Information on EC 3.2.1.96 - mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
3.2.1.96
-
RECOMMENDED NAME
GeneOntology No.
mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn- structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact
show the reaction diagram
-
-
-
-
Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn- structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact
show the reaction diagram
active site structure, catalytic mechanism in which residue E173 acts as the catalytic acid/base for reaction via an oxazoline intermediate, overview
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Other glycan degradation
-
SYSTEMATIC NAME
IUBMB Comments
glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-beta-glucosaminohydrolase
A group of related enzymes.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acetylglucosaminidase, endo-beta
-
-
-
-
beta-N-acetylglucosaminidase
-
-
CBM32
Q93HW0
family 32 carbohydrate-binding module of endo-beta-1,4-N-acetylglucosamidase EndoD
di-N-acetylchitobiosyl beta-N-acetylglucosaminidase
-
-
-
-
DI-N-acetylchitobiosyl beta-N-acetylglucosaminidase F1
-
-
-
-
DI-N-acetylchitobiosyl beta-N-acetylglucosaminidase F2
-
-
-
-
DI-N-acetylchitobiosyl beta-N-acetylglucosaminidase F3
-
-
-
-
Endo M
-
-
endo-beta-(1->4)-N-acetylglucosaminidase
-
-
-
-
endo-beta-1,4-N-acetylglucosamidase
Q93HW0
-
endo-beta-acetylglucosaminidase
-
-
-
-
endo-beta-GlcNAc-ase
-
-
endo-beta-GlcNAc-ase
-
-
endo-beta-N-acetylglucosaminidase
-
-
-
-
endo-beta-N-acetylglucosaminidase
-
-
endo-beta-N-acetylglucosaminidase
-
-
endo-beta-N-acetylglucosaminidase
Q9ZB22
-
endo-beta-N-acetylglucosaminidase
-
-
endo-beta-N-acetylglucosaminidase
-
-
endo-beta-N-acetylglucosaminidase
-
-
endo-beta-N-acetylglucosaminidase A
-
-
endo-beta-N-acetylglucosaminidase D
-
-
endo-beta-N-acetylglucosaminidase F
-
-
endo-beta-N-acetylglucosaminidase H
-
-
endo-beta-N-acetylglucosaminidase H
-
-
endo-beta-N-acetylglucosaminidase HS
-
-
endo-beta-N-acetylglucosaminidase L
-
-
endo-beta-N-acetylglucosaminidase M
-
-
endo-BII
-
-
Endo-Fsp
-
-
endo-GM
-
-
Endo-HO
-
-
endo-N-acetyl-beta-D-glucosaminidase
-
-
-
-
endo-N-acetyl-beta-glucosaminidase
-
-
-
-
Endoglycosidase F1
-
-
-
-
Endoglycosidase F2
-
-
-
-
Endoglycosidase F3
-
-
-
-
endoglycosidase S
-
-
-
-
ENGase A
-
-
ENGase Fsp
-
-
ENGase Mx
-
-
ENGase PI
-
-
ENGase PII
-
-
ENGase St
Stigmatella aurantiaca DW4
-
-
-
Engase1p
-
-
ENGase85A
-
isoform
ENGase85B
-
isoform
mannosyl-glycoprotein 1,4-N-acetamidodeoxy-beta-D-glycohydrolase
-
-
-
-
Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase
-
-
-
-
Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F1
-
-
-
-
Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F2
-
-
-
-
murein hydrolase
-
-
-
-
Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F3
-
-
-
-
additional information
Q9ZB22
the enzyme belongs to the glycoside hydrolase family 85, GH85
additional information
-
the enzyme belongs to the glycoside hydrolase family 85, GH85
CAS REGISTRY NUMBER
COMMENTARY
37278-88-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
ecotype Col-0
-
-
Manually annotated by BRENDA team
-
Q7X0Z0
SwissProt
Manually annotated by BRENDA team
strain C-125
-
-
Manually annotated by BRENDA team
strain 168
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
strain 168
-
-
Manually annotated by BRENDA team
pumpkin, cv. Kurokawa Amakuri
-
-
Manually annotated by BRENDA team
f. hiemalis
-
-
Manually annotated by BRENDA team
no activity in bovine
cattle kidney
-
-
Manually annotated by BRENDA team
no activity in Enterococcus faecium
-
-
-
Manually annotated by BRENDA team
no activity in sheep
kidney
-
-
Manually annotated by BRENDA team
mutant RUSAL2
-
-
Manually annotated by BRENDA team
Staphylococcus simulans 22
strain 22
-
-
Manually annotated by BRENDA team
Stigmatella aurantiaca DW4
strain DW4
-
-
Manually annotated by BRENDA team
mutant enzymes D130N, D130E, D130A, E132Q, E132A, and D130N/E132Q
-
-
Manually annotated by BRENDA team
no activity detected in pig kidney
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
Engase1p down regulation slows down free oligosaccharides bearing the di-N-acetylchitobiose to free oligosaccharides bearing a single N-acetylglucosamine conversion in Hep-G2 cells
malfunction
-
a double knockout mutant (At3g11040/At5g05460) showing no endo-beta-N-acetylglucosaminidase activity and no obvious morphological phenotype under standard conditions produces high-mannose type free N-glyans carrying the N,N'-acetylchitobiosyl unit that is produced by peptide:N-glycanase
physiological function
-
the enzyme (Engase1p)is necessary for efficient clearance of cytosolic free oligosaccharides into lysosomes. Engase1p trimming of free oligosaccharides bearing the di-N-acetylchitobiose is required for normal free oligosaccharides trafficking in HepG2 cells
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2S)-3-(benzyloxy)butane-1,2,4-triol + sialylglycopeptide
?
show the reaction diagram
-
transglycosylation
-
-
?
(GlcNAc)2(Man)5(GlcNAc)2Asn + H2O
?
show the reaction diagram
-
-
-
-
?
(GlcNAc)2(Man)6(GlcNAc)2 + H2O
GlcNAc + (GlcNAc)1(Man)6(GlcNAc)2
show the reaction diagram
-
-
-
?
(GlcNAc)3 + H2O
GlcNAc + (GlcNAc)2
show the reaction diagram
-
-
-
?
(GlcNAc)4 + H2O
(GlcNAc)2
show the reaction diagram
-
-
-
?
(Man)3(GlcNAc)2-N-Asn-dansyl + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
(Man)3(GlcNAc)2Asn + H2O
(Man)3GlcNAc + GlcNAc-Asn
show the reaction diagram
-
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
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
(Man)5(GlcNAc)2-Asn + H2O
?
show the reaction diagram
Q93HW0
-
-
-
?
(Man)5(GlcNAc)2-N-acetyl-Asn + H2O
(Man)5GlcNAc + GlcNAc-N-acetyl-Asn
show the reaction diagram
-
-
-
-
(Man)5(GlcNAc)2-N-acetyl-Asn + H2O
(Man)5GlcNAc + GlcNAc-N-acetyl-Asn
show the reaction diagram
-
-
-
?
(Man)5(GlcNAc)2-N-acetyl-Asn + H2O
(Man)5GlcNAc + GlcNAc-N-acetyl-Asn
show the reaction diagram
-
-
-
-
?
(Man)5(GlcNAc)2-N-dansyl-Asn + H2O
GlcNAc-N-dansyl-Asn + (Man)5-GlcNAc
show the reaction diagram
-
-
-
?
(Man)5(GlcNAc)2-pyridylamino + H2O
(Man)5(GlcNAc) + 2-(acetylamino)-2-deoxy-N-pyridin-2-yl-beta-D-glucopyranosylamine
show the reaction diagram
-
-
-
-
?
(Man)5(GlcNAc)2-pyridylamino + H2O
(Man)5(GlcNAc) + 2-(acetylamino)-2-deoxy-N-pyridin-2-yl-beta-D-glucopyranosylamine
show the reaction diagram
-
-
-
-
?
(Man)5(GlcNAc)2Asn + H2O
(Man)5GlcNAc + GlcNAc-Asn
show the reaction diagram
-
-
-
-
?
(Man)5(GlcNAc)2Asn + H2O
(Man)5GlcNAc + GlcNAc-Asn
show the reaction diagram
-
-
-
-
?
(Man)5(GlcNAc)2Asn + H2O
(Man)5GlcNAc + GlcNAc-Asn
show the reaction diagram
-
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-Ac + H2O
(Man)5GlcNAc + GlcNAc-Asn-Ac
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
(Man)6(GlcNAc)2-Asn + D-glucose
(Man)6GlcNAcGlc + ?
show the reaction diagram
-
-
-
?
(Man)6(GlcNAc)2-pyridylamino + H2O
?
show the reaction diagram
-
-
-
-
?
(Man)6(GlcNAc)2-pyridylamino + H2O
?
show the reaction diagram
-
-
-
-
?
(Man)6(GlcNAc)2Asn + H2O
(Man)6GlcNAc + GlcNAc-Asn
show the reaction diagram
-
-
-
-
?
(Man)6(GlcNAc)2Asn + H2O
(Man)6GlcNAc + GlcNAc-Asn
show the reaction diagram
-
-
-
-
?
