glycopeptides (Man)5(GlcNAc)3Asn and (Man)6(GlcNAc)2Asn by enzyme form F-I
-
-
?
(Man)6(GlcNAc)2Asn + H2O
(Man)6GlcNAc + GlcNAc-Asn
-
-
-
-
?
(Man)7(GlcNAc)2-pyridylamino + H2O
?
-
-
-
-
?
(Man)7(GlcNAc)2-pyridylamino + H2O
?
-
-
-
-
?
(Man)7(GlcNAc)2-pyridylamino + H2O
?
-
-
-
-
?
(Man)8(GlcNAc)2-pyridylamino + H2O
?
-
-
-
-
?
(Man)8(GlcNAc)2-pyridylamino + H2O
?
-
-
-
-
?
(Man)8(GlcNAc)2-pyridylamino + H2O
?
-
-
-
-
?
(Man)9(GlcNAc)2-pyridylamino + H2O
?
-
-
-
-
?
(Man)9(GlcNAc)2-pyridylamino + H2O
?
-
-
-
-
?
(Man)9(GlcNAc)2-pyridylamino + H2O
?
-
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl-beta-D-mannopyranoside + H2O
4-methylumbelliferone + beta-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl-beta-D-mannopyranoside + H2O
4-methylumbelliferone + beta-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl-beta-D-mannopyranoside + H2O
4-methylumbelliferone + beta-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl-beta-D-mannopyranoside + H2O
4-methylumbelliferone + beta-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl-beta-D-mannopyranoside + H2O
4-methylumbelliferone + beta-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl-beta-D-mannopyranoside + H2O
4-methylumbelliferone + beta-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl-beta-D-mannopyranoside + H2O
4-methylumbelliferone + beta-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl-beta-D-mannopyranoside + H2O
4-methylumbelliferone + beta-D-mannopyranose
-
-
-
-
?
acetyl-Asn(GlcNAc)2(Man)6 + H2O
acetyl-AsnGlcNAc
-
-
-
?
acetyl-Asn(GlcNAc)2(Man)6 + H2O
acetyl-AsnGlcNAc
-
-
-
-
?
acetyl-Asn(GlcNAc)2(Man)6 + H2O
acetyl-AsnGlcNAc
-
-
-
?
alpha-NeuAc-(2->6)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)[alpha-NeuAc-(2->6)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)]beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-Asn + H2O
?
hydrolytic activity of endo-beta-N-acetylglucosaminidase Endo-CC1 is higher than that of Endo-CC2
-
-
?
alpha-NeuAc-(2->6)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)[alpha-NeuAc-(2->6)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)]beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-Asn + H2O
?
hydrolytic activity of endo-beta-N-acetylglucosaminidase Endo-CC1 is higher than that of Endo-CC2
-
-
?
Asn(GlcNAc)2(Man)3 + H2O
?
-
-
-
-
?
Asn(GlcNAc)2(Man)3 + H2O
?
-
-
-
-
?
Asn(GlcNAc)2-(Man)5 + H2O
AsnGlcNAc + Man5(GlcNAc)
-
-
-
-
?
Asn(GlcNAc)2-(Man)5 + H2O
AsnGlcNAc + Man5(GlcNAc)
-
-
-
-
?
Asn(GlcNAc)2-(Man)5 + H2O
AsnGlcNAc + Man5(GlcNAc)
-
-
-
?
Asn(GlcNAc)2-(Man)5 + H2O
AsnGlcNAc + Man5(GlcNAc)
-
-
-
-
?
Asn(GlcNAc)2-(Man)5 + H2O
AsnGlcNAc + Man5(GlcNAc)
-
-
-
?
Asn(GlcNAc)2-(Man)6 + H2O
AsnGlcNAc + (GlcNAc)1-(Man)6
-
-
-
-
?
Asn(GlcNAc)2-(Man)6 + H2O
AsnGlcNAc + (GlcNAc)1-(Man)6
-
-
-
-
?
Asn(GlcNAc)2-(Man)6 + H2O
AsnGlcNAc + (GlcNAc)1-(Man)6
-
-
-
?
Asn(GlcNAc)2-(Man)6 + H2O
AsnGlcNAc + (GlcNAc)1-(Man)6
-
-
-
?
Asn(GlcNAc)2-(Man)6(GlcNAc)2 + H2O
AsnGlcNAc + (GlcNAC)1-(Man)6(GlcNAc)2
-
-
-
?
Asn(GlcNAc)2-(Man)6(GlcNAc)2 + H2O
AsnGlcNAc + (GlcNAC)1-(Man)6(GlcNAc)2
-
-
-
?
Asn-(GlcNAc)2(Man)6 + gentiobiose
?
Halalkalibacterium halodurans
-
enzyme shows transglycosylation activity in the presence of glucose and gentiobiose, but with galactose
-
-
?
Asn-(GlcNAc)2(Man)6 + gentiobiose
?
Halalkalibacterium halodurans C-125
-
enzyme shows transglycosylation activity in the presence of glucose and gentiobiose, but with galactose
-
-
?
Asn-(GlcNAc)2(Man)6 + glucose
?
Halalkalibacterium halodurans
-
enzyme shows transglycosylation activity in the presence of glucose and gentiobiose, but with galactose
-
-
?
Asn-(GlcNAc)2(Man)6 + glucose
?
Halalkalibacterium halodurans C-125
-
enzyme shows transglycosylation activity in the presence of glucose and gentiobiose, but with galactose
-
-
?
beta-D-GlcNAc-(1-2)-alpha-D-Man-(1-3)-[alpha-D-Man-(1-3)-[alpha-D-Man-(1-6)]-alpha-D-Man-(1,6)]-beta-D-Man-(1-4)-beta-D-GlcNAc-(1-4)-beta-D-GlcNAc-pyridylamino
?
-
-
-
-
?
beta-D-GlcNAc-(1-2)-alpha-D-Man-(1-3)-[alpha-D-Man-(1-3)-[alpha-D-Man-(1-6)]-alpha-D-Man-(1,6)]-beta-D-Man-(1-4)-beta-D-GlcNAc-(1-4)-beta-D-GlcNAc-pyridylamino
?
-
-
-
-
?
bovine colostrum whey glycoproteins + H2O
?
-
-
-
?
bovine colostrum whey glycoproteins + H2O
?
-
-
-
?
bovine lactoferrin + H2O
?
