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Information on EC 3.2.1.96 - mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase and Organism(s) Streptomyces plicatus and UniProt Accession P04067
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3.2.1.96 mannosyl-glycoprotein endo-beta-N-acetylglucosaminidaseIUBMB Comments
A group of related enzymes.
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Word Map
- 3.2.1.96
- oligosaccharide
-
n-linked
- lysosomal
-
high-mannose
-
deglycosylation
- n-acetylglucosamine
- glycopeptides
- beta-glucuronidase
-
analbuminemic
- n-glycans
- alpha-mannosidase
- glycosidases
-
concanavalin
-
asparagine-linked
- tunicamycin
- mastitis
-
complex-type
- neuraminidase
-
pngase
-
exoglycosidases
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transglycosylation
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sialylated
- autolysins
- phytolacca
-
oxazoline
- swainsonine
- mucor
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3.2.1.30
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mannose-type
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h-sensitive
- alpha-fucosidase
-
udder
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biantennary
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high-mannose-type
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3hmannose
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hybrid-type
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intramammary
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h-resistant
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chitinolytic
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lipid-linked
- 1-deoxymannojirimycin
- beta-n-acetyl-d-glucosaminidase
- glcnac2
- man8glcnac2
- synthesis
- nutrition
-
tetraantennary
- meningosepticum
- chitobiose
-
oligomannosidic
- analysis
-
holins
- medicine
- glc3man9glcnac2
- food industry
The taxonomic range for the selected organisms is: Streptomyces plicatus
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylglucosaminidase, endo-beta
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di-N-acetylchitobiosyl beta-N-acetylglucosaminidase
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-
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DI-N-acetylchitobiosyl beta-N-acetylglucosaminidase F1
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-
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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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-
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endo-beta-acetylglucosaminidase
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endo-beta-N-acetylglucosaminidase
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endo-N-acetyl-beta-D-glucosaminidase
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-
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endo-N-acetyl-beta-glucosaminidase
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-
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endoglycosidase F1
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-
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endoglycosidase F2
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-
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endoglycosidase F3
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-
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endoglycosidase S
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mannosyl-glycoprotein 1,4-N-acetamidodeoxy-beta-D-glycohydrolase
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-
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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
LITERATURE
hydrolysis of O-glycosyl bond
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-
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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
37278-88-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ribonuclease B + H2O
?
the enzyme catalyzes cleavage between the GlcNAc residues of the chitobiose core of N-linked glycans, leaving one GlcNAc residues attached to asparagine. Endo H cleaves high mannose and hybrid, but not complex, N-linked oligosaccharides on glycoproteins
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-
?
Asn(GlcNAc)2-(Man)6(GlcNAc)2 + H2O
AsnGlcNAc + (GlcNAC)1-(Man)6(GlcNAc)2
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-
-
?
beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-Asn
beta-D-Man-(1->4)-beta-D-GlcNAc + beta-D-GlcNAc-Asn
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-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
2 N,N'-diacetylchitobiose
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-
-
?
N,N',N''-triacetylchitotriose + H2O
N-acetyl-D-glucosamine + N,N'-diacetylchiotobiose
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-
-
?
N-glycosylated RNase B + H2O
?
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the enzyme cleaves within the chitobiose core of high-mannose oligosaccharides from RNase B
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-
?
N4-(beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-N2-dansyl-L-Asn + H2O
beta-D-Man-(1->4)-beta-D-GlcNAc + N4-(beta-D-GlcNAc)-N2-dansyl-L-Asn
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-
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-
?
additional information
?
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no hydrolysis of dansyl-Asn(GlcNAc)2Man, the presence of fucose attached to the asparagine-proximal core glucosamine renders the di-N-acetylchitobiosyl moiety an inactive substrate. As the number of mannose residues is increased, the rate of hydrolysis increases to a maximum at five residues. Thereafter enzyme activity declines, but the rate is still substantial on mannosyl chains containing 54 residues
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-
?
additional information
?
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the enzyme is probably devoted to exogeneous functions, such as degrading macromolecules for feeding purposes
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?
additional information
?
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the enzyme cleaves high-mannose and hybrid-type N-glycans between the first two GlcNAc residues at the reducing end
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?
additional information
?
