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UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
additional information
?
-
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
initiating subsequent synthesis of Glc3Man9GlcNAc2-diphosphodolichol
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?, r
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
the enzyme catalyzes the first step in the assembly of dolichol-linked oligosaccharides
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
the enzyme catalyzes the first step in the assembly of dolichol-linked oligosaccharides
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
enzyme initiates the dolichol cycle for the biosynthesis of asparagine-linked glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
the enzyme catalyzes the committed step for N-linked glycosylation
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
the enzyme catalyzes the key step in the assembly of oligosaccharide-lipid intermediates in N-linked glycosylation
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
the enzyme is encoded by ALG7, whose expression affects the extent of N-glycosylation and secretion of proteins
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
deficiency of UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1 phosphate transferase (DPAGT1) causes a novel congenital disorder of glycosylation type Ij
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
first enzyme in the dolichol pathway of protein N-glycosylation. The all-trans-retinoic acid induction of the enzyme has a regulatory impact on the dolichol pathway
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
enzyme activity, immunoreactive GPT, and GPT mRNA are modulated in parallel during development and stimulated to a similar extent by a combination of insulin, hydrocortisone and prolactin in mouse mammary gland
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
the enzyme initiates the dolichol pathway of protein N-glycosylation. A 2.5- to 4fold reduction in enzyme activity gives rise to distinct phenotypes, whose severity is inversely related to the level of enzyme activity. These phenotypes include hypersensitivity to tunicamycin, enlarged cell size, extensive aggregation, lack of typical stationary arrest and defective spore germination
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
first enzyme of dolichol pathway
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
first enzyme of dolichol pathway
-
-
?
additional information
?
-
-
overexpression of GPT in CHO-K1 cells does not go along with accumulation of intermediate Man5GlcNAc2-diphosphodolichol because of alteration of levels of oligosaccharide-diphosphodolichol and monosaccharide-phosphodolichol or through GPT enzymatic activity and excessive dolichyl phosphate consumption but rather may interfere with utilization of mannose- and glucosephosphodolichol
-
-
?
additional information
?
-
the uridine moiety of UDP-GlcNAc is coordinated with eight hydrogen bonds between the one backbone amide (Leu46), seven side chains of the amino acids and two water molecules. The uridine moiety of tunicamycin occupies the identical binding sites of UDP-GlcNAc
-
-
-
additional information
?
-
-
alg7 mutants show diminished activity of GPT, reduced steady-state levels of lipid-linked oligosaccharides and hypoglycosylated carboxypeptidase Y. Mutants also lack mitochondrial DNA including the genes that encode the components of the respiratory machinery
-
-
?
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UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
additional information
?
-
-
alg7 mutants show diminished activity of GPT, reduced steady-state levels of lipid-linked oligosaccharides and hypoglycosylated carboxypeptidase Y. Mutants also lack mitochondrial DNA including the genes that encode the components of the respiratory machinery
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
the enzyme catalyzes the first step in the assembly of dolichol-linked oligosaccharides
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
the enzyme catalyzes the first step in the assembly of dolichol-linked oligosaccharides
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
enzyme initiates the dolichol cycle for the biosynthesis of asparagine-linked glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
the enzyme catalyzes the committed step for N-linked glycosylation
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
the enzyme catalyzes the key step in the assembly of oligosaccharide-lipid intermediates in N-linked glycosylation
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
the enzyme is encoded by ALG7, whose expression affects the extent of N-glycosylation and secretion of proteins
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
deficiency of UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1 phosphate transferase (DPAGT1) causes a novel congenital disorder of glycosylation type Ij
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
first enzyme in the dolichol pathway of protein N-glycosylation. The all-trans-retinoic acid induction of the enzyme has a regulatory impact on the dolichol pathway
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
enzyme activity, immunoreactive GPT, and GPT mRNA are modulated in parallel during development and stimulated to a similar extent by a combination of insulin, hydrocortisone and prolactin in mouse mammary gland
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
the enzyme initiates the dolichol pathway of protein N-glycosylation. A 2.5- to 4fold reduction in enzyme activity gives rise to distinct phenotypes, whose severity is inversely related to the level of enzyme activity. These phenotypes include hypersensitivity to tunicamycin, enlarged cell size, extensive aggregation, lack of typical stationary arrest and defective spore germination
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
first enzyme of dolichol pathway
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
-
first enzyme of dolichol pathway
-
-
?