-
-
-
?
bovine lactoferrin + H2O
?
-
-
-
?
dansyl asialotransferrin glycopeptide + H2O
?
-
-
-
-
?
dansyl asialotransferrin glycopeptide + H2O
?
-
-
-
-
?
dansyl-Asn-(GlcNAc)2(Man)6 + H2O
dansyl-Asn-GlcNAc + (Man)6GlcNAc
-
-
-
?
dansyl-Asn-(GlcNAc)2(Man)6 + H2O
dansyl-Asn-GlcNAc + (Man)6GlcNAc
-
-
-
-
?
dansyl-Asn-(GlcNAc)2(Man)6 + H2O
dansyl-Asn-GlcNAc + (Man)6GlcNAc
-
-
-
?
dansyl-Asn-(GlcNAc)2(Man)6 + H2O
dansyl-Asn-GlcNAc + (Man)6GlcNAc
-
-
-
-
?
dansyl-Asn-(GlcNAc)2(Man)6 + H2O
dansyl-Asn-GlcNAc + (Man)6GlcNAc
-
-
-
-
?
dansyl-Asn-(GlcNAc)4(Man)6 + H2O
dansyl-Asn-GlcNAc + ?
-
-
-
-
?
dansyl-Asn-(GlcNAc)4(Man)6 + H2O
dansyl-Asn-GlcNAc + ?
-
-
-
?
GlcNAcAsn + H2O
N-acetyl-D-glucosamine + L-asparagine
-
-
-
-
?
GlcNAcAsn + H2O
N-acetyl-D-glucosamine + L-asparagine
-
-
-
-
?
glycopeptide + H2O
?
-
high activity on dansyl transferrin glycopeptide, can also hydrolyze dansyl asialotransferrin glycopeptide and dansyl transferrin glycopeptide containing complex type sugar chains
-
-
?
glycopeptide + H2O
?
-
enzyme endo-BI hydrolyzes the pyridylamino-trimannosyl core and pyridylamino-agalacto biantennary complex-type oligosaccharides, enzyme form endo-BII acts specifically on the high-mannose-type oligosaccharides (Man)5-9(GlcNAc)2 present in ovomucoid in small amounts
-
-
?
glycopeptide + H2O
?
-
specificity
-
-
?
glycopeptide + H2O
?
-
two endo-beta-N-acetylglucosaminidase CI and CII with different substrate specificity
-
-
?
glycopeptide + H2O
?
-
specificity
-
-
?
glycopeptide + H2O
?
-
hydrolysis of the following oligosaccharide structures: ovalbumin-high mannose, ovalbumin-hybrid containing GlcNAc beta1,4-Man, ovalbumin-hybrid without GlcNAc beta1,4-Man, ovomucoid hybrids, biantennary complex, triantennary complex and tetraantennary complex oligosaccharide structure
-
-
?
glycopeptide + H2O
?
-
glycopeptide from immunoglobulin M, (aa)x-Asn(GlcNAC)2(Man)3(Fuc)1
-
-
?
glycopeptide + H2O
?
-
asparagine oligosaccharides of transferrin and fetuin
-
-
?
glycopeptide + H2O
?
-
endo-beta-N-acetylglucosaminidase 1: high mannose-type asparaginylglycopeptide is hydrolyzed efficiently, little activity towards complex-type glycopeptides. endo-beta-N-acetylglucosaminidase 2: hydrolyzes both the high mannose-type and the complex-type oligosaccharide with chitobiosyl group at the reducing end and without the Asn
-
-
?
glycopeptide + H2O
?
-
glycoasparagines derived from ovalbumin and asialoglycoasparagines derived from human serotransferrin
-
-
?
glycopeptide + H2O
?
-
high activity on dansyl ovalbumin glycopeptide, can also act on dansyl asialotransferrin glycopeptide containing biantennary type sugar chains
-
-
?
glycopeptide + H2O
?
-
high activity on oligomannoside-type glycoasparagines and glycoproteins, can also hydrolyze hybrid-type and complex-type glycoasparagines
-
-
?
glycopeptide + H2O
?
-
high activity on oligomannoside-type glycoasparagines and glycoproteins, can also hydrolyze hybrid-type and complex-type glycoasparagines
-
-
?
glycopeptide + H2O
?
-
-
-
-
?
glycopeptide + H2O
?
-
specificity
-
-
?
glycopeptide + H2O
?
-
hydrolysis of Asn(GlcNAc)2(Man)5 and larger neutral oligosaccharides, no hydrolysis of exoglycosidase-treated acidic IgM glycopeptides
-
-
?
glycopeptide + H2O
?
-
generally hydrolyzes side-chain-free glycopeptides of the complex heteropolysaccharide unit
-
-
?
glycopeptide + H2O
?
-
specificity
-
-
?
glycopeptide + H2O
?
-
release of Asn-GlcNAc-Fuc-containing glycopeptides from exoglycosidase-treated acidic IgM glycopeptides, limited capacity to hydrolyze ovalbumin glycopeptides larger than Asn(GlcNAc)2(Man)5
-
-
?
glycopeptide + H2O
?
-
generally hydrolyzes glycopeptides of the mannose-N-acetylglucosamine unit
-
-
?
glycoprotein + H2O
?
-
endo-BI hydrolyzes oligosaccharides of both hen ovalbumin and ovomucoid. Endo-BII can act only on oligosaccharides of hen ovalbumin and shows almost no activity towards hen ovomucoid
-
-
?
glycoprotein + H2O
?
-
high-mannose and complex glycoproteins linked through asparagine to the protein backbone, cleavage occurs via hydrolysis of the glycosidic bond of the N,N'-diacetylchiotobiose core structure adjacent to asparagine. Glycoproteins of retrovirus, lymphocytic choriomeningitis virus, Pichinde virus, and HLA-A and HLA-B antigens are cleaved in presence of nonionic detergent. Ovalbumin, fetuin, bromelain, ovomucoid, alpha1-acid glycoprotein, immunoglobulin G and influenza virus hemagglutinin are susceptible only after reduction and alkylation or in presence of 1% 2-mercaptoethanol
-
-
?
glycoprotein + H2O
?
-
cleaves the N,N'-diacetylchitobiose moiety of the sugar chain of human salivary alpha-amylase family, human transferrin and calf fetuin
-
-
?
glycoprotein + H2O
?