(Man)6(GlcNAc)2Asn + H2O
(Man)6GlcNAc + GlcNAc-Asn
show the reaction diagram
-
-
-
?
(Man)6(GlcNAc)2Asn + H2O
(Man)6GlcNAc + GlcNAc-Asn
show the reaction diagram
-
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-Ac + H2O
(Man)6GlcNAc + GlcNAc-Asn-Ac
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
(Man)6GlcNAc2-pyridylamino + H2O
?
show the reaction diagram
-
-
-
-
?
(Man)7(GlcNAc)2-pyridylamino + H2O
?
show the reaction diagram
-
-
-
-
?
(Man)7(GlcNAc)2-pyridylamino + H2O
?
show the reaction diagram
-
-
-
-
?
(Man)8(GlcNAc)2-pyridylamino + H2O
?
show the reaction diagram
-
-
-
-
?
(Man)8(GlcNAc)2-pyridylamino + H2O
?
show the reaction diagram
-
-
-
-
?
(Man)9(GlcNAc)2-pyridylamino + H2O
?
show the reaction diagram
-
-
-
-
?
(Man)9(GlcNAc)2-pyridylamino + H2O
?
show the reaction diagram
-
-
-
-
?
(Man)9GlcNAc2-pyridylamino + H2O
?
show the reaction diagram
-
-
-
-
?
1,3-di-O-benzyl-D-erythritol + sialylglycopeptide
?
show the reaction diagram
-
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 + ?
show the reaction diagram
-
-
yield 81%
-
-
4-methylumbelliferyl di-N-acetyl-beta-chitobioside + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-mannopyranoside + H2O
4-methylumbelliferone + beta-D-mannopyranose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-N-acetylglucosaminide + H2O
4-methylumbelliferone + beta-D-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-mannopyranoside + H2O
4-methylumbelliferol + beta-D-mannopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-beta-D-N-acetylglucosamine + H2O
4-nitrophenol + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-GlcNAc + Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-ManGlcNAc2]-Lys-Thr
?
show the reaction diagram
-
-
-
-
?
9H-fluoren-9-ylmethyl [(3R)-1,3-dihydroxybutan-2-yl]carbamate + H2O
?
show the reaction diagram
-
transglycosylation
-
-
?
acetyl-Asn(GlcNAc)2(Man)6 + H2O
acetyl-AsnGlcNAc
show the reaction diagram
-
-
-
?
acetyl-Asn(GlcNAc)2(Man)6 + H2O
acetyl-AsnGlcNAc
show the reaction diagram
-
-
-
-
-
alpha1-acid glycoprotein + H2O
?
show the reaction diagram
-
-
-
-
?
asialo-N-acetyl-lactosaminic-type glycoasparagine + H2O
GlcNAc-Asn + ?
show the reaction diagram
-
-
-
?
Asn(GlcNAc)2(Man)3 + H2O
?
show the reaction diagram
-
-
-
-
?
Asn(GlcNAc)2(Man)3 + H2O
?
show the reaction diagram
-
-
-
-
?
Asn(GlcNAc)2(Man)3(Fuc)1 + H2O
?
show the reaction diagram
-
-
-
-
?
Asn(GlcNAc)2-(Man)5 + H2O
AsnGlcNAc + Man5(GlcNAc)
show the reaction diagram
-
-
-
-
?
Asn(GlcNAc)2-(Man)5 + H2O
AsnGlcNAc + Man5(GlcNAc)
show the reaction diagram
-
-
-
-
?
Asn(GlcNAc)2-(Man)5 + H2O
AsnGlcNAc + Man5(GlcNAc)
show the reaction diagram
-
-
-
?
Asn(GlcNAc)2-(Man)5 + H2O
AsnGlcNAc + Man5(GlcNAc)
show the reaction diagram
-
-
-
-
?
Asn(GlcNAc)2-(Man)5 + H2O
AsnGlcNAc + Man5(GlcNAc)
show the reaction diagram
-
-
-
?
Asn(GlcNAc)2-(Man)6 + H2O
AsnGlcNAc + (GlcNAc)1-(Man)6
show the reaction diagram
-
-
-
-
?
Asn(GlcNAc)2-(Man)6 + H2O
AsnGlcNAc + (GlcNAc)1-(Man)6
show the reaction diagram
-
-
-
-
?
Asn(GlcNAc)2-(Man)6 + H2O
AsnGlcNAc + (GlcNAc)1-(Man)6
show the reaction diagram
-
-
-
?
Asn(GlcNAc)2-(Man)6 + H2O
AsnGlcNAc + (GlcNAc)1-(Man)6
show the reaction diagram
-
-
-
?
Asn(GlcNAc)2-(Man)6(GlcNAc)2 + H2O
AsnGlcNAc + (GlcNAC)2(Man)6(GlcNAc)2
show the reaction diagram
-
-
-
?
Asn(GlcNAc)2-(Man)6(GlcNAc)2 + H2O
AsnGlcNAc + (GlcNAC)2(Man)6(GlcNAc)2
show the reaction diagram
-
-
-
?
Asn(GlcNAc)4(Man)6 + H2O
?
show the reaction diagram
-
-
-
-
?
Asn(Man4GlcNAc4) + H2O
?
show the reaction diagram
Q8NFI3
-
-
-
?
Asn-(GlcNAc)2(Man)6 + gentiobiose
?
show the reaction diagram
-
enzyme shows transglycosylation activity in the presence of glucose and gentiobiose, but with galactose
-
-
?
Asn-(GlcNAc)2(Man)6 + glucose
?
show the reaction diagram
-
enzyme shows transglycosylation activity in the presence of glucose and gentiobiose, but with galactose
-
-
?
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)
show the reaction diagram
-
-
-
?
beta-Glcp-(1-4)-GlcpNAc-oxazoline
?
show the reaction diagram
-
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
-
-
?
calf fetuin + 4-nitrophenyl-beta-D-glucoside
?
show the reaction diagram
-
-
transfer of triantennary complex type oligosaccharide, yield 3.4%
-
?
carboxypeptidase Y + Lys-Val-Ala-Asn((NeuAc-Gal-GlcNAc-Man)2Man-GlcNAc2)-Lys-Thr
?
show the reaction diagram
-
-
change of hyperglycosylated protein to a sialyl complex type glycoprotein
-
-
complex-type aspargine-linked oligosaccharide + H2O
?
show the reaction diagram
-
hydrolysis of the di-N-acetylchitobiose structure. The specificity for complex type oligosaccharides is probably defined by multiple domains in Endo D structure
-
-
?
dansyl-Asn-(GlcNAc)2(Man)5 + H2O
dansyl-Asn-GlcNAc + ?
show the reaction diagram
-
-
-
-
?
dansyl-Asn-(GlcNAc)2(Man)6 + H2O
dansyl-Asn-GlcNAc + (Man)6GlcNAc
show the reaction diagram
-
-
-
?
dansyl-Asn-(GlcNAc)2(Man)6 + H2O
dansyl-Asn-GlcNAc + (Man)6GlcNAc
show the reaction diagram
-
-
-
-
?
dansyl-Asn-(GlcNAc)2(Man)6 + H2O
dansyl-Asn-GlcNAc + (Man)6GlcNAc
show the reaction diagram
-
-
-
?
dansyl-Asn-(GlcNAc)2(Man)6 + H2O
dansyl-Asn-GlcNAc + (Man)6GlcNAc
show the reaction diagram
-
-
-
-
?
dansyl-Asn-(GlcNAc)2(Man)6 + H2O
dansyl-Asn-GlcNAc + (Man)6GlcNAc
show the reaction diagram
-
-
-
-
?
dansyl-Asn-(GlcNAc)2(Man)6(GlcNAc)2 + H2O
?
show the reaction diagram
-
-
-
-
?
dansyl-Asn-(GlcNAc)4(Man)6 + H2O
dansyl-Asn-GlcNAc + ?
show the reaction diagram
-
-
-
-
?
dansyl-Asn-(GlcNAc)4(Man)6 + H2O
dansyl-Asn-GlcNAc + ?
show the reaction diagram
-
-
-
?
dansyl-Lys-Val-Ala-Asn((NeuAc-Gal-GlcNAc-Man)2Man-GlcNAc2)-Lys-Thr + H2O
?
show the reaction diagram
-
-
-
-
?
denatured RNase B + H2O
?
show the reaction diagram
-
-
-
-
?
dolichyl pyrophosphoryl oligosaccharides + H2O
?
show the reaction diagram
-
both glucosylated and unglucosylated polymannose oligosaccharides are released by the enzyme through cleavage of the di-N-acetylchitobiose squence
-
-
?
fetuin + H2O
?
show the reaction diagram
-
-
-
-
?
fluoresceinyl 2-acetamido-2-deoxy-beta-D-glucopyranoside + H2O
fluorescein + ?
show the reaction diagram
-
-
-
?
fluoresceinyl di-N-acetyl-beta-chitobioside + H2O
fluorescein + ?
show the reaction diagram
-
-
-
?
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
show the reaction diagram
Q9ZB22
Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAc-thiazoline is a transition state mimic and is resistant to Endo-A hydrolysis
-
-
?
