Information on EC 2.7.8.15 - UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
2.7.8.15
-
RECOMMENDED NAME
GeneOntology No.
UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
UDP-N-acetyl-D-glucosamine + dolichyl phosphate = UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
substituted phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
dolichyl-diphosphooligosaccharide biosynthesis
-
Metabolic pathways
-
N-Glycan biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:dolichyl-phosphate N-acetyl-D-glucosaminephosphotransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acetylglucosamine-1-phosphotransferase, uridine diphosphoacetylglucosamine-dolichyl phosphate
-
-
-
-
chitobiosylpyrophosphoryldolichol synthase
-
-
-
-
Dol-P dependent GlcNAc-1-P transferase
-
enzyme is encoded by ALG7
dolichol phosphate N-acetylglucosamine-1-phosphotransferase
-
-
-
-
dolichol-P-dependent N-acetylglucosamine-1-P transferase
-
-
-
-
dolichol-P-dependent N-acetylglucosamine-1-phosphate transferase
-
-
-
-
DPAGT1
-
-
-
-
G1PT
-
-
-
-
GlcNAc-1-P transferase
-
-
-
-
GlcNAc-1-P transferase
-
-
GlcNAc-phosphotransferase
-
encoded by genes GNPTAB and GNPTG, deficiency causes mucolipidosis II
GPT
-
-
-
-
GPT
-
-
L-G1PT
-
-
-
-
N-acetylglucosamine-1-phosphate transferase
-
-
-
-
N-acetylglucosamine-1-phosphotransferase
-
-
UDP-acetylglucosamine-dolichol phosphate acetylglucosamine phosphotransferase
-
-
-
-
UDP-acetylglucosamine-dolichol phosphate acetylglucosamine-1-phosphotransferase
-
-
-
-
UDP-GlcNAc:dolichol phosphate GlcNAc-1-phosphate transferase
-
-
UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1 phosphate transferase
-
-
-
-
UDP-GlcNAc:dolichyl-P GlcNAc1P transferase
-
-
-
-
UDP-GlcNAc:dolichyl-phosphate GlcNAc-1-phosphate transferase
-
-
-
-
UDP-N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-D-glucosamine-1-phosphate transferase
-
-
-
-
UDPGlcNAc:dolichol phosphate N-acetylglucosamine 1-phosphate transferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
70431-08-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Aspergillus niger N402
N402
-
-
Manually annotated by BRENDA team
french Canadian founder population in Saguenay-Lac-Saint-Jean (Quebec, Canada) with mucolipidosis II carrier rate at 1/39 (highest worldwide)
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae X2180-1A
X2180-1A
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
GPT is involved in glycosylation of proteins on asparagine amino acids
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-GlcNAc + dolichyl phosphate
UMP + GlcNAc-diphosphodolichol
show the reaction diagram
-
-
initiating subsequent synthesis of Glc3Man9GlcNAc2-diphosphodolichol
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?, r
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
Saccharomyces cerevisiae X2180-1A
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
Aspergillus niger N402
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
show the reaction diagram
-
the enzyme catalyzes the committed step for N-linked glycosylation
-
-
-
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
show the reaction diagram
-
the enzyme catalyzes the committed step for N-linked glycosylation
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
the enzyme catalyzes the first step in the assembly of dolichol-linked oligosaccharides
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
show the reaction diagram
-
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
?
show the reaction diagram
-
first enzyme of dolichol pathway
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
show the reaction diagram
-
enzyme initiates the dolichol cycle for the biosynthesis of asparagine-linked glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
show the reaction diagram
-
the enzyme catalyzes the key step in the assembly of oligosaccharide-lipid intermediates in N-linked glycosylation
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
show the reaction diagram
-
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
?
show the reaction diagram
Saccharomyces cerevisiae X2180-1A
-
first enzyme of dolichol pathway
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
show the reaction diagram
Aspergillus niger N402
-
the enzyme catalyzes the first step in the assembly of dolichol-linked oligosaccharides
-
-
?
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
-
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
show the reaction diagram
-
the enzyme catalyzes the committed step for N-linked glycosylation
-
-
-
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
show the reaction diagram
-
the enzyme catalyzes the committed step for N-linked glycosylation
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
the enzyme catalyzes the first step in the assembly of dolichol-linked oligosaccharides
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
show the reaction diagram
-
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
?
show the reaction diagram
-
first enzyme of dolichol pathway
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
show the reaction diagram
-
enzyme initiates the dolichol cycle for the biosynthesis of asparagine-linked glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
show the reaction diagram
-
the enzyme catalyzes the key step in the assembly of oligosaccharide-lipid intermediates in N-linked glycosylation
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
show the reaction diagram
-
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
?
show the reaction diagram
Saccharomyces cerevisiae X2180-1A
-
first enzyme of dolichol pathway
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
?
show the reaction diagram
Aspergillus niger N402
-
the enzyme catalyzes the first step in the assembly of dolichol-linked oligosaccharides
-
-
?