-
hydrolysis of asparagine-linked oligosaccharides of glycoproteins at the di-N-acetylchitobiosyl moiety of complex oligosaccharides, high-mannose oligosaccharides and hybrid structure oligosachharides
-
-
?
glycoprotein + H2O
?
-
-
-
-
?
glycoprotein + H2O
?
-
specificity
-
-
?
glycoprotein + H2O
?
-
specificity
-
-
?
glycoprotein + H2O
?
-
release of intact neutral oligosaccharides that is attached to the protein by a glycosyl asparagine bond from sulfitolyzed ovalbumin, bovine pancreatic deoxyribonuclease A, ribonuclease B, and invertase from Saccharomyces cerevisiae. Release from neutral chain only from proteins that contain both neutral and acidic oligosaccharides such as thyroglobulin, immunoglobulin M, and porcine ribonuclease
-
-
?
Manalpha1->6(Manalpha1->3)Manalpha1->6(Manalpha1->2Manalpha1->3)Manbeta1->4GlcNAcbeta1->4GlcNAcAsn + H2O
Manalpha1->6(Manalpha1->3)Manalpha1->6(Manalpha1->2Manalpha1->3)Manbeta1->4GlcNAcbeta1 + GlcNAcAsn
-
endo-beta-N-acetylglucosaminidase CII
-
?
Manalpha1->6(Manalpha1->3)Manalpha1->6(Manalpha1->2Manalpha1->3)Manbeta1->4GlcNAcbeta1->4GlcNAcAsn + H2O
Manalpha1->6(Manalpha1->3)Manalpha1->6(Manalpha1->2Manalpha1->3)Manbeta1->4GlcNAcbeta1 + GlcNAcAsn
-
endo-beta-N-acetylglucosaminidase CII
-
-
?
Manalpha1->6(Manalpha1->3)Manbeta1->4GlcNAcbeta1->4(Fucalpha1->6)GlcNAc->N-acetylAsn + H2O
Manalpha1->6(Manalpha1->3)Manbeta1->4GlcNAc + Fucalpha1-6GlcNAc-N-acetylAsn
-
endo-beta-N-acetylglucosaminidase CI
-
?
Manalpha1->6(Manalpha1->3)Manbeta1->4GlcNAcbeta1->4(Fucalpha1->6)GlcNAc->N-acetylAsn + H2O
Manalpha1->6(Manalpha1->3)Manbeta1->4GlcNAc + Fucalpha1-6GlcNAc-N-acetylAsn
-
endo-beta-N-acetylglucosaminidase CI
-
-
?
N-glycosylated bovine lactoferrin + H2O
?
-
-
-
-
?
N-glycosylated bovine lactoferrin + H2O
?
-
highest activity
-
-
?
N-glycosylated bovine lactoferrin + H2O
?
-
-
-
-
?
N-glycosylated bovine lactoferrin + H2O
?
-
highest activity
-
-
?
N-glycosylated bovine lactoferrin + H2O
?
-
-
-
-
?
N-glycosylated bovine lactoferrin + H2O
?
-
highest activity
-
-
?
N-glycosylated bovine lactoferrin + H2O
?
-
-
-
-
?
N-glycosylated bovine serum albumin + H2O
?
-
-
-
-
?
N-glycosylated bovine serum albumin + H2O
?
-
lowest activity
-
-
?
N-glycosylated bovine serum albumin + H2O
?
-
-
-
-
?
N-glycosylated bovine serum albumin + H2O
?
-
-
-
-
?
N-glycosylated bovine serum albumin + H2O
?
-
-
-
-
?
N-glycosylated human lactoferrin + H2O
?
-
-
-
-
?
N-glycosylated human lactoferrin + H2O
?
-
-
-
-
?
N-glycosylated human transferrin + H2O
?
endo-beta-N-acetylglucosaminidase Endo-CC1 acts on both N-linked high-mannose type and sialobiantennary type complex oligosaccharides of the glycoprotein human transferrin
-
-
?
N-glycosylated human transferrin + H2O
?
endo-beta-N-acetylglucosaminidase Endo-CC1 acts on both N-linked high-mannose type and sialobiantennary type complex oligosaccharides of the glycoprotein human transferrin
-
-
?
N-glycosylated immunglobuline G + H2O
?
the enzyme prefers core-fucosylated N-glycan for hydrolysis
-
-
?
N-glycosylated immunglobuline G + H2O
?
the enzyme hydrolyses the N-linked glycan on the heavy chain of immunglobuline G
-
-
?
N-glycosylated immunoglobulin A + H2O
?
-
-
-
-
?
N-glycosylated immunoglobulin A + H2O
?
-
-
-
-
?
N-glycosylated immunoglobulin G + H2O
?
-
-
-
-
?
N-glycosylated immunoglobulin G + H2O
?
-
-
-
-
?
N-glycosylated immunoglobulin G + H2O
?
-
-
-
-
?
N-glycosylated immunoglobulin G + H2O
?
-
-
-
-
?
N-glycosylated immunoglobulin G + H2O
?
-
-
-
-
?
N-glycosylated immunoglobulin G + H2O
?
-
-
-
-
?
N-glycosylated lactoferrin + H2O
?
-
-
-
-
?
N-glycosylated lactoferrin + H2O
?
-
-
-
-
?
N-glycosylated RNase B + H2O
?
-
-
-
-
?
N-glycosylated RNase B + H2O
?
-
second highest activity
-
-
?
N-glycosylated RNase B + H2O
?
-
-
-
-
?
N-glycosylated RNase B + H2O
?
endo-beta-N-acetylglucosaminidase Endo-CC1 acts on both N-linked high-mannose type and sialobiantennary type complex oligosaccharides of the glycoprotein RNase B
-
-
?
N-glycosylated RNase B + H2O
?
endo-beta-N-acetylglucosaminidase Endo-CC1 acts on both N-linked high-mannose type and sialobiantennary type complex oligosaccharides of the glycoprotein RNase B
-
-
?
N-glycosylated RNase B + H2O
?
-
-
-
?
N-glycosylated RNase B + H2O
?
-
the enzyme cleaves within the chitobiose core of high-mannose oligosaccharides from RNase B
-
-
?
N-glycosylated RNase B + H2O
?
-
-
the series Man5GlcNAc-Man9GlcNAc is released by the enzyme, but not Man5GlcNAc2-Man9GlcNAc2 thus corroborating endo activity
-
?