GlcNAc1(Man)5(GlcNAc)2-pyridylamino
?
show the reaction diagram
-
-
-
-
?
glycopeptide + H2O
?
show the reaction diagram
-
-
-
-
?
glycopeptide + H2O
?
show the reaction diagram
-
specificity
-
-
?
glycopeptide + H2O
?
show the reaction diagram
-
specificity
-
-
?
glycopeptide + H2O
?
show the reaction diagram
-
specificity
-
-
-
glycopeptide + H2O
?
show the reaction diagram
-
specificity
-
-
?
glycopeptide + H2O
?
show the reaction diagram
-
asparagine oligosaccharides of transferrin and fetuin
-
-
?
glycopeptide + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
glycopeptide from immunoglobulin M, (aa)x-Asn(GlcNAC)2(Man)3(Fuc)1
-
-
?
glycopeptide + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
high activity on dansyl transferrin glycopeptide, can also hydrolyze dansyl asialotransferrin glycopeptide and dansyl transferrin glycopeptide containing complex type sugar chains
-
-
?
glycopeptide + H2O
?
show the reaction diagram
-
hydrolysis of Asn(GlcNAc)2(Man)5 and larger neutral oligosaccharides, no hydrolysis of exoglycosidase-treated acidic IgM glycopeptides
-
-
?
glycopeptide + H2O
?
show the reaction diagram
-
high activity on oligomannoside-type glycoasparagines and glycoproteins, can also hydrolyze hybrid-type and complex-type glycoasparagines
-
-
?
glycopeptide + H2O
?
show the reaction diagram
-
generally hydrolyzes side-chain-free glycopeptides of the complex heteropolysaccharide unit
-
-
?
glycopeptide + H2O
?
show the reaction diagram
-
generally hydrolyzes glycopeptides of the mannose-N-acetylglucosamine unit
-
-
-
glycopeptide + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
two endo-beta-N-acetylglucosaminidase CI and CII with different substrate specificity
-
-
?
glycopeptide + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
high activity on dansyl ovalbumin glycopeptide, can also act on dansyl asialotransferrin glycopeptide containing biantennary type sugar chains
-
-
?
glycopeptide + H2O
?
show the reaction diagram
-
glycoasparagines derived from ovalbumin and asialoglycoasparagines derived from human serotransferrin
-
-
?
glycopeptide + H2O
?
show the reaction diagram
Stigmatella aurantiaca DW4
-
high activity on oligomannoside-type glycoasparagines and glycoproteins, can also hydrolyze hybrid-type and complex-type glycoasparagines
-
-
?
glycoprotein + H2O
?
show the reaction diagram
-
-
-
-
?
glycoprotein + H2O
?
show the reaction diagram
-
specificity
-
-
?
glycoprotein + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
cleaves the N,N'-diacetylchitobiose moiety of the sugar chain of human salivary alpha-amylase family, human transferrin and calf fetuin
-
-
?
glycoprotein + H2O
?
show the reaction diagram
-
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
-
-
?
glycoprotein + H2O
?
show the reaction diagram
-
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
-
-
?
glycosylated ascorbate oxidase + H2O
?
show the reaction diagram
-
-
-
-
?
glycosylated human apo-transferrin + H2O
?
show the reaction diagram
-
-
-
-
?
glycosylated mAb 2G12 + H2O
?
show the reaction diagram
-
-
-
-
?
glycosylated type VI-A horseraddish peroxidase + H2O
?
show the reaction diagram
-
-
-
-
?
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
?
show the reaction diagram
-
-
-
-
?
H-Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-Man-GlcNAc2]-Lys-Thr-OH + 1-deoxy-1-phenyl-alpha-D-gluco-2-heptulopyranose
?
show the reaction diagram
-
-
-
-
?
H-Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-Man-GlcNAc2]-Lys-Thr-OH + 2-benzamido-2-deoxy-D-glucopyranose
?
show the reaction diagram
-
-
-
-
?
H-Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-Man-GlcNAc2]-Lys-Thr-OH + 2-benzoylcarbonylamino-2-deoxy-D-glucopyranose
?
show the reaction diagram
-
-
-
-
?
H-Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-Man-GlcNAc2]-Lys-Thr-OH + 2-deoxy-2-naphthoamido-D-glucopyranose
?
show the reaction diagram
-
-
-
-
?
H-Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-Man-GlcNAc2]-Lys-Thr-OH + 2-deoxy-2-phenoxyacetamido-D-glucopyranose
?
show the reaction diagram
-
-
-
-
?
H-Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-Man-GlcNAc2]-Lys-Thr-OH + 2-deoxy-2-phthalimido-D-glucopyranose
?
show the reaction diagram
-
-
-
-
?
H-Lys-Val-Ala-Asn[(NeuAc-Gal-GlcNAc-Man)2-Man-GlcNAc2]-Lys-Thr-OH + benzyl beta-D-glucopyranoside
?
show the reaction diagram
-
-
-
-
?
haptoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
hen egg glycopeptide + 4-nitrophenyl-beta-D-glucose
?
show the reaction diagram
-
-
transfer of asparagine-linked oligosaccharide
-
?
human alpha1-acid glycoprotein + 4-nitrophenyl-beta-D-glucose
?
show the reaction diagram
-
-
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
?
show the reaction diagram
-
-
change of hyperglycosylated protein to a sialyl complex type glycoprotein
-
-
keratan sulfate + H2O
?
show the reaction diagram
-, Q7X0Z0
hydrolyzes keratan sulfate between the 4GlcNAcbeta1-3Gal1 structure, digests shark cartilage keratan sulfate to disaccharides and tetrasaccharides and bovine cornea keratan sulfate to hexasaccharides, prefers highly sulfated keratan sulfate
-
-
?
lectin + H2O
?
show the reaction diagram
-
-
-
-
?
Lys-Val-Ala-Asn((NeuAc-Gal-GlcNAc-Man)2Man-GlcNAc2)-Lys-Thr + 4-methylumbelliferyl-beta-D-N-acetylglucosaminide
?
show the reaction diagram
-
-
-
-
-
Man(GlcNAc)2Asn + H2O
ManGlcNAc + GlcNAcAsn
show the reaction diagram
-
-
-
-
?
Man(GlcNAc)2Asn-dansyl + H2O
ManGlcNAc + GlcNAcAsn-dansyl
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
Manalpha1-2Manalpha1-6(Manalpha1-3)Manalpha1-6(Manalpha1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-PA + H2O
?
show the reaction diagram
-
-
-
-
?
Manalpha1-3Manalpha1-6(Manalpha1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-PA + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
Manalpha1-6(Manalpha1-3)Manalpha1-6(Manalpha1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-PA + H2O
?
show the reaction diagram
-
-
-
-
?
Manalpha1-6(Manalpha1-3)Manalpha1-6(Manalpha1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-pyridylamino + H2O
?
show the reaction diagram
-
-
-
-
?
Manalpha1-6(Manalpha1-3)Manalpha1-6(Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-PA + H2O
?
show the reaction diagram
-
-
-
-
?
Manalpha1->6(Manalpha1->3)Manalpha1->6(Manalpha1->2Manalpha1->3)Manbeta1->4GlcNAcbeta1->4GlcNAcAsn + H2O
GlcNAc->N-acetylAsn + ?
show the reaction diagram
-
endo-beta-N-acetylglucosaminidase CII
-
?
Manalpha1->6(Manalpha1->3)Manalpha1->6(Manalpha1->2Manalpha1->3)Manbeta1->4GlcNAcbeta1->4GlcNAcAsn + H2O
GlcNAc->N-acetylAsn + ?
show the reaction diagram
-
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
show the reaction diagram
-
endo-beta-N-acetylglucosaminidase CI
-
?
Nalpha-9-fluorenylmethoxycarbonyl-Nbeta-3-hydroxymetyl-4-hydroxy-cyclohexyl-L-asparagine + sialylglycopeptide
?
show the reaction diagram
-
transglycosylation
-
-
?
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 + ?
show the reaction diagram
-
-
-
-
?
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 + ?
show the reaction diagram
-
-
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 + ?
show the reaction diagram
-
-
-
-
?
ovalbumin + H2O
oligosaccharides + ?
show the reaction diagram
-
-
-
?
ovalbumin + H2O
oligosaccharides + ?
show the reaction diagram
-
the enzyme hydrolyzes all five heterogenous ovalbumin glycopeptides, the rate of hydrolysis decreases as the size of the sugar moiety increases
-
?
ovalbumin + H2O
oligosaccharides + ?
show the reaction diagram
-
native ovalbumin
-
-
?
ovalbumin + H2O
oligosaccharides + ?
show the reaction diagram
-
native ovalbumin
-
?
ovalbumin + H2O
oligosaccharides + ?
show the reaction diagram
-
native ovalbumin
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
Micrococcus luteus cell wall and Bacillus subtilis cell walls
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
no hydrolyis of Micrococcus lysodeikticus cell walls
-
-
-
peptidoglycan + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
Bacillus subtilis 168
-
Micrococcus luteus cell wall and Bacillus subtilis cell walls
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
Staphylococcus simulans 22
-
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
?
show the reaction diagram
-
-
-
-
?
ribonuclease B + H2O
?
show the reaction diagram
-
-
-
-
?
ribonuclease B + H2O
?
show the reaction diagram
-
bovine pancreatic ribonuclease B
-
-
?
