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Information on EC 2.4.1.141 - N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase
for references in articles please use BRENDA:EC2.4.1.141
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.141 N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
showSynonyms
alg13, alg14, alg13p, udp-glcnac transferase, alg13p/alg14p, alg 14, udp-glcnac:glcnac-p-p-dol n-acetylglucosaminyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Alg13
Alg13p
-
the catalytic subunit of the endoplasmic reticulum UDP-GlcNAc glycosyltransferase
Alg14
inverting beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol glycosyltransferase
-
N,N'-diacetylchitobiosylpyrophosphoryldolichol synthase
-
-
-
-
UDP-GlcNAc:dolichyl-pyrophosphoryl-GlcNAc GlcNAc transferase
-
-
-
-
uridine diphosphoacetylglucosamine-dolichylacetylglucosamine pyrophosphate acetylglucosaminyltransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
protein N-glycosylation initial phase (eukaryotic)
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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
75536-54-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-acetyl-D-glucosaminyl-diphosphodolichol + UDP-glucuronic acid
D-glucuronyl-1,4-N-acetyl-D-glucosaminyl-diphosphodolichol + UDP
UDP-N-acetyl-alpha-D-glucosamine + acceptor1
UDP + product1
Substrates: -
Products: -
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UDP-N-acetyl-alpha-D-glucosamine + acceptor2
UDP + product2
Substrates: -
Products: -
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UDP-N-acetyl-alpha-D-glucosamine + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
UDP + N,N'-diacetylchitobiosyl-diphosphodolichol
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
N-acetyl-D-glucosaminyl-diphosphodolichol + UDP-glucuronic acid
D-glucuronyl-1,4-N-acetyl-D-glucosaminyl-diphosphodolichol + UDP
-
Substrates: -
Products: -
Products: -
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N-acetyl-D-glucosaminyl-diphosphodolichol + UDP-glucuronic acid
D-glucuronyl-1,4-N-acetyl-D-glucosaminyl-diphosphodolichol + UDP
-
Substrates: -
Products: -
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N-acetyl-D-glucosaminyl-diphosphodolichol + UDP-glucuronic acid
D-glucuronyl-1,4-N-acetyl-D-glucosaminyl-diphosphodolichol + UDP
-
Substrates: -
Products: -
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UDP-N-acetyl-alpha-D-glucosamine + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
UDP + N,N'-diacetylchitobiosyl-diphosphodolichol
-
Substrates: -
Products: -
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UDP-N-acetyl-alpha-D-glucosamine + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
UDP + N,N'-diacetylchitobiosyl-diphosphodolichol
-
Substrates: -
Products: -
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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
-
Substrates: -
Products: -
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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
Substrates: second step in the biosynthesis of the unique lipid-linked core oligosaccharide
Products: -
Products: -
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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
Substrates: -
Products: -
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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
-
Substrates: -
Products: -
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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
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Substrates: -
Products: -
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?
additional information
?
-
-
Substrates: 5-fluoro N-acetylglucosamine is completely inactive as a glycosyl donor
Products: -
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?
additional information
?
-
Substrates: a short C-terminal alpha helix of Alg13 is required for interaction with Alg14 and for enzyme activity. The C-terminal three amino acids of Alg14 are required for maintaining the integrity of Alg13/Alg14 complex. They are involved in the stabilization of the interaction between the C-termini of Alg13 and Alg14. Deletion of the N-terminal alpha strand of Alg13 causes the destruction of protein, indicating the structural importance of this region in protein stability
Products: -
Products: -
?
additional information
?
-
-
Substrates: a short C-terminal alpha helix of Alg13 is required for interaction with Alg14 and for enzyme activity. The C-terminal three amino acids of Alg14 are required for maintaining the integrity of Alg13/Alg14 complex. They are involved in the stabilization of the interaction between the C-termini of Alg13 and Alg14. Deletion of the N-terminal alpha strand of Alg13 causes the destruction of protein, indicating the structural importance of this region in protein stability
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-acetyl-D-glucosaminyl-diphosphodolichol + UDP-glucuronic acid
D-glucuronyl-1,4-N-acetyl-D-glucosaminyl-diphosphodolichol + UDP
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
Substrates: second step in the biosynthesis of the unique lipid-linked core oligosaccharide
Products: -
Products: -
?