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metabolism
UDP-N-acetylglucosamine-dolichylphosphate N-acetylglucosamine phosphotransferase (GPT) is involved in an initial step in the N-glycosylation pathway
additional information
catalytic mechanism of DPAGT1, overview
malfunction
N-glycan biosynthesis can be inhibited by disruption of the first committed enzyme, DPAGT1
malfunction
pathogenic mutations in DPAGT1 are manifested as two possible phenotypes: congenital disorder of glycosylation DPAGT1-CDG (also known as CDG-Ij), and limb-girdle congenital myasthenic syndrome (CMS) with tubular aggregates, analysis of DPAGT1 transcriptional profiles and GTP levels in patient-derived fibroblast. enzyme mutations affect the splicing process, the stability of GTP, or the ability of this protein to correctly localise in the endoplasmic reticulum membrane
physiological function
-
GPT is involved in glycosylation of proteins on asparagine amino acids
physiological function
-
GPT is involved in glycosylation of proteins on asparagine amino acids
physiological function
-
GPT is involved in glycosylation of proteins on asparagine amino acids
physiological function
-
GPT is involved in glycosylation of proteins on asparagine amino acids
physiological function
-
GPT is involved in glycosylation of proteins on asparagine amino acids
physiological function
DPAGT1 is an integral membrane protein localized in the endoplasmic reticulum (ER) that catalyzes the transformation from UDP-GlcNAc to N-acetyl-D-glucosaminyl-diphosphodolichol. Anchored N-acetyl-D-glucosaminyldiphosphodolichol in the ER membrane is modified by sequential glycosyltransferases to form dolichol-linked oligosaccharide precursors that are transferred to selected asparagine residues of polypeptide chains by oligosaccharyltransferase. DPAGT1 catalyzes N-glycosylation of beta-catenin and E-cadherin
physiological function
the endoplasmic reticulum (ER)-resident transmembrane protein catalyses the transfer of N-acetylglucosamine from cytosolic UDP-N-acetylglucosamine to dolichol-phosphate, which is also located in the ER membrane. The result is the formation of dolichol-diphosphate-N-acetylglucosamine, the carrier of the sugars that are finally attached to proteins in glycosylation
physiological function
AglH is essential for viability in Sulfolobus acidocaldarius. AglH is able to replace the endogenous GlcNAc-1-phosphotransferase activity of Alg7 in a conditional lethal Saccharomyces cerevisiae strain, in which the first step of the eukaryal protein N-glycosylation process is repressed
physiological function
gene disruption or deletion result in larval lethality, defects in oogenesis and oocyte-to-embryo transition. Endomitotic oocytes, abnormal fusion of pronuclei, abnormal AB cell rotation, disruption of permeation barriers of eggs, and abnormal expression of chitin and chitin synthase in oocytes and eggs are the typical phenotypes observed
physiological function
-
AglH is essential for viability in Sulfolobus acidocaldarius. AglH is able to replace the endogenous GlcNAc-1-phosphotransferase activity of Alg7 in a conditional lethal Saccharomyces cerevisiae strain, in which the first step of the eukaryal protein N-glycosylation process is repressed
-
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A263D
-
mutation allows plasmid shuffling, indicating that the residue is not essential for activity
D252A
-
mutation does not allow plasmid shuffling, indicating that the residues is essential for activity
D252A/F254I
-
mutation does not allow plasmid shuffling, indicating that the residues are essential for activity
D252A/L102F
-
mutation does not allow plasmid shuffling, indicating that the residues are essential for activity
DELTA395-408
-
mutation fully eliminates enzyme expression in vivo
DELTA398-408
-
removal of the last 11 amino acids 398-408 from the enzyme has no significant effect on the catalytic activity, thermal stability, tunicamycin binding, reticular localization, or consumption of cellular dolichol phosphate
F249A
-
mutation allows plasmid shuffling, indicating that the residue is not essential for activity
F257A
-
mutation allows plasmid shuffling, indicating that the residue is not essential for activity
