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Information on EC 3.2.1.96 - mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase and Organism(s) Homo sapiens

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EC Tree
IUBMB Comments
A group of related enzymes.
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
nagase, beta-n-acetylglucosaminidase, endo-beta-n-acetylglucosaminidase h, endo h, endo-beta-n-acetylglucosaminidase, murein hydrolase, endod, engase, endo-beta-n-acetylglucosaminidase f, endo-m, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylglucosaminidase, endo-beta
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di-N-acetylchitobiosyl beta-N-acetylglucosaminidase
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DI-N-acetylchitobiosyl beta-N-acetylglucosaminidase F1
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DI-N-acetylchitobiosyl beta-N-acetylglucosaminidase F2
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DI-N-acetylchitobiosyl beta-N-acetylglucosaminidase F3
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endo-beta-(1->4)-N-acetylglucosaminidase
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endo-beta-acetylglucosaminidase
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endo-beta-N-acetylglucosaminidase
endo-beta-N-acetylglucosaminidase HS
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endo-N-acetyl-beta-D-glucosaminidase
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endo-N-acetyl-beta-glucosaminidase
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endoglycosidase F1
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endoglycosidase F2
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endoglycosidase F3
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endoglycosidase S
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Engase1p
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mannosyl-glycoprotein 1,4-N-acetamidodeoxy-beta-D-glycohydrolase
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Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase
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Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F1
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Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F2
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Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F3
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murein hydrolase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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PATHWAY SOURCE
PATHWAYS
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.
CAS REGISTRY NUMBER
COMMENTARY hide
37278-88-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(Man)6(GlcNAc)2Asn + H2O
(Man)6GlcNAc + GlcNAc-Asn
show the reaction diagram
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?
Asn(Man4GlcNAc4) + H2O
?
show the reaction diagram
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?
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
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?
calf fetuin + 4-nitrophenyl-beta-D-glucoside
?
show the reaction diagram
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transfer of triantennary complex type oligosaccharide, yield 3.4%
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?
glycopeptide + H2O
?
show the reaction diagram
glycoprotein + H2O
?
show the reaction diagram
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cleaves the N,N'-diacetylchitobiose moiety of the sugar chain of human salivary alpha-amylase family, human transferrin and calf fetuin
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?
hen egg glycopeptide + 4-nitrophenyl-beta-D-glucose
?
show the reaction diagram
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transfer of asparagine-linked oligosaccharide
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?
human alpha1-acid glycoprotein + 4-nitrophenyl-beta-D-glucose
?
show the reaction diagram
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transfer of bi-, tri- and tetraantennary complex type oligosaccharide, yield 1.7%
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?
ovalbumin + H2O
oligosaccharides + ?
show the reaction diagram
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?
transferrin + 4-nitrophenyl-alpha-D-galactoside
?
show the reaction diagram
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transfer of asialobiantennary complex type oligosaccharide of human native transferrin
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?
transferrin + 4-nitrophenyl-alpha-D-glucoside
?
show the reaction diagram
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transfer of asialobiantennary complex type oligosaccharide of human native transferrin
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?
transferrin + 4-nitrophenyl-beta-D-galactoside
?
show the reaction diagram
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transfer of asialobiantennary complex type oligosaccharide of human native transferrin
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?
transferrin + 4-nitrophenyl-beta-D-glucoside
?
show the reaction diagram
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transfer of asialobiantennary complex type oligosaccharide of human native transferrin with yield of 1.1%
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?
transferrin + 4-nitrophenyl-beta-D-mannoside
?
show the reaction diagram
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transfer of asialobiantennary complex type oligosaccharide of human native transferrin
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?
transferrin + 4-nitrophenyl-beta-D-xyloside
?
show the reaction diagram
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transfer of asialobiantennary complex type oligosaccharide of human native transferrin
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?
transferrin + 4-nitrophenyl-glycerol
?
show the reaction diagram
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transfer of asialobiantennary complex type oligosaccharide of human native transferrin
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?
transferrin + 4-nitrophenyl-N-acetyl-beta-D-glucosaminide
?