Ricinus lectin + H2O
?
show the reaction diagram
-
-
-
-
-
RNase B + H2O
?
show the reaction diagram
-
cleaves high mannose-type glycans in glycoproteins between the N-acetylglucosamine residues of the pentasaccharide core
-
-
?
RNase B + H2O
?
show the reaction diagram
-
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
-
-
?
transferrin + 4-nitrophenyl-alpha-D-galactoside
?
show the reaction diagram
-
-
transfer of asialobiantennary complex type oligosaccharide of human native transferrin
-
?
transferrin + 4-nitrophenyl-alpha-D-glucoside
?
show the reaction diagram
-
-
transfer of asialobiantennary complex type oligosaccharide of human native transferrin
-
?
transferrin + 4-nitrophenyl-beta-D-galactoside
?
show the reaction diagram
-
-
transfer of asialobiantennary complex type oligosaccharide of human native transferrin
-
?
transferrin + 4-nitrophenyl-beta-D-glucoside
?
show the reaction diagram
-
-
transfer of asialobiantennary complex type oligosaccharide of human native transferrin with yield of 1.1%
-
?
transferrin + 4-nitrophenyl-beta-D-mannoside
?
show the reaction diagram
-
-
transfer of asialobiantennary complex type oligosaccharide of human native transferrin
-
?
transferrin + 4-nitrophenyl-beta-D-xyloside
?
show the reaction diagram
-
-
transfer of asialobiantennary complex type oligosaccharide of human native transferrin
-
?
transferrin + 4-nitrophenyl-glycerol
?
show the reaction diagram
-
-
transfer of asialobiantennary complex type oligosaccharide of human native transferrin
-
?
transferrin + 4-nitrophenyl-N-acetyl-beta-D-glucosaminide
?
show the reaction diagram
-
-
transfer of asialobiantennary complex type oligosaccharide of human native transferrin
-
?
transferrin + H2O
complex oligosaccharides + ?
show the reaction diagram
-
-
-
?
yeast carboxypeptidase + H2O
?
show the reaction diagram
-
-
-
-
?
yeast invertase + H2O
?
show the reaction diagram
-
-
-
-
?
Manalpha1->6(Manalpha1->3)Manbeta1->4GlcNAcbeta1->4(Fucalpha1->6)GlcNAc->N-acetylAsn + H2O
Manalpha1->6(Manalpha1->3)Manbeta1->4GlcNAc + Fucalpha1-6GlcNAc-N-acetylAsn
show the reaction diagram
-
endo-beta-N-acetylglucosaminidase CI
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
specificity
-
-
-
additional information
?
-
-
specificity
-
-
-
additional information
?
-
-
specificity
-
-
-
additional information
?
-
-
specificity
-
-
-
additional information
?
-
-
specificity
-
-
-
additional information
?
-
-
specificity
-
-
-
additional information
?
-
-
specificity
-
-
-
additional information
?
-
-
two endo-beta-N-acetylglucosaminidase CI and CII with different substrate specificity
-
-
-
additional information
?
-
-
no exo-activity
-
-
-
additional information
?
-
-
in the presence of exoglycosidases removing peripheral sugars, the enzyme acts on serum glycoproteins such as transferrin and fetuin
-
-
-
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
?
-
-
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,-
-
-
-
additional information
?
-
-
structural basis of the specificity of endo-beta-N-acetylglucosaminidase
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
requires choline in the teichoic acid of the cell wall substrate for the catalytic activity
-
-
-
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
?
-
-
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
-
-
-
additional information
?
-
-
completely inactive towards conjugate 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 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
-
-
-
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 specific for high mannose glycans, no hydrolysis of either hybrid or complex glycans
-
-
-
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
?
-
-
specific for glycans with a terminal chitobiose residue
-
-
-
additional information
?
-
-
constitutive enzyme
-
-
-
additional information
?
-
-
the enzyme functions as a virulence determinant which interferes with the host cellular immune response
-
-
-
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
?
-
-
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
?
-
-
the enzyme is probably devoted to exogeneous functions, such as degrading macromolecules for feeding purposes
-
-
-
additional information
?
-
-
inhibits response of human lymphocytes to mitogens and interferes with production of antibodies in mice
-
-
-
additional information
?
-
-
inducible by yeast extract
-
-
-
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
?
-
-
cleaves the beta(1-4) link between the core GlcNAc of asparagine-linked oligosaccharides, with specificity for biantennary and triantennary complex glycans
-
-
-
additional information
?
-
Q93HW0
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
-
-
-
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
?
-
-
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
?
-
-
enzyme is highly active towards the high-mannose-type glycans bearing the Manalpha1-2Manalpha1-3Manbeta1-structural unit
-
-
-
additional information
?
-
-, Q7X0Z0
no substrates are: desulfated keratan sulfate, hyaluronic acid, chondroitin sulfate C, heparan sulfate, heparin
-
-
-
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
?
-
Q9ZB22
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
?
-
-
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
-
-
-
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
?
-
-
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, 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
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme catalyzes the hydrolysis of the beta-(1->4)-glycosidic linkage between the N,N'-diacetylchitobiose moiety of N-glycans
-
-
-
additional information
?
-
-
the enzyme is inactive in the presence of core fucose residue N149 and N153 linked to the reducing-end N-acetylglucosamine residue
-
-
-
additional information
?
-
Bacillus subtilis 168
-
no exo-activity
-
-
-
RNase B + Lys-Val-Ala-Asn((NeuAc-Gal-GlcNAc-Man)2Man-GlcNAc2)-Lys-Thr
?
show the reaction diagram
-
-
change of high-mannose type oligosaccharide of Rnase B to a sialyl complex type
-
-
Taka-amylase A glycopeptide + H2O
additional information
-
-
,, 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
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
constitutive enzyme
-
-
-
additional information
?
-
-
the enzyme functions as a virulence determinant which interferes with the host cellular immune response
-
-
-
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
?
-
-
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
?
-
-
the enzyme is probably devoted to exogeneous functions, such as degrading macromolecules for feeding purposes
-
-
-
additional information
?
-
-
inhibits response of human lymphocytes to mitogens and interferes with production of antibodies in mice
-
-
-
additional information
?
-
-
inducible by yeast extract
-
-
-
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
?
-
-
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
?
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Li+
-
maximal activation near 0.2 M LiCl with Micrococcus luteus cell walls as substrate, sharp optimal activation at 0.1 M with Bacillus subtilis cell walls as substrate
Mg2+
-
activates
Mg2+
-
slight activation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acetate
-
endo-beta-N-acetylglucosaminidase 2
Ag2+
-
1 mM, significant inactivation
alpha-D-mannosides
-
-
choline
-
2%, activates
Co2+
-
10 mM, 75% inhibition
Cu2+
-
6 mM, 80% inhibition
Cu2+
-
10 mM, 75% inhibition
EDTA
-
10 mM, 60% inhibition of endo-beta-N-acetylglucosaminidase CI, 22% inhibition of endo-beta-N-acetylglucosaminidase CII
EDTA
-
slight inhibition
Fe3+
-
10 mM, about 50% inhibition
-
Fe3+
-
10 mM, 75% inhibition
-
galactose
-
0.5 M, 23% inhibition
glycoprotein
-
glycoproteins present in the rat liver homogenate
Hg2+
-
1 mM HgCl2, 85% loss of activity
Hg2+
-
1 mM HgCl2, 60% loss of activity
Hg2+
-
1 mM HgCl2, about 50% inhibition
Hg2+
-
1 mM, significant inactivation
lipoteichoic acid
-
from Pneumococcus sp.