N4-(2-acetamido-3-O-benzyl-2-deoxy-beta-D-glucopyranosyl)-N2-(9-fluorenylmethoxycarbonyl)asparagine + H2O
?
-
-
-
-
?
N4-(2-acetamido-3-O-benzyl-2-deoxy-beta-D-glucopyranosyl)-N2-(9-fluorenylmethoxycarbonyl)asparagine + H2O
?
-
-
-
-
?
N4-(2-acetamido-4-O-benzyl-2-deoxy-beta-D-glucopyranosyl)-N2-(9-fluorenylmethoxycarbonyl)-L-asparagine + H2O
?
-
-
-
-
?
N4-(2-acetamido-4-O-benzyl-2-deoxy-beta-D-glucopyranosyl)-N2-(9-fluorenylmethoxycarbonyl)-L-asparagine + H2O
?
-
-
-
-
?
N4-(2-acetamido-6-O-benzyl-2-deoxy-beta-D-glucopyranosyl)-N2-(9-fluorenylmethoxycarbonyl)-L-asparagine + H2O
?
-
-
-
-
?
N4-(2-acetamido-6-O-benzyl-2-deoxy-beta-D-glucopyranosyl)-N2-(9-fluorenylmethoxycarbonyl)-L-asparagine + H2O
?
-
-
-
-
?
N4-(alpha-L-fucopyranosyl-(1 ->3)-2-acetamido-2-deoxy-beta-D-glucopyranosyl)-N2-(9-fluorenylmethoxycarbonyl)-L-asparagine + H2O
?
-
-
-
-
?
N4-(alpha-L-fucopyranosyl-(1 ->3)-2-acetamido-2-deoxy-beta-D-glucopyranosyl)-N2-(9-fluorenylmethoxycarbonyl)-L-asparagine + H2O
?
-
-
-
-
?
Neu2Gal2GlcNAc2-Man3GlcNAc2-Asn + H2O
?
hydrolytic activity of endo-beta-N-acetylglucosaminidase Endo-CC1 on Neu2Gal2GlcNAc2-Man3GlcNAc2-Asn is higher than that of Endo-CC2
-
-
?
Neu2Gal2GlcNAc2-Man3GlcNAc2-Asn + H2O
?
hydrolytic activity of endo-beta-N-acetylglucosaminidase Endo-CC1 on Neu2Gal2GlcNAc2-Man3GlcNAc2-Asn is higher than that of Endo-CC2
-
-
?
ovalbumin + H2O
oligosaccharides + ?
-
the enzyme hydrolyzes all five heterogenous ovalbumin glycopeptides, the rate of hydrolysis decreases as the size of the sugar moiety increases
-
?
ovalbumin + H2O
oligosaccharides + ?
-
native ovalbumin
-
-
?
ovalbumin + H2O
oligosaccharides + ?
-
native ovalbumin
-
?
ovalbumin + H2O
oligosaccharides + ?
-
native ovalbumin
-
-
?
ovalbumin + H2O
oligosaccharides + ?
-
-
-
?
peptidoglycan + H2O
?
-
Micrococcus luteus cell wall and Bacillus subtilis cell walls
-
-
?
peptidoglycan + H2O
?
-
Micrococcus luteus cell wall and Bacillus subtilis cell walls
-
-
?
peptidoglycan + H2O
?
-
no hydrolyis of Micrococcus lysodeikticus cell walls
-
-
?
peptidoglycan + H2O
?
-
no attack of intact cell walls of Staphylococcus simulans 22, hydrolysis of cell walls of Micrococcus luteus and soluble peptidoglycan chains of Staphylococcus simulans 22
-
-
?
peptidoglycan + H2O
?
-
no attack of intact cell walls of Staphylococcus simulans 22, hydrolysis of cell walls of Micrococcus luteus and soluble peptidoglycan chains of Staphylococcus simulans 22
-
-
?
ribonuclease B + H2O
?
-
-
-
-
?
ribonuclease B + H2O
?
-
-
-
?
ribonuclease B + H2O
?
-
-
-
?
ribonuclease B + H2O
?
-
-
-
-
?
ribonuclease B + H2O
?
-
bovine pancreatic ribonuclease B
-
-
?
ribonuclease B + H2O
?
the enzyme catalyzes cleavage between the GlcNAc residues of the chitobiose core of N-linked glycans, leaving one GlcNAc residues attached to asparagine. Endo H cleaves high mannose and hybrid, but not complex, N-linked oligosaccharides on glycoproteins
-
-
?
rituximab + H2O
?
releases the fucose-containing oligosaccharides residues from rituximab (immunoglobulin G) but not the high-mannose-containing oligosaccharides residues from RNase B
-
-
?
rituximab + H2O
?
releases the fucose-containing oligosaccharides residues from rituximab (immunoglobulin G) but not the high-mannose-containing oligosaccharides residues from RNase B
-
-
?
rituximab + H2O
?
releases the fucose-containing oligosaccharides residues from rituximab (immunoglobulin G) but not the high-mannose-containing oligosaccharides residues from RNase B
-
-
?
rituximab + H2O
?
releases the fucose-containing oligosaccharides residues from rituximab (immunoglobulin G) but not the high-mannose-containing oligosaccharides residues from RNase B
-
-
?
rituximab + H2O
?
releases the fucose-containing oligosaccharides residues from rituximab (immunoglobulin G) but not the high-mannose-containing oligosaccharides residues from RNase B
-
-
?
RNase B + H2O
?
-
cleaves high mannose-type glycans in glycoproteins between the N-acetylglucosamine residues of the pentasaccharide core
-
-
?
RNase B + H2O
?
-
cleaves high mannose-type glycans in glycoproteins between the N-acetylglucosamine residues of the pentasaccharide core
-
-
?
RNase B + H2O
?
-
cleaves high mannose-type glycans in glycoproteins between the N-acetylglucosamine residues of the pentasaccharide core
-
-
?
RNase B + H2O
?
-
cleaves high mannose-type glycans in glycoproteins between the N-acetylglucosamine residues of the pentasaccharide core
-
-
?
RNase B + H2O
?
-
cleaves high mannose-type glycans in glycoproteins between the N-acetylglucosamine residues of the pentasaccharide core
-
-
?
RNase B + H2O
?
-
model glycoprotein with a single N-glycosylation site occupied by a family of high-mannose-type glycans, is degraded of all high mannose-type glycoforms to a single N-linked N-acetylglucosamine residue
-
-
?