N-acetyl-D-glucosaminyl-diphosphodolichol + UDP-glucuronic acid
D-glucuronyl-1,4-N-acetyl-D-glucosaminyl-diphosphodolichol + UDP
-
Substrates: -
Products: -
Products: -
?
N-acetyl-D-glucosaminyl-diphosphodolichol + UDP-glucuronic acid
D-glucuronyl-1,4-N-acetyl-D-glucosaminyl-diphosphodolichol + UDP
-
Substrates: -
Products: -
Products: -
?
N-acetyl-D-glucosaminyl-diphosphodolichol + UDP-glucuronic acid
D-glucuronyl-1,4-N-acetyl-D-glucosaminyl-diphosphodolichol + UDP
-
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diphosphodolichyl-N-acetyl-D-glucosaminyl-N-acetyl-D-glucosamine
-
exogenously added, extensive inhibition in absence and presence of +mannosyl-phosphodolichol and showdomycin
N-acetyl-D-glucosaminyl-diphosphodolichol
-
exogenously added, in presence of mannosyl-phosphodolichol
P1-dolichyl P2-(2-deoxy-2-fluoro-alpha-D-glucopyranosyl) diphosphate
-
inhibitors when studied in competition with N-acetyl-D-glucosaminyl-diphosphodolichol
P1-dolichyl P2-(2-deoxy-2-trifluoroacetamido-alpha-D-glucopyranosyl) diphosphate
-
inhibitors when studied in competition with N-acetyl-D-glucosaminyl-diphosphodolichol
P1-dolichyl P2-(2-O-ethyl-alpha-D-glucopyranosyl) diphosphate
-
inhibitors when studied in competition with N-acetyl-D-glucosaminyl-diphosphodolichol
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Alg14
Alg13 is active only in the presence of a binding partner Alg14
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Distinct expression and prognostic value of OTU domain-containing proteins in non-small-cell lung cancer.
Brain Diseases
ALG13 X-linked intellectual disability: New variants, glycosylation analysis, and expanded phenotypes.
Brain Diseases
ALG13-CDG with Infantile Spasms in a Male Patient Due to a De Novo ALG13 Gene Mutation.
Brain Diseases
Exome sequence identified a c.320A > G ALG13 variant in a female with infantile epileptic encephalopathy with normal glycosylation and random X inactivation: Review of the literature.
Brain Diseases
High prevalence of genetic alterations in early-onset epileptic encephalopathies associated with infantile movement disorders.
Brain Diseases
Predominant and novel de novo variants in 29 individuals with ALG13 deficiency: Clinical description, biomarker status, biochemical analysis, and treatment suggestions.
Brain Diseases
The First Metabolome Analysis in Children with Epilepsy and ALG13-CDG Resulting from c.320A>G Variant.
Carcinoma
Distinct expression and prognostic value of OTU domain-containing proteins in non-small-cell lung cancer.
Carcinoma, Squamous Cell
Distinct expression and prognostic value of OTU domain-containing proteins in non-small-cell lung cancer.
Congenital Disorders of Glycosylation
ALG13 participates in epileptogenesis via regulation of GABAA receptors in mouse models.
Congenital Disorders of Glycosylation
Early and lethal neurodegeneration with myasthenic and myopathic features: A new ALG14-CDG.
Congenital Disorders of Glycosylation
X chromosome exome sequencing reveals a novel ALG13 mutation in a nonsyndromic intellectual disability family with multiple affected male siblings.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
ALG13 participates in epileptogenesis via regulation of GABAA receptors in mouse models.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
ALG13 X-linked intellectual disability: New variants, glycosylation analysis, and expanded phenotypes.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Early and lethal neurodegeneration with myasthenic and myopathic features: A new ALG14-CDG.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Girls with Seizures Due to the c.320A>G Variant in ALG13 Do Not Show Abnormal Glycosylation Pattern on Standard Testing.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Predominant and novel de novo variants in 29 individuals with ALG13 deficiency: Clinical description, biomarker status, biochemical analysis, and treatment suggestions.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
X chromosome exome sequencing reveals a novel ALG13 mutation in a nonsyndromic intellectual disability family with multiple affected male siblings.