-
lipoteichoic acid
-
-
-
Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAc-thiazoline
-
-
Mannose
-
0.5 M, 94% inhibition
Mannose
-
0.5 mM 20% inhibition
methyl alpha-D-mannoside
-
0.05 M, 53% inhibition
N-acetylglucosamino(1->5)lactone
-
-
O-(2,3,4,6-tetra-O-acetyl-alpha-D-mannopyranosyl)-(1,6)-[(2,3,4,6-tetra-O-acetyl-alpha-D-mannopyranosyl)-(1,3)]-2,4-di-O-acetyl-beta-D-mannopyranosyl-(1,4)-(3,6-di-O-acetyl-1,2-dideoxy-alpha-D-glucopyrano)-[2,1-d]-2-thiazoline
-
-
O-(2,3,4,6-tetra-O-acetyl-alpha-D-mannopyranosyl)-(1,6)-[(2,3,4,6-tetra-O-acetyl-alpha-D-mannopyranosyl)-(1,3)]-2,4-di-O-acetyl-beta-D-mannopyranosyl-(1,4)-(3,6-di-O-acetyl-1,2-dideoxy-alpha-D-glucopyrano)-[2,1-d]-2-thiazoline
-
75% inhibition at 0.001 mM
O-(2,3,4,6-tetra-O-acetyl-alpha-D-mannopyranosyl)-(1,6)-[(2,3,4,6-tetra-O-acetyl-alpha-D-mannopyranosyl)-(1,3)]-2,4-di-O-acetyl-beta-D-mannopyranosyl-(1,4)-(3,6-di-O-acetyl-1,2-dideoxy-alpha-D-glucopyrano)-[2,1-d]-2-thiazoline
-
-
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-thiazoline
-
-
O-(beta-D-mannopyranosyl)-(1,4)-(1,2-dideoxy-alpha-D-glucopyrano)-[2,1-d]-2-thiazoline
-
-
p-Chloromercuriphenyl sulfonate
-
-
p-nitrophenyl alpha-D-mannoside
-
0.01 M, 70% inhibition; 0.01 M, no inhibition
PCMB
-
1 mM, 30% loss of activity
PCMB
-
1 mM, 84% inhibition
SDS
-
0.1%, strong inhibition
SDS
-
0.2%, complete inactivation
Urea
-
50% inhibition by 2 M, 65% inhibition at 4 M
yeast mannan
-
no inhibition
-
yeast mannan
-
15 mg/ml, 62% inhibition
-
Zn2+
-
6 mM, complete inhibition
Zn2+
-
10 mM, 50% inhibition
methyl alpha-D-mannoside
-
0.5 M, 10% inhibition
additional information
-
not inhibitory up to 0.1 mM: O-(beta-D-mannopyranosyl)-(1,4)-(1,2-dideoxy-alpha-D-glucopyrano)-[2,1-d]-2-thiazoline, 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-thiazoline
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
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
choline
-
0.1%, activates
dithiothreitol
-
1 mM, 18% stimulation
dithiothreitol
-
optimal activation at 10 mM
L-Cys
-
1 mM, 18% stimulation
nisin
-
activates hydrolysis of cell walls of Micrococcus luteus, no influence of hydrolysis of soluble peptidoglycan
Nonionic detergent
-
glycoproteins of retrovirus, lymphocytic choriomeningitis virus; Pichinde virus, and HLA-A and HLA-B antigens are cleaved in presence of nonionic detergent
-
Pep 5
-
cationic peptide antibiotic, activates hydrolysis of cell walls of Micrococcus luteus, no influence of hydrolysis of soluble peptidoglycan
-
poly(L-Lys)
-
activates hydrolysis of cell walls of Micrococcus luteus, no influence of hydrolysis of soluble peptidoglycan
Triton X-100
-
maximal stimulation at 0.03%, or small amounts of other detergents
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.4
-
(Man)5(GlcNAc)2-pyridylamino
-
-
0.2
-
(Man)5(GlcNAc)2Asn-acetyl
-
-
0.025
-
(Man)6(GlcNAc)2-pyridylamidated
-
-
0.25
-
(Man)6(GlcNAc)2-pyridylamino
-
-
0.32
-
(Man)9(GlcNAc)2-pyridylamino
-
-
0.00625
-
4-methylumbelliferyl di-N-acetyl-beta-chitobioside
-
-
-
3.5
-
4-nitrophenyl-beta-D-N-acetylglucosamine
-
pH 6.5, 30C, recombinant mutant N175Q
4.2
-
4-nitrophenyl-beta-D-N-acetylglucosamine
-
pH 6.5, 30C, recombinant mutant N175G
9.1
-
4-nitrophenyl-beta-D-N-acetylglucosamine
-
pH 6.5, 30C, recombinant mutant Y217F/N175Q
52
-
4-nitrophenyl-beta-D-N-acetylglucosamine
-
pH 6.5, 30C, recombinant mutant D279A
77.4
-
4-nitrophenyl-beta-D-N-acetylglucosamine
-
pH 6.5, 30C, recombinant mutant N175A
0.25
-
Asn(GlcNAc)2-(Man)5
-
-
-
0.68
-
dansyl asialotransferrin glycopeptide
-
-
-
2
-
dansyl asialotransferrin glycopeptide
-
-
-
0.0868
-
dansyl derivative of Taka-amylase A glycopeptide
-
-
-
0.207
-
dansyl-Asn-(GlcNAc)2(Man)5
-
wild-type, pH 6.0, 37C
0.876
-
dansyl-Asn-(GlcNAc)2(Man)5
-
mutant E174A, presence of 2 M sodium azide, pH 6.0, 37C
0.3
-
dansyl-Asn-(GlcNAc)2(Man)6
-
-
0.3
-
dansyl-Asn-(GlcNAc)4(Man)6
-
-
0.3
-
dansyl-Asn-(GlcNAc)4(Man)6
-
-
54
-
Keratan sulfate
-, Q7X0Z0
keratan sulfate from cartilage, pH 6, 37C
143
-
Keratan sulfate
-, Q7X0Z0
keratan sulfate from cornea, pH 6, 37C
0.7
-
Man(GlcNAc)2Asn-dansyl
-
-
0.05
-
Manalpha1->6(Manalpha1->3)Manalpha1->6(Manalpha1->2Manalpha1->3)Manbeta1->4GlcNAcbeta1->4GlcNAcAsn
-
endo-beta-N-acetylglucosaminidase CII
2.56
-
ovalbumin
-
-
-
0.032
-
Manalpha1->6(Manalpha1->3)Manbeta1->4GlcNAcbeta1->4(Fucalpha1->6)GlcNAc->N-acetylAsn
-
endo-beta-N-acetylglucosaminidase CI
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic analysis, kinetics for the transglycosylation using Man9GlcNAc-oxazoline as a donor substrate, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
11
-
4-nitrophenyl-beta-D-N-acetylglucosamine
-
pH 6.5, 30C, recombinant mutant N175A
64
-
4-nitrophenyl-beta-D-N-acetylglucosamine
-
pH 6.5, 30C, recombinant mutant N175G
67
-
4-nitrophenyl-beta-D-N-acetylglucosamine
-
pH 6.5, 30C, recombinant mutant Y217F/N175Q
150
-
4-nitrophenyl-beta-D-N-acetylglucosamine
-
pH 6.5, 30C, recombinant mutant D279A
250
-
4-nitrophenyl-beta-D-N-acetylglucosamine
-
pH 6.5, 30C, recombinant mutant N175Q
0.0458
-
dansyl-Asn-(GlcNAc)2(Man)5
-
mutant E174A, presence of 2 M sodium azide, pH 6.0, 37C
365
-
dansyl-Asn-(GlcNAc)2(Man)5
-
wild-type, pH 6.0, 37C
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.023
-
4-nitrophenyl-beta-D-N-acetylglucosamine
-
pH 6.5, 30C, recombinant mutant N175A
302424
0.126
-
4-nitrophenyl-beta-D-N-acetylglucosamine
-
pH 6.5, 30C, recombinant mutant Y217F/N175Q
302424
0.27
-
4-nitrophenyl-beta-D-N-acetylglucosamine
-
pH 6.5, 30C, recombinant mutant N175G
302424
1.2
-
4-nitrophenyl-beta-D-N-acetylglucosamine
-
pH 6.5, 30C, recombinant mutant N175Q
302424
1.28
-
4-nitrophenyl-beta-D-N-acetylglucosamine
-
pH 6.5, 30C, recombinant mutant D279A
302424
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
10
-
Fe3+
-
-
-
2000
-
Urea
-
-
10
-
Zn2+
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00022
-
O-(2,3,4,6-tetra-O-acetyl-alpha-D-mannopyranosyl)-(1,6)-[(2,3,4,6-tetra-O-acetyl-alpha-D-mannopyranosyl)-(1,3)]-2,4-di-O-acetyl-beta-D-mannopyranosyl-(1,4)-(3,6-di-O-acetyl-1,2-dideoxy-alpha-D-glucopyrano)-[2,1-d]-2-thiazoline
-
pH 6.5, 30C
0.00042
-
O-(2,3,4,6-tetra-O-acetyl-alpha-D-mannopyranosyl)-(1,6)-[(2,3,4,6-tetra-O-acetyl-alpha-D-mannopyranosyl)-(1,3)]-2,4-di-O-acetyl-beta-D-mannopyranosyl-(1,4)-(3,6-di-O-acetyl-1,2-dideoxy-alpha-D-glucopyrano)-[2,1-d]-2-thiazoline
-
pH 6.5, 30C
0.006
-
O-(2,3,4,6-tetra-O-acetyl-alpha-D-mannopyranosyl)-(1,6)-[(2,3,4,6-tetra-O-acetyl-alpha-D-mannopyranosyl)-(1,3)]-2,4-di-O-acetyl-beta-D-mannopyranosyl-(1,4)-(3,6-di-O-acetyl-1,2-dideoxy-alpha-D-glucopyrano)-[2,1-d]-2-thiazoline
-
pH 6.5, 30C
0.013
-
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-thiazoline
-
pH 6.5, 30C
0.064
-
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-thiazoline
-
pH 6.5, 30C
0.038
-
O-(beta-D-mannopyranosyl)-(1,4)-(1,2-dideoxy-alpha-D-glucopyrano)-[2,1-d]-2-thiazoline
-
pH 6.5, 30C
0.08
-
O-(beta-D-mannopyranosyl)-(1,4)-(1,2-dideoxy-alpha-D-glucopyrano)-[2,1-d]-2-thiazoline
-
pH 6.5, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00039
-
-
mutant N175A, hydrolytic activity, pH 6.25, 30C
0.0017
-
-
mutant N249S, transglycosylation activity, pH 6.25, 30C
0.0018
-
-
mutant W251N, transglycosylation activity, pH 6.25, 30C
0.0027
-
-