RNase B + H2O
?
-
cleaves high mannose-type glycans in glycoproteins between the N-acetylglucosamine residues of the pentasaccharide core
-
-
?
RNase B + H2O
?
-
cleaves high mannose-type glycans in glycoproteins between the N-acetylglucosamine residues of the pentasaccharide core
-
-
?
RNase B + H2O
?
-
cleaves high mannose-type glycans in glycoproteins between the N-acetylglucosamine residues of the pentasaccharide core
-
-
?
RNase B + H2O
?
-
cleaves high mannose-type glycans in glycoproteins between the N-acetylglucosamine residues of the pentasaccharide core
-
-
?
additional information
?
-
-
the enzyme is probably devoted to exogeneous functions, such as degrading macromolecules for feeding purposes
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the glycosidic linkage in the N-acetylchitobiosyl unit to form the GN1 type free N-glycans with only one GlcNAc residue at the reducing end. The enzyme shows strong activity against high-mannose type N-glycans having Manalpha(1->2)Manalpha(1->3)Manbeta1-unit, but no activity against plant complex and truncated structures having GlcNAcbeta(1->4)(Fucalpha(1->3))GlcNAc-unit at their reducing ends
-
-
?
additional information
?
-
-
high-mannose-type glycopeptides are rapidly hydrolyzed, hybrid-type glycopeptides are good substrates, complex-type glycopeptides as well as smaller glycopeptides prepared by partial glycosidase digestion of complex-type glycopeptides are resistant to the enzyme
-
-
?
additional information
?
-
-
no exo-activity
-
-
?
additional information
?
-
-
no exo-activity
-
-
?
additional information
?
-
the enzyme can hydrolytically remove fucose-containing oligosaccharides from glycoproteins. The enzyme specicically hydrolyzes fucose-containing biantennary oligosaccharides. It exhibits higher activity for the substrate containing terminal sialic acid with the alpha2,3-linkage. Terminal fucosylation is not accepted as a substrate
-
-
?
additional information
?
-
-
the enzyme can hydrolytically remove fucose-containing oligosaccharides from glycoproteins. The enzyme specicically hydrolyzes fucose-containing biantennary oligosaccharides. It exhibits higher activity for the substrate containing terminal sialic acid with the alpha2,3-linkage. Terminal fucosylation is not accepted as a substrate
-
-
?
additional information
?
-
the enzyme can hydrolytically remove fucose-containing oligosaccharides from glycoproteins. The enzyme specicically hydrolyzes fucose-containing biantennary oligosaccharides. It exhibits higher activity for the substrate containing terminal sialic acid with the alpha2,3-linkage. Terminal fucosylation is not accepted as a substrate
-
-
?
additional information
?
-
-
the enzyme is active toward all major types of N-linked glycans found in glycosylated proteins. Its activity is not affected by core fucosylation or extensive fucosylation, antenna number, or sialylation. Extensive N-deglycosylation of whole breast milk is also observed after coincubation with this enzyme
-
-
?
additional information
?
-
the enzyme that cleaves N-N'-diacetyl chitobiose moieties found in the N-glycan core of high mannose, hybrid, and complex N-glycans. These conjugated N-glycans as a prebiotic source stimulates the growth of a key infant gut microbe, Bifidobacterium longum subsp. infantis
-
-
?
additional information
?
-
-
the enzyme that cleaves N-N'-diacetyl chitobiose moieties found in the N-glycan core of high mannose, hybrid, and complex N-glycans. These conjugated N-glycans as a prebiotic source stimulates the growth of a key infant gut microbe, Bifidobacterium longum subsp. infantis
-
-
?
additional information
?
-
the enzyme cleaves the N-N'-diacetyl chitobiose moiety found in the N-glycan core of high mannose, hybrid and complex N-glycans. EndoBI-1 can facilitate large-scale release of complex, bioactive glycans from a variety of glycoprotein substrates
-
-
?
additional information
?
-
the enzyme that cleaves N-N'-diacetyl chitobiose moieties found in the N-glycan core of high mannose, hybrid, and complex N-glycans
-
-
?
additional information
?
-
-
the enzyme that cleaves N-N'-diacetyl chitobiose moieties found in the N-glycan core of high mannose, hybrid, and complex N-glycans
-
-
?
additional information
?
-
-
the enzyme is active toward all major types of N-linked glycans found in glycosylated proteins. Its activity is not affected by core fucosylation or extensive fucosylation, antenna number, or sialylation. Extensive N-deglycosylation of whole breast milk is also observed after coincubation with this enzyme
-
-
?
additional information
?
-
the enzyme that cleaves N-N'-diacetyl chitobiose moieties found in the N-glycan core of high mannose, hybrid, and complex N-glycans. These conjugated N-glycans as a prebiotic source stimulates the growth of a key infant gut microbe, Bifidobacterium longum subsp. infantis
-
-
?
additional information
?
-
the enzyme that cleaves N-N'-diacetyl chitobiose moieties found in the N-glycan core of high mannose, hybrid, and complex N-glycans
-
-
?
additional information
?
-
the enzyme cleaves the N-N'-diacetyl chitobiose moiety found in the N-glycan core of high mannose, hybrid and complex N-glycans. EndoBI-1 can facilitate large-scale release of complex, bioactive glycans from a variety of glycoprotein substrates
-
-
?
additional information
?
-
-
the enzyme is active toward all major types of N-linked glycans found in glycosylated proteins. Its activity is not affected by core fucosylation or extensive fucosylation, antenna number, or sialylation. Extensive N-deglycosylation of whole breast milk is also observed after coincubation with this enzyme
-
-
?
additional information
?
-
-
the enzyme is specific for high mannose glycans, no hydrolysis of either hybrid or complex glycans
-
-
?
additional information
?
-
-
two endo-beta-N-acetylglucosaminidase CI and CII with different substrate specificity
-
-
?
additional information
?
-
-
constitutive enzyme
-
-
?
additional information
?
-
-
the enzyme is probably devoted to exogeneous functions, such as degrading macromolecules for feeding purposes
-
-
?
additional information
?
-
endo-beta-N-acetylglucosaminidase Endo-CC1 does not act on the sialotriantennary type complex oligosaccharide of glycoprotein fetuin. Endo-CC1 can not transfer the sialobiantennary type complex oligosaccharide onto the deglycosylated RNase B
-
-
?
additional information
?