Epilepsy
A novel ALG14 missense variant in an alive child with myopathy, epilepsy, and progressive cerebral atrophy.
Epilepsy
ALG13 participates in epileptogenesis via regulation of GABAA receptors in mouse models.
Epilepsy
Genomic screening in rare disorders: New mutations and phenotypes, highlighting ALG14 as a novel cause of severe intellectual disability.
Genetic Diseases, Inborn
ALG13 participates in epileptogenesis via regulation of GABAA receptors in mouse models.
Intellectual Disability
ALG13 X-linked intellectual disability: New variants, glycosylation analysis, and expanded phenotypes.
Intellectual Disability
Genomic screening in rare disorders: New mutations and phenotypes, highlighting ALG14 as a novel cause of severe intellectual disability.
Intellectual Disability
X chromosome exome sequencing reveals a novel ALG13 mutation in a nonsyndromic intellectual disability family with multiple affected male siblings.
Muscular Diseases
A novel ALG14 missense variant in an alive child with myopathy, epilepsy, and progressive cerebral atrophy.
Myasthenic Syndromes, Congenital
Congenital myasthenic syndromes due to mutations in ALG2 and ALG14.
Myasthenic Syndromes, Congenital
Trouble at the junction: When myopathy and myasthenia overlap.
n-acetylglucosaminyldiphosphodolichol n-acetylglucosaminyltransferase deficiency
ALG13 Deficiency Associated with Increased Seizure Susceptibility and Severity.
n-acetylglucosaminyldiphosphodolichol n-acetylglucosaminyltransferase deficiency
Predominant and novel de novo variants in 29 individuals with ALG13 deficiency: Clinical description, biomarker status, biochemical analysis, and treatment suggestions.
Neoplasms
Genomic Fabric Remodeling in Metastatic Clear Cell Renal Cell Carcinoma (ccRCC): A New Paradigm and Proposal for a Personalized Gene Therapy Approach.
Neoplasms
Phenotypic and genotypic features of a large kindred with a germline AIP variant.
Seizures
ALG13-CDG in a male with seizures, normal cognitive development, and normal transferrin isoelectric focusing.
Seizures
Girls with Seizures Due to the c.320A>G Variant in ALG13 Do Not Show Abnormal Glycosylation Pattern on Standard Testing.
Spasms, Infantile
ALG13 X-linked intellectual disability: New variants, glycosylation analysis, and expanded phenotypes.
Spasms, Infantile
ALG13-CDG with Infantile Spasms in a Male Patient Due to a De Novo ALG13 Gene Mutation.
Spasms, Infantile
High prevalence of genetic alterations in early-onset epileptic encephalopathies associated with infantile movement disorders.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Alg13p protein localizes both to the membrane and cytosol
brenda
-
localized on the cytosolic face of the endoplasmic reticulum
brenda
-
Alg 14 protein functions as a membrane anchor that recruits Alg 13 protein to the cytosolic face of the endoplasmic reticulum, where catalysis of GlcNAc2-PP-dol occurs. Alg 13 protein and Alg 14 protein physically interact and under normal conditions, are associated with the membrane of the endoplasmic reticulum
brenda
-
cytosolic Alg13p is very short-lived, whereas membrane-associated Alg13 is relatively stable
brenda
Alg13p protein localizes both to the membrane and cytosol
brenda
Alg14p protein is exclusively membrane-bound
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
bioinformatics and structural modeling reveal similarities of Agl24 to the eukaryotic Alg14/13 and a distant relation to the bacterial MurG, which are catalyzing the same or a similar reaction, respectively. Phylogenetic analysis of Alg14/13 homologs indicates that they are ancient in Eukaryotes, either as a lateral transfer or inherited through eukaryogenesis
metabolism
-
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
physiological function
-
the Alg7p and Alg13p/Alg14p UDP-GlcNAc transferases together mediate the earliest steps of the N-linked glycosylation pathway
physiological function
Agl24 is a key player in the N-glycosylation pathway. The enzyme is responsible for the synthesis of the N-glycan chitobiose core
Show AA Sequence and Transmembrane Helices (3621 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22600