mutant Y250N, transglycosylation activity, pH 6.25, 30C
0.01
-
-
specific transglycosylation activity of mutant N171A
0.023
-
-
mutant N230S, transglycosylation activity, pH 6.25, 30C; mutant Y217F/W228F, transglycosylation activity, pH 6.25, 30C
0.026
-
-
mutant W228F, transglycosylation activity, pH 6.25, 30C
0.058
-
-
wild-type, transglycosylation activity, pH 6.25, 30C
0.085
-
-
mutant Y217F, transglycosylation activity, pH 6.25, 30C
0.24
-
-
-
0.299
-
-
endo-beta-N-acetylglucosaminidase CI
0.3
-
-
mutant Y250N, hydrolytic activity, pH 6.25, 30C
0.304
-
-
endo-beta-N-acetylglucosaminidase CII
0.32
-
-
mutant N249S, hydrolytic activity, pH 6.25, 30C
0.43
-
-
mutant W251N, hydrolytic activity, pH 6.25, 30C
0.46
-
-
mutant W228F, hydrolytic activity, pH 6.25, 30C
0.62
-
-
mutant Y217F/W228F, hydrolytic activity, pH 6.25, 30C
0.7
-
-
mutant N230S, hydrolytic activity, pH 6.25, 30C
1.2
-
-
mutant Y217F, hydrolytic activity, pH 6.25, 30C
1.6
-
-
wild-type, hydrolytic activity, pH 6.25, 30C
1.61
-
-
specific transglycosylation activity of mutant Y205F
1.72
-
-
specific transglycosylation activity of the wild-type
2.3
-
Q8NFI3
-
5.11
-
-
specific transglycosylation activity of mutant Y299F
9.5
-
-
purified recombinant wild-type enzyme, hydrolysis of natural N-glycan substrate
400
-
-
-
1270
-
-, Q7X0Z0
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
N175 mutant hydrolytic activities, and that of mutants E177A, E177Q, E177H, D218A, and D279A lay below 1% of wild-type activity, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
3.5
-
endo-beta-N-acetylglucosaminidase 2
4
4.5
-
hydrolysis of Man(GlcNAc)2Asn-dansyl
4
4.5
-
ENGase L
4
4.8
-
hydrolysis of dansyl derivative of Taka-amylase A glycopeptide
4.5
5.5
-
Micrococcus luteus cell walls as substrate, in 50 mM acetic acid/acetate buffer or succinate/NaOH buffer
4.5
-
-
endo-beta-N-acetylglucosaminidase 1
4.5
-
-
Bacillus subtilis cell walls
5
6
-
hydrolysis of dansyl-Asn-(GlcNAc)4(Man)6
5
6
-
hydrolysis of dansyl-Asn-(GlcNAc)4(Man)6
5
6
-
ENGase PI
5
6
-
ENGase PI
5
9
-
enzyme is most active within this range
5
-
-
hydrolysis of ovalbumin
5
-
-, Q7X0Z0
-
5.4
-
-
hydrolysis of (Man)5(GlcNAc)2Asn-acetyl, enzyme type F-II
5.5
6
-
enzyme form endo-BI and endo-BII
5.5
-
-
hydrolysis of dansyl-Asn(GlcNAc)2-(Man)6; hydrolysis of peptide-Asn(GlcNAc)2(Man)3(Fuc)1
5.5
-
-
hydrolysis of dansyl-Asn(GlcNAc)2-(Man)6
5.5
-
-
ENGase H
5.9
-
-
hydrolysis of (Man)5(GlcNAc)2Asn-acetyl, enzyme type F-I
6
6.5
-
ENGase CI
6
8
-
ENGase PII
6
-
-
hydrolysis of (Man)6(GlcNAc)2-pyridylamino
6.5
-
-
Micrococcus luteus cell walls as substrate
6.5
-
-
in 20 mM phosphate buffer, at 30C
6.5
-
-
endo-beta-N-acetylglucosaminidase CI, citrate-phosphate buffer
6.5
-
-
hydrolysis of (Man)5(GlcNAc)2Asn-acetyl
6.5
-
-
hydrolysis of (Man)6(GlcNAc)2-pyridylamino
6.5
-
-
hydrolysis of Asn(GlcNAc)2-(Man)5
6.5
-
-
endo-beta-N-acetylglucosaminidase CI
6.5
-
-
-
6.5
-
-
-
6.5
-
-
hydrolytic assay at
6.5
-
-
isoform ENGase85A
7
-
-
endo-beta-N-acetylglucosaminidase CII, in Tris buffer and citrate-phosphate buffer. endo-beta-N-acetylglucosaminidase CI in Tris buffer
7
-
-
-
7
-
-
endo-beta-N-acetylglucosaminidase CI
7
-
-
ENGase CII
7
-
-
hydrolysis of (Man)6(GlcNAc)2-pyridylamino
7
-
-
isoform ENGase85B
7.2
-
-
transglycosylation assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.3
5.5
-
pH 2.3: about 20% of maximal activity, pH 5.5: about 25% of maximal activity
2.5
4.5
-
about 70% of maximal activity at pH 2.5 and at pH 4.5, endo-beta-N-acetylglucosaminidase 2
2.5
5
-
about 30% of maxiaml activity at pH 2.5 and at pH 5.0
2.5
8
-
pH 2.5: about 20% of maximal activity, pH 8.0: about 30% of maximal activity
3
8
-
pH 3.0-5.0: optimum, pH 8.0: 60% of maximal activity
3.3
6.3
-
pH 3.3: about 60% of maximal activity, pH 6.3: about 50% of maximal activity
4.5
7
-
pH 4.5: about 60% of maximal activity, pH 7.0: about 50% of maximal activity, endo-beta-N-acetylglucosaminidase 1
4.5
8
-
pH 4.5: about 75% of maximal activity, pH 8.0: about 40% of maximal activity
4.5
8.5
-
pH 4.5: about 25% of maximal activity, pH 8.5: about 30% of maximal activity
5
8.5
-
about 55% of maximal activity at pH 5.0 and at pH 8.5
5.3
8.2
-
about 50% of maximal activity at pH 5.3 and at pH 8.2
5.5
9.5
-
pH 5.5: maximal activity, pH 9.5: about 40% of maximal activity, hydrolysis of dansyl-Asn(GlcNAc)2(Man)6
6
7.5
-
80% of maximal activity at pH 6.0 and at pH 7.5
9
-
-
60% activity at pH 9
10
-
-
28% activity at pH 10
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
40
-
-
hydrolysis of (Man)6(GlcNAc)2-pyridylamino
55
-
-, Q7X0Z0
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
60
-
25C: about 80% of maximal activity, 60C: about 45% of maximal activity
50
60
-, Q7X0Z0
80% activity at 50C, 79% activity at 60C
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Stigmatella aurantiaca DW4
-
-
-
Manually annotated by BRENDA team
-
expression of Endo-LE mRNA does not vary significantly with the tomato ripening process
Manually annotated by BRENDA team
-
leaf blade, high activity
Manually annotated by BRENDA team
-
in adult leaves the predominance of isoform ENGase85A accounts for 80% of the total activity
Manually annotated by BRENDA team
-
highest activity in rootlets
Manually annotated by BRENDA team
-
epithelial cells peeling from the oral cavity epithelium into saliva
Manually annotated by BRENDA team
Q8NFI3
highest activity
Manually annotated by BRENDA team
-
isoform ENGase85A only
Manually annotated by BRENDA team
Q8NFI3
; weak expression
Manually annotated by BRENDA team
additional information
-
enzyme activity is present in all organs tested, with quantitative differences. In youngest parts of the plant, both endo N-acetyl-beta-D-glucosaminidase and N4-N-acetyl-beta-D-glucosaminidase activity are detected, associated with high levels of proteins and protease activities
Manually annotated by BRENDA team
additional information
-
no enzyme activity is detected in siliques
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Staphylococcus simulans 22
-
-
-
Manually annotated by BRENDA team
-
recombinant enzyme produced in Escherichia coli appears both in the periplasmic space and in the cell
Manually annotated by BRENDA team
-
no evidence for a lysosomal enzyme form
Manually annotated by BRENDA team
-
recombinant enzyme produced in Escherichia coli appears both in the periplasmic space and in the cell
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
17500
-
-
enzyme type F-II, gel filtration
23500
-
-
gel filtration
27000
-
-
gel filtration
27000
-
-
equilibrium sedimentation analysis
27200
-
-
equilibrium sedimentation
30000
-
-
SDS-PAGE
31000
-
-
gel filtration
35000
-
-
gel filtration
41670
-
-
MALDI-TOF mass spectrometry
46000
-
-
gel filtration
49500
-
-
equilibrium sedimentation
52000
-
-
enzyme type F-I, gel filtration
54000
-
-
gel filtration
55000
-
Q8NFI3
SDS-PAGE
56000
-
-
gel filtration
62000
-
-
gel filtration
90000
-
-
SDS-PAGE
95000
-
-
gel filtration
150000
-
-
enzyme form endo-BII, non-denaturing PAGE
178000
-
-
SDS-PAGE
190000
-
-
gel filtration
200000
-
-, Q7X0Z0
SDS-PAGE and calculated from amino acid sequence
210000
-
-
enzyme form endo-BI, non-denaturing PAGE
280000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 64000, SDS-PAGE
?