-
endo-beta-N-acetylglucosaminidase Endo-CC1 does not act on the sialotriantennary type complex oligosaccharide of glycoprotein fetuin. Endo-CC1 can not transfer the sialobiantennary type complex oligosaccharide onto the deglycosylated RNase B
-
-
?
additional information
?
-
-
endo-beta-N-acetylglucosaminidase Endo-CC1 does not act on the sialotriantennary type complex oligosaccharide of glycoprotein fetuin. Endo-CC1 can not transfer the sialobiantennary type complex oligosaccharide onto the deglycosylated RNase B
-
-
?
additional information
?
-
endo-beta-N-acetylglucosaminidase Endo-CC1 does not act on the sialotriantennary type complex oligosaccharide of glycoprotein fetuin. Endo-CC1 can not transfer the sialobiantennary type complex oligosaccharide onto the deglycosylated RNase B
-
-
?
additional information
?
-
endo-beta-N-acetylglucosaminidase Endo-CC1 does not act on the sialotriantennary type complex oligosaccharide of glycoprotein fetuin. Endo-CC1 can not transfer the sialobiantennary type complex oligosaccharide onto the deglycosylated RNase B
-
-
?
additional information
?
-
the enzyme can hydrolytically remove fucose-containing oligosaccharides from glycoproteins. The enzyme specicically hydrolyzes fucose-containing biantennary oligosaccharides. It exhibits higher activity for the substrate containing terminal sialic acid with the alpha2,3-linkage. Terminal fucosylation is not accepted
-
-
?
additional information
?
-
-
the enzyme can hydrolytically remove fucose-containing oligosaccharides from glycoproteins. The enzyme specicically hydrolyzes fucose-containing biantennary oligosaccharides. It exhibits higher activity for the substrate containing terminal sialic acid with the alpha2,3-linkage. Terminal fucosylation is not accepted
-
-
?
additional information
?
-
the enzyme can hydrolytically remove fucose-containing oligosaccharides from glycoproteins. The enzyme specicically hydrolyzes fucose-containing biantennary oligosaccharides. It exhibits higher activity for the substrate containing terminal sialic acid with the alpha2,3-linkage. Terminal fucosylation is not accepted
-
-
?
additional information
?
-
-
important role in the development of growing process of seedlings, involved in the production of high-mannose type glycans
-
-
?
additional information
?
-
-
enzyme is highly active towards the high-mannose-type glycans bearing the Manalpha1-2Manalpha1-3Manbeta1-structural unit
-
-
?
additional information
?
-
-
specificity
-
-
?
additional information
?
-
-
the enzyme is probably devoted to exogeneous functions, such as degrading macromolecules for feeding purposes
-
-
?
additional information
?
-
-
cleaves the beta(1-4) link between the core GlcNAc of asparagine-linked oligosaccharides, with specificity for biantennary and triantennary complex glycans
-
-
?
additional information
?
-
-
enzyme type F-I hydrolyzes the tri-mannosyl derivatives di-N-acetylglycosaminylasparagine faster than the penta-mannosyl compounds and the hexamannosyl compounds. Enzyme type F-II hydrolyzes the penta-mannosyl derivatives and hexa-mannosyl derivatives, but not the tri-mannosyl compounds
-
-
?
additional information
?
-
-
the enzyme is probably devoted to exogeneous functions, such as degrading macromolecules for feeding purposes
-
-
?
additional information
?
-
-
inducible by yeast extract
-
-
?
additional information
?
-
-
specificity
-
-
?
additional information
?
-
-
the enzyme hydrolyzes oligomannose-type sugar chains faster than complex-type chains and hybrid-type chains. Sugar chains containing the manalpha1-2Manalpha1-3Manbeta1-4GlcNAcbeta1-GlcNAc structure are good substrates
-
-
?
additional information
?
-
-
in cytosol the enzyme contributes to the production of free oligosaccharides with one reducing end N-acetylglucosamine residue in cooperation with neutral alpha-mannosidase
-
-
?
additional information
?
-
-
probably responsible for hydrolysis of both fucose-containing and fucose-depleted substrates
-
-
?
additional information
?
-
-
important role in the development of growing process of seedlings, involved in the production of high-mannose type glycans
-
-
?
additional information
?
-
-
the enzyme is probably devoted to exogeneous functions, such as degrading macromolecules for feeding purposes
-
-
?
additional information
?
-
-
enzyme has transglycosylation activity, high-mannose-type oligosaccharides are transferred to suitable glycosides as acceptor substrates, enzyme transfers high-mannose-type oligosaccharides more efficiently to beta-linked disaccharides than to alpha-linked disaccharides
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the beta-1,4-glycosidic bond in the core N,N'-diacetylchitobiose moiety of N-glycoproteins to release the N-glycan. The enzyme also possesses transglycosylation activity and is able to transfer the released N-glycan to a GlcNAc-peptide acceptor to form a new glycopeptide
-
-
?
additional information
?
-
-
minimum structure of the donor substrate required for transglycosylation is the Man-beta-1,4-N-acetyl-Glc oxazoline moiety. Replacement of beta-D-mannose with beta-D-glucose, beta-D-galactose, or beta-D-N-acetylglucose monosaccharides results in loss of substrate activity for the disaccharide oxazoline
-
-
?
additional information
?
-
conserved essential catalytic residues E173, N171 and Y205 are within hydrogen bonding distance of the substrate. W216 and W244 regulate access to the active site during transglycosylation by serving as gate-keepers
-
-
?
additional information
?
-
-
conserved essential catalytic residues E173, N171 and Y205 are within hydrogen bonding distance of the substrate. W216 and W244 regulate access to the active site during transglycosylation by serving as gate-keepers
-
-
?
additional information
?
-
the enzyme is responsible for the hydrolysis of beta-1,4 linkage in the N,Ndiacetylchitobiose core of N-linked glycans. It also shows transglycosylation activity
-
-
?
additional information
?
-
-
the enzyme is responsible for the hydrolysis of beta-1,4 linkage in the N,Ndiacetylchitobiose core of N-linked glycans. It also shows transglycosylation activity
-
-
?
additional information
?
-
active site structure, catalytic mechanism in which residue E173 acts as the catalytic acid/base for reaction via an oxazoline intermediate, asparagine in the active centre is in a position likely to interact with the acetyl NH group. Three-dimensional structure of this important biocatalyst reveals that residues implicated in the enhancement of transglycosylation and synthetic capacity are proximal to the active centre, where they may act to favor binding of acceptor substrates
-
-
?
additional information
?