show the reaction diagram
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transfer of asialobiantennary complex type oligosaccharide of human native transferrin
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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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
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
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endo-beta-N-acetylglucosaminidase 2
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
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optimal activation at 10 mM
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
Homo sapiens
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pH 6.5, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 3.5
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endo-beta-N-acetylglucosaminidase 2
4.5
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endo-beta-N-acetylglucosaminidase 1
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 4.5
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about 70% of maximal activity at pH 2.5 and at pH 4.5, endo-beta-N-acetylglucosaminidase 2
4.5 - 7
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pH 4.5: about 60% of maximal activity, pH 7.0: about 50% of maximal activity, endo-beta-N-acetylglucosaminidase 1
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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epithelial cells peeling from the oral cavity epithelium into saliva
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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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
physiological function
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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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ENASE_HUMAN
743
0
83987
Swiss-Prot
Mitochondrion (Reliability: 2)
B4DVK0_HUMAN
220
0
24616
TrEMBL
other Location (Reliability: 2)
J9JID0_HUMAN
183
0
20518
TrEMBL
other Location (Reliability: 3)
F8W925_HUMAN
365
0
41471
TrEMBL
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
endo-beta-N-acetylglucosaminidase 1 and 2
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homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in COS-7 cells
expressed in Saccharomyces cerevisiae png1DELTA cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
DeGasperi, R.; Li, Y.T.; Li, S.C.
Presence of two endo-beta-N-acetylglucosaminidases in human kidney
J. Biol. Chem.
264
9329-9334
1989
Homo sapiens
Manually annotated by BRENDA team
Song, Z.; Li, S.C.; Li, Y.T.
Absence of endo-beta-N-acetylglucosaminidase activity in the kidneys of sheep, cattle and pig
Biochem. J.
248
145-149
1987
Homo sapiens, no activity in bovine, no activity in sheep
Manually annotated by BRENDA team
Overdijk, B.; van der Kroef, W.M.J.; Lisman, J.J.W.; Pierce, R.J.; Montreuil, J.; Spik, G.
Demonstration and partial characterization of endo-N-acetyl-beta-D-glucosaminidase in human tissues
FEBS Lett.
128
364-366
1981
Homo sapiens
Manually annotated by BRENDA team
Tachibana, Y.; Yamashita, K.; Kobata, A.
Substrate specificity of mammalian endo-beta-N-acetylglucosaminidase: study with the enzyme of rat liver
Arch. Biochem. Biophys.
214
199-210
1982
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Ito, K.; Okada, Y.; Ishida, K.; Minamiura, N.
Human salivary endo-beta-N-acetylglucosaminidase HS specific for complex type sugar chains of glycoproteins
J. Biol. Chem.
268
16074-16081
1993
Homo sapiens
Manually annotated by BRENDA team
Suzuki, T.; Yano, K.; Sugimoto, S.; Kitajima, K.; Lennarz, W.J.; Inoue, S.; Inoue, Y.; Emori, Y.
Endo-beta-N-acetylglucosaminidase, an enzyme involved in processing of free oligosaccharides in the cytosol
Proc. Natl. Acad. Sci. USA
99
9691-9696
2002
Homo sapiens (Q8NFI3), Homo sapiens
Manually annotated by BRENDA team
Ito, K.; Miyagawa, K.; Matsumoto, M.; Yabuno, S.; Kawakami, N.; Hamaguchi, T.; Iizuka, M.; Minamiura, N.
Evidence for the transglycosylation of complex type oligosaccharides of glycoproteins by endo-beta-N-acetylglucosaminidase HS
Arch. Biochem. Biophys.
454
89-99
2006
Homo sapiens
Manually annotated by BRENDA team
Li, B.; Takegawa, K.; Suzuki, T.; Yamamoto, K.; Wang, L.X.
Synthesis and inhibitory activity of oligosaccharide thiazolines as a class of mechanism-based inhibitors for endo-beta-N-acetylglucosaminidases
Bioorg. Med. Chem.
15
4670-4675
2008
Glutamicibacter protophormiae, Flavobacterium sp., Homo sapiens, Mucor hiemalis
Manually annotated by BRENDA team
Chantret, I.; Fasseu, M.; Zaoui, K.; Le Bizec, C.; Yaye, H.S.; Dupre, T.; Moore, S.E.
Identification of roles for peptide: N-glycanase and endo-beta-N-acetylglucosaminidase (Engase1p) during protein N-glycosylation in human HepG2 cells
PLoS ONE
5
e11734
2010
Homo sapiens
Manually annotated by BRENDA team