-
x * 150000, SDS-PAGE
?
-
x * 72000, SDS-PAGE
?
-
x * 32000, ENGase F1, SDS-PAGE; x * 33000, ENGase F3, SDS-PAGE; x * 39500, ENGase F2, SDS-PAGE
?
-
x * 30000, SDS-PAGE
?
-
x * 27000, SDS-PAGE
?
-
x * 27000, SDS-PAGE
?
-
x * 106000, endo-beta-N-acetylglucosaminidase PI, SDS-PAGE; x * 94000, endo-beta-N-acetylglucosaminidase PI, SDS-PAGE
?
-
x * 183200, calculated from amino acid sequence
?
Stigmatella aurantiaca DW4
-
x * 27000, SDS-PAGE
-
dimer
-
2 * 90000, SDS-PAGE
dimer
-
2 * 55000, SDS-PAGE
dimer
Bacillus subtilis 168
-
2 * 90000, SDS-PAGE
-
monomer
-
1 * 30000, SDS-PAGE
monomer
-
1 * 27000, SDS-PAGE
monomer
-
1 * 52000-54000, SDS-PAGE
monomer
-
1 * 35000, SDS-PAGE
monomer
-
1 * 52000, SDS-PAGE in presence of 2-mercaptoethanol
monomer
-
1 * 42000, SDS-PAGE
additional information
-
the GH85 enzyme Endo-A displays a trimodular architecture in which a (betaalpha)8 catalytic domain occurs with two ancillary beta-sheet modules
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
no modification
-
contains no carbohydrate
proteolytic modification
-
autolysin atl gene product is a bifunctional protein that has an amidase domain and an endo-beta-N-acetylglucosaminidase domain which must undergo proteolytic processing to generate two extracellular lytic enzymes
no modification
-
contains no carbohydrate
proteolytic modification
-
a proenzyme or more probably a prepro enzyme may be the primary product of translation. The 42 or 44 residue leader sequence is partially removed by E. coli
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Endo-A in the native form or in complex with Man3GlcNAc-thiazoline or GlcNAc-Asn, between 2-3.5 A resolution. Crystals of Endo-A belong to P1 space group with four molecules of the protein in the asymmetric unit. The carbohydrate moiety sits above the TIM-barrel in a cleft region surrounded by aromatic residues. N171 is hydrogen bonded to the thiazoline nitrogen, mimicking the ability of the asparagine to orient the acetamido group for a nucleophilic attack on the anomeric carbon
-
purifed recombinant wild-type enzyme and mutant E173Q in unlabeled or selenomethionine-labeled forms, 1:1 mixture of 42 mg/mL protein with a reservoir solution consisting of 0.35 M KSCN, 0.1 M 1,3-bis(tris(hydroxymethyl)methylamino)propane, pH 6.5, and 15% w/v PEG 3350, 30 days at 4 C for the unlabeled, and 14 days at 18 C for the SeM-labeled enzymes, X-ray diffraction and analysis at 1.8 A resolution, multiple-wavelength anomalous scattering methods, structure modelling, overview
-
hanging drop vapor diffusion method, complexed with Gal-beta(1-4)-GlcNAc-beta(1-2)-Man-alpha(1-3)[Gal-beta(1-4)-GlcNAc-beta(1-2)-Man-alpha(1-6)]Man-beta(1-4)-GlcNAc
-
CBM32 (a family 32 carbohydrate-binding module of endo-beta-1,4-N-acetylglucosamidase), hanging drop vapor diffusion method, using 30% (w/v) PEG 4000, 0.2 M ammonium acetate and 0.1 M sodium citrate pH 6.5
-
at 1.9 A resolution
-
wild-type enzyme and mutant enzymes D130N, D130E, D130A, E132Q, E132A, and D130N/E132Q
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.2
8
-
room temperature, 24 h, enzyme type F-II retains 80-100% of its activity
4
6
-
in the refrigerator, stable for at least 4 months
4
7
-
stable
4
8
-
4C, 48 h, stable
4.5
8.5
-
37C, stable between pH 4.5 and pH 8.5, rapid loss of activity below pH 4.5
4.5
8.5
-
37C, stable between pH 4.5 and pH 8.5, rapid loss of activity below pH 4.5
4.5
-
-
37C, rapid inactivation below
5
7
-
4C, 2 days, stable
5
7
-, Q7X0Z0
enzyme is stable between pH 6-7, less stable at pH 5
5
8
-
room temperature, 24 h, enzyme type F-I is stable, unstable below pH 5
6
7
-
4C, 10 min, stable
6
8
-
4C, 5 d, stable
7
8
-
4C, 3 days, stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
50
-
stable
37
-
-
pH 4.5-8.5, protein concentration 0.0003 mg/ml, stable. Rapid loss of activity below pH 4.5
37
-
-
48 h, stable
37
-
-
24 h, 30% loss of activity
40
-
-
10 min, 10 mM phosphate buffer, pH 7.0, stable up to
40
-
-
10 min, stable up to
45
55
-, Q7X0Z0
stable up to 45C, retains 65% activity at 50C after 1 h at pH 6 in 100 mM acetate buffer, enzyme is unstable at 55C
45
-
-
10 min, stable up to
45
-
-
10 min, 10 mM phosphate buffer, pH 7.0, stable below
45
-
-
10 min, 5% loss of activity, endo-beta-N-acetylglucosaminidase PII
50
-
-
pH 5.0, 0.1 M acetate buffer, 2 h, less than 10% loss of activity
50
-
-
70 min, 75% loss of activity
50
-
-
10 min, 60% loss of activity, endo-beta-N-acetylglucosaminidase PII
50
-
-
unstable
50
-
-
5 min, about 90% loss of activity
55
-
-
10 min, 10 mM phosphate buffer, pH 7.0, 70% loss of activity
55
-
-
10 min, stable, endo-beta-N-acetylglucosaminidase I
55
-
-
5 min, about 65% loss of activity
60
-
-
10 min, more than 90% loss of activity
60
-
-
stable up to
80
-
-
10 min, 65% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
trypsin, 0.01 mg/ml, pH 7.2, 50 mM Tris/HCl, 70% inactivation after 15 min
-
stable to lyophilization
-
stable to freezing at -70C
-
activity decreases on repeated freezing
-
pronase, trypsin, and chymotrypsin at 2.5 mg per ml, when incubated with 0.005-0.010 mg of enzyme per ml, has little or no effect after 5 h at 37C. 5 mg/ml pronase inactivates slowly during a 12 h period
-
stable to repeated freezing and thawing or lyophilization
-
20-30% loss of initial activity is lost when the protein concentration is decreased to less than 0.02-0.03 mg/ml
-
retains nearly 30% of its activity in 1% SDS
-
stable to incubation with 250fold excess of either Pronase, chymotrypsin, or trypsin w/w. Slow inactivation by 1000fold excess of Pronase during 12 h incubation
-
stable to lyophilization
-
stable to repeated freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stable for at least 4 months in the refrigerator at pH 4.0-6.0
-
4C, stable for months
-
-10C up to -20C, inactivation
-
4C, 6 months, 10-15% loss of activity
-
4C, loss of activity within two to three days
-
4C, with a drop of toluene, stable for at least 1 year
-
0C, stable for at least 1 month
-
-20C, pH 7.0, 3 months, stable
-
0C, stable for at least 1 month
-
-20C, protein concentration more than 0.5 mg/ml, less than 30% loss of activity after 2 months
-
-20C, stable for at least 2 years
-
4C, stable for up to 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Ni-NTA column chromatography
-
on Ni-NTA resin and on ion-exchange chromatography column and by gel filtration
-
enzyme form endo-BI and endo-BII
-
endo-beta-N-acetylglucosaminidase CI and CII
-
carbohydrate-binding module fused to the N-terminus of mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase. The fusion protein also carries a hexahistidine tag
-
endo-beta-N-acetylglucosaminidase F-I and F-II
-
endo-beta-N-acetylglucosaminidase F-I and F-II; partial
-
partial
-
endo-beta-N-acetylglucosaminidase 1 and 2
-
homogeneity
Q8NFI3
endo-beta-N-acetylglucosaminidase PI and PII
-
Ni2+-affinity resin column chromatography and Sephacryl S-200 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), and of selenomethionine-labeled enzymes in strain B834(DE3)
-
into vector pET15b and transformed into Escherichia coli BL21(DE3) cells
-
pGEX-2T/Endo-A plasmid overexpressed in Escherichia coli
-
expressed in Escherichia coli
-
expression in Escherichia coli, carbohydrate-binding module fused to the N-terminus of mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase. The fusion protein also carries a hexahistidine tag
-
expressed in Escherichia coli
-
expressed in COS-7 cells
Q8NFI3
expressed in Saccharomyces cerevisiae png1DELTA cells
-
expressed in Candida boidinii
-
expression of wild-type Endo-M and mutants in Escherichia coli strain BL21(DE3)
-
expressed from vector pET41-b in Escherichia coli BL21 (DE3)
-
expression in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli B834 (DE3) cells
-
overexpression in Escherichia coli TOP10, enzymes with truncation or point mutation
-
expression in Escherichia coli
-
expression in Escherichia coli with 150fold improvement in yield
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E173A
-
mutation in catalytically essential residue. Partial rescue of activity by addition of sodium azide or sodium formate, the produced beta-glycosyl azide retaines the anomeric configuration
E173Q
-
site-directed mutagenesis, the mutant shows increased transglycosylation activity compared to the wild-type enzyme, three-dimensional structure determination and analysis, overview
N171A
-
completely abolishes enzymatic activity
Y205F
-
exhibits reduced hydrolysis activity with an increase in transglycosylation yields
Y299F
-
3fold increase in the transglycosylation activity, while the hydrolysis activity remains unchanged
W215R
-
enzyme has lower transglycosylation activity
D121N
-
mutant has no enzymatic activity
D124N
-
mutant has 35% of the wild-type activity
D126E
-
mutant has 0.1% of the wild-type activity
D126N
-
mutant has 2% of the wild-type activity
D127A
-
mutant has 1.8% of the wild-type activity
D127E
-
mutant has 7.2% of the wild-type activity
D127N
-
mutant has 6% of the wild-type activity
E128A
-
mutant has no enzymatic activity
F42G
-
mutant has 30% of the wild-type activity
G122L
-
mutant has 4.4% of the wild-type activity
N17A
-