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the enzyme hydrolyzes GlcNAcbeta1->4GlcNAc linkage of high mannose and hybrid type glycans and cannot cleave the linkage of complex type glycans
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme is probably devoted to exogeneous functions, such as degrading macromolecules for feeding purposes
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 4.5
5 - 6
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 7
-
the enzymatic activity of the recombinant enzyme is retained at pH 4.0-7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27 - 47
-
the enzymatic activity of the recombinant enzyme is retained at 27-47°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
recombinant enzyme produced in Escherichia coli appears both in the periplasmic space and in the cell
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recombinant enzyme produced in Escherichia coli appears both in the periplasmic space and in the cell
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
LITERATURE
wild-type enzyme and mutant enzymes D130N, D130E, D130A, E132Q, E132A, and D130N/E132Q
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D130
-
1.25-3.14% of the activity of the wild-type enzyme, depending on assay method
D130N
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0.1-0.21% of the activity of the wild-type enzyme, depending on assay method
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8.5
-
37°C, stable between pH 4.5 and pH 8.5, rapid loss of activity below pH 4.5
171686
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
pH 4.5-8.5, protein concentration 0.0003 mg/ml, stable. Rapid loss of activity below pH 4.5
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
20-30% loss of initial activity is lost when the protein concentration is decreased to less than 0.02-0.03 mg/ml
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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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the non-secreted form of Endo H without a signal peptide is expressed and purified from silkworm fat body
nickel affinity column chromatography and StrepTrap column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
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essential reagent for the investigation of the structure and functions of glycoproteins
analysis
-
commonly used reagent in glycobiology research, including the characterization of oligosaccharides in glycoproteins
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Trimble, R.B.; Trumbly, R.J.; Maley, F.
endo-beta-N-Acetylglucosaminidase H from Streptomyces plicatus
Methods Enzymol.
138
763-770
1987
Streptomyces plicatus
Tarentino, A.L.; Trimble, R.B.; Maley, F.
endo-beta-N-Acetylglucosaminidase from Streptomyces plicatus
Methods Enzymol.
50C
574-580
1978
Streptomyces plicatus
Robbins, P.W.; Trimble, R.B.; Wirth, D.F.; Hering, C.; Maley, F.; Maley, G.F.; Das, R.; Gibson, B.W.; Royal, N.; Biemann, K.
Primary structure of the Streptomyces enzyme endo-beta-N-acetylglucosaminidase H
J. Biol. Chem.
259
7577-7583
1984
Streptomyces plicatus
Trimble, R.B.; Tarentino, A.L.; Evans, G.; Maley, F.
Purification and properties of endo-beta-N-acetylglucosaminidase L from Streptomyces plicatus
J. Biol. Chem.
254
9708-9713
1979
Streptomyces plicatus
Rao, V.; Cui, T.; Guan, C.; van Roey, P.
Mutations of endo-beta-N-acetylglucosaminidase H active site residues Asp130 and Glu132: activities and conformations
Protein Sci.
8
2338-2346
1999
Streptomyces plicatus
Karamanos, Y.; Bourgerie, S.; Barreaud, J.P.; Julien, R.
Are there biological functions for bacterial endo-N-acetyl-beta-D-glucosaminidases?
Res. Microbiol.
146
437-443
1995
Acinetobacter sp., Glutamicibacter protophormiae, Paenibacillus alvei, Elizabethkingia meningoseptica, Clostridium perfringens, Streptococcus pneumoniae, Flavobacterium sp., Myxococcus xanthus, Pseudomonas sp., Stigmatella aurantiaca, Streptomyces plicatus
Rao, V.; Guan, C.; van Roey, P.
Crystal structure of endo-beta-N-acetylglucosaminidase H at 1.9 A resolution: active-site geometry and substrate recognition
Structure
3
449-457
1995
Streptomyces plicatus
Frisch, E.; Schwedler, C.; Kaup, M.; Iona Braicu, E.; Groene, J.; Lauscher, J.C.; Sehouli, J.; Zimmermann, M.; Tauber, R.; Berger, M.; Blanchard, V.
Endo-beta-N-acetylglucosaminidase H de-N-glycosylation in a domestic microwave oven: application to biomarker discovery
Anal. Biochem.
433
65-69
2013
Streptomyces plicatus
Mitsudome, T.; Xu, J.; Nagata, Y.; Masuda, A.; Iiyama, K.; Morokuma, D.; Li, Z.; Mon, H.; Lee, J.M.; Kusakabe, T.
Expression, purification, and characterization of endo-beta-N-acetylglucosaminidase H using baculovirus-mediated silkworm protein expression system
Appl. Biochem. Biotechnol.
172
3978-3988
2014
Streptomyces plicatus
Masuda, A.; Xu, J.; Mitsudome, T.; Morokuma, D.; Mon, H.; Banno, Y.; Kusakabe, T.; Lee, J.
Improvement of endo-beta-N-acetylglucosaminidase H production using silkworm-baculovirus protein expression system
J. Asia Pac. Entomol.
18
175-180
2015
Streptomyces plicatus (P04067)
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EXTERNAL LINKS (specific for EC-Number 3.2.1.96)
Transporter Classification Database (TCDB): 1.C.105.2.7, 1.C.105.2.6
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