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Information on EC 2.4.1.141 - N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P53178

for references in articles please use BRENDA:EC2.4.1.141
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Saccharomyces cerevisiae
UNIPROT: P53178 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
alg13, alg14, alg13p, udp-glcnac transferase, udp-glcnac:glcnac-p-p-dol n-acetylglucosaminyltransferase, alg13p/alg14p, alg 14, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Alg13p
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the catalytic subunit of the endoplasmic reticulum UDP-GlcNAc glycosyltransferase
Alg14
N,N'-diacetylchitobiosylpyrophosphoryldolichol synthase
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UDP-GlcNAc:dolichyl-pyrophosphoryl-GlcNAc GlcNAc transferase
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uridine diphosphoacetylglucosamine-dolichylacetylglucosamine pyrophosphate acetylglucosaminyltransferase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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-
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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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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 + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
show the reaction diagram
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-alpha-D-glucosamine + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
show the reaction diagram
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
UDP-N-acetyl-alpha-D-glucosamine + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
show the reaction diagram
second step in the biosynthesis of the unique lipid-linked core oligosaccharide
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-
?
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-alpha-D-glucosamine + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
show the reaction diagram
second step in the biosynthesis of the unique lipid-linked core oligosaccharide
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-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Alg14
Alg13 is active only in the presence of a binding partner Alg14
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Alg13p protein localizes both to the membrane and cytosol
Manually annotated by BRENDA team
Alg13p protein localizes both to the membrane and cytosol
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bickel, T.; Lehle, L.; Schwarz, M.; Aebi, M.; Jakob, C.A.
Biosynthesis of Lipid-linked Oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc2-PP-dolichol
J. Biol. Chem.
280
34500-34506
2005
Saccharomyces cerevisiae (P38242), Saccharomyces cerevisiae (P53178), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Gao, X.; Tachikawa, H.; Sato, T.; Jigami, Y.; Dean, N.
Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation
J. Biol. Chem.
280
36254-36262
2005
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Gao, X.D.; Moriyama, S.; Miura, N.; Dean, N.; Nishimura, S.I.
Interaction between the C-termini of Alg13 and Alg14 mediate formation of the active UDP-N-acetylglucosamine transferase complex
J. Biol. Chem.
283
32534-32541
2008
Saccharomyces cerevisiae (P53178), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Averbeck, N.; Gao, X.D.; Nishimura, S.; Dean, N.
Alg13p, the catalytic subunit of the endoplasmic reticulum UDP-GlcNAc glycosyltransferase, is a target for proteasomal degradation
Mol. Biol. Cell
19
2169-2178
2008
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Wang, X.; Weldeghiorghis, T.; Zhang, G.; Imperiali, B.; Prestegard, J.H.
Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase
Structure
16
965-975
2008
Saccharomyces cerevisiae (P53178), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Lu, J.; Takahashi, T.; Ohoka, A.; Nakajima, K.; Hashimoto, R.; Miura, N.; Tachikawa, H.; Gao, X.D.
Alg14 organizes the formation of a multiglycosyltransferase complex involved in initiation of lipid-linked oligosaccharide biosynthesis
Glycobiology
22
504-516
2012
Saccharomyces cerevisiae
Manually annotated by BRENDA team