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

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IUBMB Comments
A group of related enzymes.
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This record set is specific for:
UNIPROT: Q93HW0
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Word Map
The enzyme appears in 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
CBM32
family 32 carbohydrate-binding module of endo-beta-1,4-N-acetylglucosamidase EndoD
endo-beta-1,4-N-acetylglucosamidase
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endo-beta-N-acetylglucosaminidase
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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
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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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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)5(GlcNAc)2-Asn + H2O
?
show the reaction diagram
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?
Man3GlcNAc-oxazoline + Fmoc-Asn(Fucalpha(1->6)GlcNAc)-OH
?
show the reaction diagram
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?
Man3GlcNAc-oxazoline + Fmoc-Asn(GlcNAc)-OH
?
show the reaction diagram
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?
N-glycosylated immunglobuline G + H2O
?
show the reaction diagram
the enzyme prefers core-fucosylated N-glycan for hydrolysis
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?
additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.51 - 18.51
Fmoc-Asn(Fucalpha(1->6)GlcNAc)-OH
0.73 - 5.22
Fmoc-Asn(GlcNAc)-OH
0.5 - 0.67
Man3GlcNAc-oxazoline
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.24 - 14.32
Fmoc-Asn(Fucalpha(1->6)GlcNAc)-OH
0.5 - 6.37
Fmoc-Asn(GlcNAc)-OH
0.21 - 10.17
Man3GlcNAc-oxazoline
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0286 - 0.77
Fmoc-Asn(Fucalpha(1->6)GlcNAc)-OH
0.096 - 8.7
Fmoc-Asn(GlcNAc)-OH
0.31 - 20.4
Man3GlcNAc-oxazoline
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q93HW0_STREE
1646
0
182122
TrEMBL
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
x * 100000, SDS-PAGE
102000
x * 102000, calculated from amino acid sequence
183200
x * 183200, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H371W
the mutant shows increased hydrolytic activity compared to the wild type
N322A
N322Q
the mutant demonstrates remarkable transglycosylation activity with only marginal hydrolysis activity, having much higher catalytic efficiency for glycosylating the nonfucosylated GlcNAc acceptor
Y360F
the mutant shows slightly reduced hydrolytic activity compared to the wild type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+-affinity resin column chromatography and Sephacryl S-200 gel filtration
Ni2+-immobilized HisTrap column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli B834 (DE3) cells
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Muramatsu, H.; Tachikui, H.; Ushida, H.; Song, X.J.; Qiu, Y.; Yamamoto, S.; Muramatsu, T.
Molecular cloning and expression of endo-beta-N-acetylglucosaminidase D, which acts on the core structure of complex type asparagine-linked oligosaccharides
J. Biochem.
129
923-928
2001
Streptococcus pneumoniae (Q93HW0), Streptococcus pneumoniae
Manually annotated by BRENDA team
Abbott, D.W.; Boraston, A.
Structural analysis of a putative family 32 carbohydrate-binding module from the Streptococcus pneumoniae enzyme EndoD
Acta Crystallogr. Sect. F
67
429-433
2011
Streptococcus pneumoniae (Q93HW0), Streptococcus pneumoniae
Manually annotated by BRENDA team
Fan, S.; Huang, W.; Wang, L.
Remarkable transglycosylation activity of glycosynthase mutants of Endo-D, an endo-beta-N-acetylglucosaminidase from Streptococcus pneumoniae
J. Biol. Chem.
287
11272-11281
2012
Streptococcus pneumoniae (Q93HW0)
Manually annotated by BRENDA team