-
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
-
1 * 23000 + 1 * 30000, molecular weights of subunits Alg13p and Alg14p, gel filtration
27000
-
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
-
1 * 23000 + 1 * 30000, molecular weights of subunits Alg13p and Alg14p, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
additional information
heterodimer
-
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
heterodimer
-
1 * 23000 + 1 * 30000, molecular weights of subunits Alg13p and Alg14p, gel filtration
additional information
Alg13p associates with Alg14p to a complex forming the active transferase catalyzing the biosynthesis of GlcNAc2-PP-Dol
additional information
Alg13p associates with Alg14p to a complex forming the active transferase catalyzing the biosynthesis of GlcNAc2-PP-Dol
additional information
-
Alg13p associates with Alg14p to a complex forming the active transferase catalyzing the biosynthesis of GlcNAc2-PP-Dol
additional information
-
Alg 14 protein functions as a membrane anchor that recruits Alg 13 protein to the cytosolic face of the ER, where catalysis of GlcNAc2-PP-dol occurs. Alg 13 protein and Alg 14 protein physically interact and under normal conditions, are associated with the membrane of the endoplasmic reticulum
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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
LITERATURE
Triton X-100
-
the Alg13p/Alg14p complex remains stable in the presence of 0.1% Triton X-100
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Turco, S.J.; Heath, E.C.
Glucuronosyl-N-acetylglucosaminyl pyrophosphoryldolichol. Formation in SV40-transformed human lung fibroblasts and biosynthesis in rat lung microsomal preparations
J. Biol. Chem.
252
2918-2928
1977
Homo sapiens, Rattus norvegicus
brenda
Kaushal, G.P.; Elbein, A.D.
Purification and properties of UDP-GlcNAc:dolichyl-pyrophosphoryl-GlcNAc transferase from mung bean seedling
Plant Physiol.
81
1086-1091
1986
Vigna radiata
brenda
McLachlan, K.R.; Krag, S.S.
Three enzymes involved in oligosaccharide-lipid assembly in chinese hamster ovary cells differ in lipid substrate preference
J. Lipid Res.
35
1861-1868
1994
Cricetulus griseus
brenda
Kean, E.L.; Niu, N.
Kinetics of formation of GlcNAc-GlcNAc-P-P-dolichol by microsomes from the retina of the embryonic chick
Glycoconjugate J.
15
11-17
1998
Gallus gallus
brenda
Kean, E.L.; Wei, Z.; Anderson, V.E.; Zhang, N.; Sayre, L.M.
Regulation of the biosynthesis of N-acetylglucosaminylpyrophosphoryldolichol, feedback and product inhibition
J. Biol. Chem.
274
34072-34082
1999
Gallus gallus
brenda
Tai, V.W.F.; O'Reilly, M.K.; Imperiali, B.
Substrate specificity of N-acetylglucosaminyl(diphosphodolichol) N-acetylglucosaminyl transferase, a key enzyme in the dolichol pathway
Bioorg. Med. Chem.
9
1133-1140
2001
Sus scrofa
brenda
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 (P53178), Saccharomyces cerevisiae (P38242), Saccharomyces cerevisiae
brenda
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
brenda
Hartman, M.C.; Jiang, S.; Rush, J.S.; Waechter, C.J.; Coward, J.K.
Glycosyltransferase mechanisms: impact of a 5-fluoro substituent in acceptor and donor substrates on catalysis
Biochemistry
46
11630-11638
2007
Cricetulus griseus
brenda
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
brenda
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
brenda
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
brenda
Noffz, C.; Keppler-Ross, S.; Dean, N.
Hetero-oligomeric interactions between early glycosyltransferases of the dolichol cycle
Glycobiology
19
472-478
2009
Mesocricetus auratus
brenda
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
brenda
Meyer, B.H.; Adam, P.S.; Wagstaff, B.A.; Kolyfetis, G.E.; Probst, A.J.; Albers, S.V.; Dorfmueller, H.C.
Agl24 is an ancient archaeal homolog of the eukaryotic N-glycan chitobiose synthesis enzymes
eLife
11
e67448
2022
Sulfolobus acidocaldarius (Q4J9C3)
brenda
EXTERNAL LINKS (specific for EC-Number 2.4.1.141)
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