F395L/S396M/I397W
-
expression of the mutant enzyme
F395L/S396M/I397W/DELTA398-408
-
mutation fully eliminates enzyme expression in vivo
K125A
-
mutation allows plasmid shuffling, indicating that the residue is not essential for activity
N182A
-
mutation allows plasmid shuffling, indicating that the residue is not essential for activity
N182A/I186M
-
mutation does not allow plasmid shuffling, indicating that the residues are essential for activity
N182A/W122R
-
mutation does not allow plasmid shuffling, indicating that the residues are essential for activity
N185A
-
mutation does not allow plasmid shuffling, indicating that the residue is essential for activity
R123A
-
mutation allows plasmid shuffling, indicating that the residue is not essential for activity
W122R
-
mutation allows plasmid shuffling, indicating that the residue is not essential for activity
Y256A
-
mutation allows plasmid shuffling, indicating that the residue is not essential for activity
Y256A/F286S
-
mutation allows plasmid shuffling, indicating that the residue is not essential for activity
F110S
naturally occuring mutation in gene DPAGT1, c.329T>C, patient with hypotonia, muscle weakness, hypoacusia, psychomotor retardation, the mutation affects splicing and enzyme protein
L120M
naturally occuring mutation in gene DPAGT1, c.358C>A, patient with hypotonia phenotype, the mutation affects splicing and enzyme protein
L385R
naturally occuring mutation in gene DPAGT1, c.1154T>G, patients with foetal hypokinesia, facial dysmorphism, hypertrichosis, hypotonia, papilar atrophy, bilateral cochlear impairment, the mutation affects splicing and enzyme protein
R301C
naturally occuring mutation in gene DPAGT1, c.901C>T, the mutation affects splicing and enzyme protein
R301H
naturally occuring mutation in gene DPAGT1, c.902G>A, the mutation affects splicing and enzyme protein
V264G
naturally occuring mutation in gene DPAGT1, c.791T>G, the mutation affects splicing and enzyme protein
Y170C
-
mutant enzyme has almost no activity
D100A
mutation of conserved amino acid in the putative cytoplasmic loop II, results in loss of function
D39A
mutation in cytoplasmic loop I, no effect on function
F220A
mutation of conserved amino acid in the putative cytoplasmic loops IV, results in loss of function
F264A
mutation of conserved amino acid in the putative cytoplasmic loops V, results in loss of function
K218A
mutation in cytoplasmic loop III, no effect on function
K42A
mutation in cytoplasmic loop I, no effect on function
N103A
mutation in cytoplasmic loop II, no effect on function
D39A
-
mutation in cytoplasmic loop I, no effect on function
-
F220A
-
mutation of conserved amino acid in the putative cytoplasmic loops IV, results in loss of function
-
K218A
-
mutation in cytoplasmic loop III, no effect on function
-
K42A
-
mutation in cytoplasmic loop I, no effect on function
-
N103A
-
mutation in cytoplasmic loop II, no effect on function
-
R303K
-
catalytically inactive mutant
R303K
-
catalytically inactive mutant enzyme, this mutant can be expressed in CHO-K1 cells and can bind tunicamycin efficiently, indicative of proper folding. The R303K mutant can inhibit exogenously expressed normal enzyme
additional information
-
c.3503_3504delTC: heterozygous, two-nucleotide deletion in exon 19, causes frameshift and premature translational stop (p.L1168QfsX5), detected by PCR in all tested parents of children with mucolipidosis II
additional information
analysis of DPAGT1 transcriptional profiles and GTP levels in patient-derived fibroblasts. The enzyme mutations affect the splicing process, the stability of GTP, or the ability of this protein to correctly localise in the endoplasmic reticulum membrane, role of endoplasmic reticulum stress, detailed overview
additional information
-
analysis of DPAGT1 transcriptional profiles and GTP levels in patient-derived fibroblasts. The enzyme mutations affect the splicing process, the stability of GTP, or the ability of this protein to correctly localise in the endoplasmic reticulum membrane, role of endoplasmic reticulum stress, detailed overview
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Sharma, C.B.; Lehle, L.; Tanner, W.
Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast
Eur. J. Biochem.
126
319-325
1982
Saccharomyces cerevisiae, Saccharomyces cerevisiae X2180-1A
brenda
Villemez, C.L.; Carlo, P.L.
Properties of a soluble polyprenyl phosphate. UDP-D-N-acetylglucosamine N-acetylglucosamine-1-phosphate transferase
J. Biol. Chem.
255
8174-8178
1980
Acanthamoeba castellanii
brenda
Shailubhai, K.; Dong-Yu, B.; Saxena, E.S.; Vijay, I.K.
Purification and characterization of UDP-N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-D-glucosamine-1-phosphate transferase involved in the biosynthesis of asparagine-linked glycoproteins in the mammary gland
J. Biol. Chem.
263
15964-15972
1988
Bos taurus
brenda
Kaushal, G.P.; Elbein, A.D.
Purification and properties of UDP-GlcNAc:dolichyl-phosphate GlcNAc-1-phosphate transferase. Activation and inhibition of the enzyme
J. Biol. Chem.
260
16303-16309
1985
Sus scrofa
brenda
Plouhar, P.L.; Bretthauer, R.K.
A phospholipid requirement for dolichol pyrophosphate N-acetylglucosamine synthesis in phospholipase A2-treated rat lung microsomes
J. Biol. Chem.
257
8907-8911
1982
Rattus norvegicus
brenda
Heifetz, A.; Keenan, R.W.; Elbein, A.D.
Mechanism of action of tunicamycin on the UDP-GlcNAc:dolichyl-phosphate Glc-NAc-1-phosphate transferase
Biochemistry
18
2186-2192
1979
Sus scrofa
brenda
Kaushal, G.P.; Elbein, A.D.
Properties of solubilized UDP-GlcNAc:dolichyl phosphate-GlcNAc-1-P-transferase from soybean cultured cells
Plant Physiol.
82
748-752
1986
Glycine max
brenda
Chandra, N.C.; Doody, M.B.; Bretthauer, R.K.
Specific lipids enhance the activity of UDP-GlcNAc: dolichol phosphate GlcNAc-1-phosphate transferase in rat liver endoplasmic reticulum membrane vesicles
Arch. Biochem. Biophys.
290
345-354
1991
Rattus norvegicus
brenda
Zeng, Y.; Elbein, A.D.
UDP-N-acetylglucosamine:dolichyl-phosphate N-acetylglucosamine-1-phosphate transferase is amplified in tunicamycin-resistant soybean cells
Eur. J. Biochem.
233
458-466
1995
Glycine max
brenda
Sorensen, T.K.; Dyer, P.S.; Fierro, F.; Laube, U.; Peberdy, J.F.
Characterisation of the gptA gene, encoding UDP N-acetylglucosamine: dolichol phosphate N-acetylglucosaminylphosphoryl transferase, from the filamentous fungus, Aspergillus niger
Biochim. Biophys. Acta
1619
89-97
2003
Aspergillus niger, Aspergillus niger N402
brenda
Kukuruzinska, M.A.; Lennon, K.
Diminished activity of the first N-glycosylation enzyme, dolichol-P-dependent N-acetylglucosamine-1-P transferase (GPT), gives rise to mutant phenotypes in yeast
Biochim. Biophys. Acta
1247
51-59
1995
Saccharomyces cerevisiae
brenda
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