Information on EC 2.4.1.94 - protein N-acetylglucosaminyltransferase

for references in articles please use BRENDA:EC2.4.1.94
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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
2.4.1.94
-
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RECOMMENDED NAME
GeneOntology No.
protein N-acetylglucosaminyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-D-glucosamine + [protein]-L-asparagine = UDP + [protein]-N4-(N-acetyl-D-glucosaminyl)-L-asparagine
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:[protein]-L-asparagine beta-N-acetyl-D-glucosaminyl-transferase
The acceptor is the asparagine residue in a sequence of the form Asn-Xaa-Thr or Asn-Xaa-Ser.
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CAS REGISTRY NUMBER
COMMENTARY hide
72319-34-7
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
mutant 2180-1A-5mnn2
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-
Manually annotated by BRENDA team
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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
UDP-N-acetyl-alpha-D-glucosamine + pancreatic ribonuclease A
UDP + pancreatic ribonuclease A with N-acetylglucosamine linked to Asp
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + protein
UDP + 4-N-(N-acetyl-D-glucosaminyl)-protein
show the reaction diagram
UDP-N-acetylglucosamine + pancreatic ribonuclease A
UDP + pancreatic ribonuclease A with N-acetylglucosamine linked to Asp-34
show the reaction diagram
additional information
?
-
-
catalyses the glycosylation in vitro of the asparagine residue present in the sequence Asn, Leu, Thr
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
catalyses the glycosylation in vitro of the asparagine residue present in the sequence Asn, Leu, Thr
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
activation
Ni2+
-
slight activation
additional information
-
Mg2+ is ineffective
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Triton X-100
-
at 0.1% and 0.2% concentrations has no effect, at a concentration of 1%, there is a 47% inhibition of enzyme activity
UDP
-
at concentrations of UDP of 0.02, 0.10, and 0.2 mM, the glycosylation of ribonuclease A is inhibited to the extent of 2,15, and 27%, respectively
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CDP-choline
-
activator, 2.4 mM
spermidine
-
most effective activator, 10-15 mM
spermine
-
activator
Triton X-100
-
1.7fold at 0.04%
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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LINKS TO OTHER DATABASES (specific for EC-Number 2.4.1.94)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)