Information on EC 2.4.1.141 - N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.141
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RECOMMENDED NAME
GeneOntology No.
N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-diphosphodolichol = UDP + N,N'-diacetylchitobiosyl-diphosphodolichol
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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N-Glycan biosynthesis
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protein N-glycosylation (eukaryotic, high mannose)
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Various types of N-glycan biosynthesis
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dolichyl-diphosphooligosaccharide biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:N-acetyl-D-glucosaminyl-diphosphodolichol N-acetyl-D-glucosaminyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
75536-54-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
15-16 days old
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
var. radiata
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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during complex formation, Alg14 functions as a membrane anchor that recruits Alg13 to the cytosolic face of the endoplasmic reticulum as a result of interaction between their C-terminal regions. The N-terminal region of Alg14 is involved in mediating the interaction with Alg7
physiological function
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the Alg7p and Alg13p/Alg14p UDP-GlcNAc transferases together mediate the earliest steps of the N-linked glycosylation pathway
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-acetyl-D-glucosaminyl-diphosphodolichol + UDP-glucuronic acid
D-glucuronyl-1,4-N-acetyl-D-glucosaminyl-diphosphodolichol + UDP
show the reaction diagram
N-acetyl-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-D-glucosamine
diphosphodolichyl-N-acetyl-D-glucosaminyl-N-acetyl-D-glucosamine + UDP
show the reaction diagram
N-acetyl-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-D-glucosamine
N,N'-diacetylchitobiosyl-diphosphodolichol + UDP
show the reaction diagram
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?
N-acetyl-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-D-glucosamine
UDP + diphosphodolichyl-N-acetyl-D-glucosaminyl-N-acetyl-D-glucosamine
show the reaction diagram
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?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
N-acetyl-D-glucosaminyl-diphosphodolichol + UMP
show the reaction diagram
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-diphosphodolichol
UDP + N,N'-diacetylchitobiosyl-diphosphodolichol
show the reaction diagram
additional information
?
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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
N-acetyl-D-glucosaminyl-diphosphodolichol + UDP-glucuronic acid
D-glucuronyl-1,4-N-acetyl-D-glucosaminyl-diphosphodolichol + UDP
show the reaction diagram
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
N-acetyl-D-glucosaminyl-diphosphodolichol + UMP
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-fluoro N-acetylglucosamine
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Amphomycin
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partial inhibition
bacitracin
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diphosphodolichyl-N-acetyl-D-glucosaminyl-N-acetyl-D-glucosamine
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exogenously added, extensive inhibition in absence and presence of +mannosyl-phosphodolichol and showdomycin
Diumycin
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Mg2+
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concentrations above 6.7 mM
N-acetyl-D-glucosaminyl-diphosphodolichol
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exogenously added, in presence of mannosyl-phosphodolichol
P1-dolichyl P2-(2-deoxy-2-fluoro-alpha-D-glucopyranosyl) diphosphate
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inhibitors when studied in competition with N-acetyl-D-glucosaminyl-diphosphodolichol
P1-dolichyl P2-(2-deoxy-2-trifluoroacetamido-alpha-D-glucopyranosyl) diphosphate
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inhibitors when studied in competition with N-acetyl-D-glucosaminyl-diphosphodolichol
P1-dolichyl P2-(2-O-ethyl-alpha-D-glucopyranosyl) diphosphate
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inhibitors when studied in competition with N-acetyl-D-glucosaminyl-diphosphodolichol
Showdomycin
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complete inhibition
UDPglucose
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Alg14
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Alg13 is active only in the presence of a binding partner Alg14
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mannosyl-phosphodolichol
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Triton X-100
TX-100
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0.15%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0002 - 0.00264
N-acetyl-D-glucosaminyl-diphosphodolichol
0.00025 - 0.392
UDP-N-acetyl-D-glucosamine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0028
diphosphodolichyl-N-acetyl-D-glucosaminyl-N-acetyl-D-glucosamine
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0.0044
N-acetyl-D-glucosaminyl-diphosphodolichol
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.25
5-fluoro N-acetylglucosamine
Cricetulus griseus
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 7.6
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Alg13p protein localizes both to the membrane and cytosol
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22600
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1 * 22600 + 1 * 27000, predicted molecular weights of subunits Alg13p and Alg14p, Alg13p is the soluble, cytosolic subunit that contains the catalytic domain, Alg14p is the membrane-spanning subunit that is required to recruit Alg13p to the cytosolic face of the endoplasmic reticulum
23000
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1 * 23000 + 1 * 30000, molecular weights of subunits Alg13p and Alg14p, gel filtration
27000
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1 * 22600 + 1 * 27000, predicted molecular weights of subunits Alg13p and Alg14p, Alg13p is the soluble, cytosolic subunit that contains the catalytic domain, Alg14p is the membrane-spanning subunit that is required to recruit Alg13p to the cytosolic face of the endoplasmic reticulum
30000
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1 * 23000 + 1 * 30000, molecular weights of subunits Alg13p and Alg14p, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
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1 * 22600 + 1 * 27000, predicted molecular weights of subunits Alg13p and Alg14p, Alg13p is the soluble, cytosolic subunit that contains the catalytic domain, Alg14p is the membrane-spanning subunit that is required to recruit Alg13p to the cytosolic face of the endoplasmic reticulum; 1 * 23000 + 1 * 30000, molecular weights of subunits Alg13p and Alg14p, gel filtration
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
cytosolic Alg13p is very short-lived, whereas membrane-associated Alg13 is relatively stable. Cytosolic Alg13p is a target for proteasomal degradation, and the failure to degrade excess Alg13p leads to glycosylation defects. Alg13p degradation requires a C-terminal domain whose deletion results in Alg13p stability. Appending this sequence onto normally long-lived beta-galactosidase causes it to undergo rapid degradation, demonstrating that this C-terminal domain represents a novel and autonomous degradation motif. Proteasomal degradation of excess unassembled Alg13p is an important quality control mechanism that ensures proper protein complex assembly and correct N-linked glycosylation
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Triton X-100
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the Alg13p/Alg14p complex remains stable in the presence of 0.1% Triton X-100
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20ºC, 0.5 mM DTT, pH 7.2, 20% glycerol, 10% loss of activity after 1 month
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-80ºC, 30% glycerol, several months
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4ºC, Tris-buffered saline, pH 7.4, 48 hs
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
solubilized enzyme purified on DE-52 column
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae strain XGY151
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expression in Escherichia coli
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Show AA Sequence (647 entries)
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