mutant has 80% of the wild-type activity
N45A
-
mutant has 70% of the wild-type activity
N58A
-
mutant has 100% of the wild-type activity
N60A
-
mutant has 100% of the wild-type activity
N89S
-
mutant has 100% of the wild-type activity
Q91A
-
mutant has 100% of the wild-type activity
V16A
-
mutant has 70% of the wild-type activity
Y129A
-
mutant has 70% of the wild-type activity
Y13A
-
mutant has 0.1% of the wild-type activity
Y164A
-
mutant has 70% of the wild-type activity
Y191A
-
mutant has 0.2% of the wild-type activity
Y241A
-
mutant has 20% of the wild-type activity
Y56A
-
mutant has 100% of the wild-type activity
D147A
-
site-directed mutagenesis, the mutant show 19% reduced activity compared to the wild-type enzyme
D158A
-
site-directed mutagenesis, the mutant show 88% reduced activity compared to the wild-type enzyme
D170A
-
site-directed mutagenesis, the mutant show 98.8% reduced activity compared to the wild-type enzyme
D218A
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
D279A
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
E177A
-
complete loss of activities
E177A
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
E177H
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
N175A
-
mutant acts like a glycosynthase. Mutation knocks out the hydrolytic activity, but mutant takes sugar oxazolines as donor substrates for transglycosylation
N175A
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
N175D
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
N175H
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
N175M
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
N175Q
-
site-directed mutagenesis, the mutant possesses dramatically enhanced glycosynthase-like activity with sugar oxazoline in comparison with N175A and a transglycosidase-like activity with natural N-glycan as well; site-directed mutagenesis, the mutant shows only residual hydrolytic activity
N175Q/Y217F
-
site-directed mutagenesis, the double mutant is a glycosynthase, but the additional mutation at Tyr217 does not further enhance the activity
N175S
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
N175T
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
N230S
-
reduction in transglycosylation activity
N249S
-
almost complete loss of transglycosylation activity
W228F
-
reduction in transglycosylation activity
W251N
-
almost complete loss of transglycosylation activity
Y217F
-
enhanced transglycosylation activity and diminished hydrolytic activity
Y217F/W228F
-
reduction in transglycosylation activity
Y250N
-
almost complete loss of transglycosylation activity
del316/delY319/E320
-
mutation completely removes the activity for (Man)5(GlcNAc)2Asn, a low level of activity towards (Man)3(GlcNAc)2Asn remains
delE324
-
loss of activity
D130
-
1.25-3.14% of the activity of the wild-type enzyme, depending on assay method
D130A
-
0.04-0.1% of the activity of the wild-type enzyme
D130N
-
0.1-0.21% of the activity of the wild-type enzyme, depending on assay method
D130N/E132Q
-
no actvity
E132A
-
no actvity
E132D
-
0.03-0.05% of the activity of the wild-type enzyme
E132Q
-
less than 0.05% of the activity of the wild-type enzyme
E172Q
-
mutant has no enzymatic activity
additional information
-
deletion of 219 C-terminal amino acid residues, deletion mutant shows wild-type activity
E172Q
-
mutant has no enzymatic activity
-
additional information
-
deletion of 219 C-terminal amino acid residues, deletion mutant shows wild-type activity
-
W215R
-
enzyme has lower transglycosylation activity
-
additional information
-
a carbohydrate-binding module is fused to the N-terminus of mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase. The fusion protein also carries a hexahistidine tag and is as effective as the native enzyme at deglycosylating RNaseB
E177Q
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
additional information
-
as to the specific hydrolysis activity for N-glycopeptide SGP, i.e. biantennary complex-type sialylglycopeptide, all the Asn175 mutants show none or only marginal activity, but most of the Asn175 mutants show transglycosylation activity with Man9GlcNAc-oxazoline
delW359/delY360
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loss of activity
additional information
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truncated enzyme form in which 134 N-terminal and 599-C-tterminal amino acids are deleted, still retains enzymatic activity. The specificity of the truncated enzyme is indistinguishable from the intact enzyme and also acts on the core structure of the asparagine-linked oligosaccharides attached to intact IgG
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
after denaturation with 8 M urea
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
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fluorescence-based assay for the transglycosylation activity of endo-beta-N-acetylglucosaminidases, highly sensitive, easy and quantitative method for screening endo-beta-N-acetylglucosaminidases with transglycosylation activity useful for glycoconjugate synthesis
synthesis
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highly efficient chemoenzymatic synthesis of N-glycopeptides. The use of the synthetic oligosaccharide oxazolines as the donor substrates for the transglycosylation expands the substrate availability and results in substantial enhancement of the synthetic efficiency
synthesis
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construction of natural or selectively modified glycopeptides by endoglycosidase-catalyzed transglycosylation
nutrition
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deglycosylation of hen ovomucoid, enzyme may be useful for the preparation of allergen-free egg products
analysis
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essential reagent for the investigation of the structure and functions of glycoproteins
analysis
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study of glycans and protein backbones as discrete entities and for defining the nature of the glycan-protein interface
analysis
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essential reagent for the investigation of the structure and functions of glycoproteins
analysis
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the enzyme will be an excellent tool for clarification of the structures and functions of complex oligosaccharides in glycoproteins
medicine
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use of enzyme for synthesis of a human immunodeficiency virus type 1 glycopeptide with potent anti-HIV activity
synthesis
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fluorescence-based assay for the transglycosylation activity of endo-beta-N-acetylglucosaminidases, highly sensitive, easy and quantitative method for screening endo-beta-N-acetylglucosaminidases with transglycosylation activity useful for glycoconjugate synthesis
synthesis
-
highly efficient chemoenzymatic synthesis of N-glycopeptides. The use of the synthetic oligosaccharide oxazolines as the donor substrates for the transglycosylation expands the substrate availability and results in substantial enhancement of the synthetic efficiency
synthesis
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use of enzyme for the in vitro synthesis of glycoproteins containing complex type oligosaccharides from glycoproteins produced by yeast. Transglycosylation activity of enzyme can change high-mannose type oligosaccharides on glycoproteins to complex type ones
synthesis
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use of enzyme for synthesis of a human immunodeficiency virus type 1 glycopeptide with potent anti-HIV activity
analysis
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essential reagent for the investigation of the structure and functions of glycoproteins
analysis
-
the enzyme will be an excellent tool for clarification of the structures and functions of complex oligosaccharides in glycoproteins
analysis
-
essential reagent for the investigation of the structure and functions of glycoproteins
analysis
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useful in metabolic studies dealing with oligosaccharide-lipid assembly and their involvement in the N-glycosylation of proteins
analysis
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essential reagent for the investigation of the structure and functions of glycoproteins
analysis
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commonly used reagent in glycobiology research, including the characterization of oligosaccharides in glycoproteins
synthesis
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synthesis of oxazoline mono-, di-, tri- and hexasaccharides as potential glycosyl donors for enzyme catalyzed glycosylation of glycopeptides and glycoprotein remodelling
analysis
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essential reagent for the investigation of the structure and functions of glycoproteins
additional information
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polymerization by endo-beta-N-acetylglucosaminidase may find useful applications for the synthesis of novel artificial polysaccharides