-
-
active site structure, catalytic mechanism in which residue E173 acts as the catalytic acid/base for reaction via an oxazoline intermediate, asparagine in the active centre is in a position likely to interact with the acetyl NH group. Three-dimensional structure of this important biocatalyst reveals that residues implicated in the enhancement of transglycosylation and synthetic capacity are proximal to the active centre, where they may act to favor binding of acceptor substrates
-
-
?
additional information
?
-
-
specificity
-
-
?
additional information
?
-
-
description of substrate specificity, enzyme barely hydrolyzes xylose-containing N-glycans (Man)3(Xyl)1(GlcNAc)2-pyridylamino and (Man)3(Fuc)1(Xyl)1(GlcNAc)2-pyridylamino
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
specific for complex type sugar chains and can release the sugar chains from native glycoproteins and glycopeptides regardless of the existence of a Fuc residue on the proximal GlcNAc of the N,N'-diacetylchitobiose core of their sugar chains
-
-
?
additional information
?
-
-
the enzyme is responsible for the formation of most oligosaccharides excreted in the urine of patients with congenital exoglycosidase deficiencies and also explains why large amounts of glycopeptides are excreted in the urine of fucosidosis patients
-
-
?
additional information
?
-
-
enzyme hydrolyzes the glycosidic bond in the N,N'-diacetylchitobiose moiety of N-linked oligosaccharides in glycoproteins and glycopeptides. Enzyme also has transglycosylation activity, transferring both complex-type oligosaccharides and high mannose-type oligosaccharides of N-linked sugar chains from the glycopeptide to suitable acceptors having an N-acetylglucosamine residue
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the beta-1,4-glycosidic bond in the core N,N'-diacetylchitobiose moiety of N-glycoproteins to release the N-glycan. The enzyme also possesses transglycosylation activity and is able to transfer the released N-glycan to a GlcNAc-peptide acceptor to form a new glycopeptide
-
-
?
additional information
?
-
-
Endo-M is unique in that it can transfer en bloc the oligosaccharide of various types of N-glycans onto different acceptors, and thereby it enzymatically generates diverse glycoconjugates
-
-
?
additional information
?
-
-
Endo-M can transfer en bloc the oligosaccharide of various types of N-glycans onto different acceptors, using synthetic sugar oxazoline or biantennary complex-type sialylglycopeptide as donor substrates, and thereby it enzymatically generates diverse glycoconjugates, key residue is the catalytic Asn175. Most of the Asn175 mutants have significantly diminished hydrolysis activity but act as glycosynthases capable of using synthetic sugar oxazoline for transglycosylation
-
-
?
additional information
?
-
-
beta-N-acetylglucosaminidase is an endoglycosidase capable of hydrolyzing N,N'-diacetylchitobiose moiety in N-linked oligosaccharides bound to the asparagine amino acid residue in various glycoproteins
-
-
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additional information
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the enzyme catalyzes the hydrolysis of the beta-(1->4)-glycosidic linkage between the N,N'-diacetylchitobiose moiety of N-glycans
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additional information
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the enzyme is inactive in the presence of core fucose residue N149 and N153 linked to the reducing-end N-acetylglucosamine residue
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?
additional information
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transglycosylation reaction is investigated by using chemically modified donors
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?
additional information
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transglycosylation reaction is investigated by using chemically modified donors
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additional information
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the enzyme is probably devoted to exogeneous functions, such as degrading macromolecules for feeding purposes
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?
additional information
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the enzyme exhibits hydrolytic activity for high-mannose, hybrid, biantennary and (2,6)-branched triantennary N-linked oligosaccharides, but not for tetraantennary, (2,4)-branched triantennary, bisecting N-acetylglucosamine structure and core-fucosylated biantennary N-linked oligosaccharides. The enzyme shows almost the same relative activity for both biantennary (37%) and (2,6)-triantennary oligosaccharides (35%), and also for both hybrid (10.6%) and asialo biantennary (8.3%) oligosaccharides
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?
additional information
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the enzyme exhibits hydrolytic activity for high-mannose, hybrid, biantennary and (2,6)-branched triantennary N-linked oligosaccharides, but not for tetraantennary, (2,4)-branched triantennary, bisecting N-acetylglucosamine structure and core-fucosylated biantennary N-linked oligosaccharides. The enzyme shows almost the same relative activity for both biantennary (37%) and (2,6)-triantennary oligosaccharides (35%), and also for both hybrid (10.6%) and asialo biantennary (8.3%) oligosaccharides
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additional information
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the enzyme has dual catalytic activity in the hydrolysis and transglycosylation of complex N-glycans. Trp295 is involved in the recognition of oligosaccharide substrates
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additional information
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the enzyme has dual catalytic activity in the hydrolysis and transglycosylation of complex N-glycans. Trp295 is involved in the recognition of oligosaccharide substrates
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additional information
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the enzyme is probably devoted to exogeneous functions, such as degrading macromolecules for feeding purposes
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?
additional information
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endo-beta-N-acetylglucosaminidase PI hydrolyzes high-mannose type oligosaccharides GP-IV and GP-V faster than the hybrid type FP-I, GP-II, and GP-III. Endo-beta-N-acetylglucosaminidase PII hydrolyzes high mannose and hybrid type oligosaccharides
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additional information
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the enzyme is probably devoted to exogeneous functions, such as degrading macromolecules for feeding purposes
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additional information
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specificity
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additional information
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cleaves the N,N'-diacetylchitobiose moiety of Manalpha1, 6(manalpha1, 3)Manbeta1, 4R in which R represents either GlcNAc to Asn or N-acetylglucosamine. The enzyme can hardly act on the sugar chains with Fucalpha1, 3 or 6GlcNAc, Asn or N-acetylglucosaminitol as their R residues. The sugar chains substituted at C-3 and C-6 positions of the Manalpha1, 6 residue and at C-2 position of the Manalpha1, 3 residue by other sugars are also cleaved
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?
additional information
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completely inactive towards conjugate glycans
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additional information
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specific for glycans with a terminal chitobiose residue
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additional information
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specificity
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?
additional information
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description of substrate specificity, enzyme barely hydrolyzes xylose-containing N-glycans (Man)3(Xyl)1(GlcNAc)2-pyridylamino and (Man)3(Fuc)1(Xyl)1(GlcNAc)2-pyridylamino
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?
additional information
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recombinant Endo-LE, as well as native Endo-LE, is highly active towards high mannose type N-glycans with the Manalpha1-2Manalpha1-3Manbeta1-4GlcNAcbeta1-4GlcNAc unit
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?
additional information
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the enzyme can hydrolytically remove fucose-containing oligosaccharides from glycoproteins. The enzyme specicically hydrolyzes fucose-containing biantennary oligosaccharides. It exhibits higher activity for the substrate containing terminal sialic acid with the alpha2,3-linkage. Terminal fucosylation is not accepted
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?
additional information
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the enzyme can hydrolytically remove fucose-containing oligosaccharides from glycoproteins. The enzyme specicically hydrolyzes fucose-containing biantennary oligosaccharides. It exhibits higher activity for the substrate containing terminal sialic acid with the alpha2,3-linkage. Terminal fucosylation is not accepted
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?
additional information
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the enzyme can hydrolytically remove fucose-containing oligosaccharides from glycoproteins. The enzyme specicically hydrolyzes fucose-containing biantennary oligosaccharides. It exhibits higher activity for the substrate containing terminal sialic acid with the alpha2,3-linkage. Terminal fucosylation is not accepted
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?
additional information
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the enzyme can hydrolytically remove fucose-containing oligosaccharides from glycoproteins. The enzyme specicically hydrolyzes fucose-containing biantennary oligosaccharides. It exhibits higher activity for the substrate containing terminal sialic acid with the alpha2,3-linkage. Terminal fucosylation is not accepted
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?
additional information
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the enzyme can hydrolytically remove fucose-containing oligosaccharides from glycoproteins. The enzyme specifically hydrolyzes fucose-containing biantennary oligosaccharides. It exhibits higher activity for the substrate containing terminal sialic acid with the alpha2,3-linkage. Terminal fucosylation is not accepted
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?
additional information
?
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the enzyme can hydrolytically remove fucose-containing oligosaccharides from glycoproteins. The enzyme specifically hydrolyzes fucose-containing biantennary oligosaccharides. It exhibits higher activity for the substrate containing terminal sialic acid with the alpha2,3-linkage. Terminal fucosylation is not accepted
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?
additional information
?
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the enzyme can hydrolytically remove fucose-containing oligosaccharides from glycoproteins. The enzyme specifically hydrolyzes fucose-containing biantennary oligosaccharides. It exhibits higher activity for the substrate containing terminal sialic acid with the alpha2,3-linkage. Terminal fucosylation is not accepted
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?
additional information
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the enzyme can hydrolytically remove fucose-containing oligosaccharides from glycoproteins. The enzyme specifically hydrolyzes fucose-containing biantennary oligosaccharides. It exhibits higher activity for the substrate containing terminal sialic acid with the alpha2,3-linkage. Terminal fucosylation is not accepted
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additional information
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the enzyme functions as a virulence determinant which interferes with the host cellular immune response
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additional information
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inhibits response of human lymphocytes to mitogens and interferes with production of antibodies in mice
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additional information
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specificity
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additional information
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in the presence of exoglycosidases removing peripheral sugars, the enzyme acts on serum glycoproteins such as transferrin and fetuin
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?
additional information
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endo-beta-N-acetylglucosaminidase D does not require the presence of a free hydroxyl group at the C-4 position of the alpha-mannosyl residue of the trisaccharide glycan Manalpha, 3Manbeta1, 4GlcNAcbeta1,-
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?
additional information
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structural basis of the specificity of endo-beta-N-acetylglucosaminidase
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?
additional information
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requires choline in the teichoic acid of the cell wall substrate for the catalytic activity
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additional information
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the enzyme is probably devoted to exogeneous functions, such as degrading macromolecules for feeding purposes
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?
additional information
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cleaves the di-N-acetylchitobiose structure in asparagine-linked oligosaccharides and complex type glycopeptides from thyrogloblulin after digestion with neuramidase, beta-galactosidase and beta-N-acetylgucosaminidase
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additional information
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cleaves the di-N-acetylchitobiose structure in asparagine-linked oligosaccharides and complex type glycopeptides from thyrogloblulin after digestion with neuramidase, beta-galactosidase and beta-N-acetylgucosaminidase
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additional information
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the enzyme also possesses transglycosylation activity with sugar oxazoline as the donor substrate, but the transglycosylation yield is low due to enzymatic hydrolysis of the donor substrate and the product. The enzyme favors nonfucosylated GlcNAc acceptor for transglycosylation
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additional information
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no activity with N-glycosylated macroglobulin, N-glycosylated ovalbumin, N-glycosylated lactoferrin, N-glycosylated RNase B, and N-glycosylated fetuin
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additional information
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no activity with N-glycosylated macroglobulin, N-glycosylated ovalbumin, N-glycosylated lactoferrin, N-glycosylated RNase B, and N-glycosylated fetuin
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additional information
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additional information
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specificity
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additional information
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the rate of hydrolysis of lipid-linked (Glc)3(Man)9(GlcNAc)2 is substantially slower than that of the same oligosaccharide attached to asparagine in a peptide sequence
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additional information
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no hydrolysis of dansyl-Asn(GlcNAc)2Man, the presence of fucose attached to the asparagine-proximal core glucosamine renders the di-N-acetylchitobiosyl moiety an inactive substrate. As the number of mannose residues is increased, the rate of hydrolysis increases to a maximum at five residues. Thereafter enzyme activity declines, but the rate is still substantial on mannosyl chains containing 54 residues
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additional information
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the enzyme is probably devoted to exogeneous functions, such as degrading macromolecules for feeding purposes
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?
additional information
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the enzyme cleaves high-mannose and hybrid-type N-glycans between the first two GlcNAc residues at the reducing end
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additional information
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the enzyme hydrolyzes GlcNAcbeta1->4GlcNAc linkage of high mannose and hybrid type glycans and cannot cleave the linkage of complex type glycans
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additional information
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the enzyme does not hydrolyze fucosylated, hybrid, complex type or bisecting N-acetylglucosamine-containing structures from bovine fetuin, ovalbumin and immunglobuline G
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Taka-amylase A glycopeptide + H2O
additional information
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dansyl derivative of taka-amylase A glycopeptide
product contains N-acetylglucosaminitol and mannose in the molar ratio 1.0:5.2, but no N-acetylglucosamine or mannitol
?
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