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
divalent metal required, Ca2+ is less effective than Mg2+
Ca2+
-
less effective than Mn2+ or Mg2+
Ca2+
-
1-2 mM, weak stimulation
Mg2+
-
divalent metal required, optimal activity in presence of Mg2+
Mg2+
-
divalent cation required for dialyzed enzyme, maximal activity in presence of 8-10 mM
Mg2+
-
stimulates
Mg2+
-
either Mn2+, 1 mM, or Mg2+, 10 mM, required for optimal activity
Mg2+
-
10 mM required for optimal activity
Mn2+
-
divalent metal required, Mn2+ is less effective than Mg2+
Mn2+
-
divalent cation required for dialyzed enzyme, Mg2+ or Mn2+
Mn2+
-
stimulates
Mn2+
-
either Mn2+, 1 mM, or Mg2+, 10 mM, required for optimal activity
Mn2+
-
1-2 mM, weak stimulation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Amphomycin
-
-
Ca2+
-
above 2 mM
Diumycin
-
-
-
Diumycin
-
-
-
dolichyl phosphate
-
at high concentrations
GDP-mannose
-
-
GDP-mannose
-
slight
GDP-mannose
-
5 residues of mannose from GDP-mannose
GTP
-
0.4 mM, 25-30% inhibition, enzyme from tunicamycin-resistant cells, no inhibition of wild-type enzyme up to 0.4 mM
Hg2+
-
partially reversed by dithiothreitol
iodoacetamide
-
-
Mn2+
-
above 2 mM
NEM
-
protected to the extent of about 50% when all of the substrates, UDP-GlcNAc, dolichyl phosphate and Mn2+ are added before addition of the sulfhydryl reagent
PCMB
-
protected to the extent of about 50% when all of the substrates, UDP-GlcNAc, dolichyl phosphate anf Mn2+ are added before addition of the sulfhydryl reagent
PCMB
-
the enzyme from tunicamycin-resistant cells is equally sensitive to tunicamycin as the wilde-type enzyme
phosphatidylcholine
-
-
phosphatidylethanolamine
-
-
phosphatidylserine
-
-
Showdomycin
-
-
Triton X-100
-
substrate protects from inhibition
Tunicamycin
-
1 mM, complete inhibition
Tunicamycin
-
0.00005-0.0001 mg/ml, 50% inhibition, noncompetitive with respect to UDP-GlcNAc or dolichyl phosphate, both directions
Tunicamycin
-
-
Tunicamycin
-
-
UDP
-
1 mM, 55% inhibition
UDP-GlcNAc
-
strong inhibition
UDP-glucose
-
-
UDP-glucose
-
-
UDP-hexanolamine
-
-
UDP-xylose
-
-
UMP
-
1 mM, 45% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
-
0.01-0.025 mM, stimulates activity of tunicamycin-resistant cells about 20-30%
cardiolipin
-
stimulates activity of enzyme in endoplasmic membrane vesicles, due to better solubilization of the dolichol phosphate
Dolichyl-phosphoryl-mannose
-
stimulates
Dolichyl-phosphoryl-mannose
-
stimulates
GDP-mannose
-
stimulates by protecting the substrate UDP-GlcNAc from degradation
monogalactosyldiglyceride
-
stimulates activity of enzyme in endoplasmic membrane vesicles
phosphatidylcholine
-
0.001 mM/ml, 30-40% inhibition
phosphatidylethanolamine
-
stimulates activity of enzyme in endoplasmic membrane vesicles
phosphatidylglycerol
-
solubilized enzyme is stimulated by exogenously added phospholipids in order of increasing activity: phosphatidylglycerol, phosphatidylinositol, phosphatidylserine
phosphatidylglycerol
-
2- to 3fold maximal stimulation at 0.06 mg/ml
phosphatidylglycerol
-
activity is slightly enhanced
phosphatidylinositol
-
solubilized enzyme is stimulated by exogenously added phospholipids in order of increasing activity: phosphatidylglycerol, phosphatidylinositol, phosphatidylserine
phosphatidylinositol
-
stimulates
phosphatidylserine
-
solubilized enzyme is stimulated by exogenously added phospholipids in order of increasing activity: phosphatidylglycerol, phosphatidylinositol, phosphatidylserine
Phospholipid
-
solubilized enzyme is stimulated by exogenously added phospholipids in order of increasing activity: phosphatidylglycerol, phosphatidylinositol, phosphatidylserine
Phospholipid
-
endogenous microsomal phospholipid is required for reaction to proceed normally in rat lung microsomes
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0007
-
dolichyl phosphate
-
37C
0.001
-
dolichyl phosphate
-
pH 7.5
0.001
-
dolichyl phosphate
-
pH 7.5, 37C
0.0045
-
dolichyl phosphate
-
pH 7.4, 30C
0.0062
-
dolichyl phosphate
-
pH 7.5, 37C
0.016
-
dolichyl phosphate
-
pH 7.6, 37C
0.0001
-
UDP-GlcNAc
-
pH 7.5, 37C
0.0002
-
UDP-GlcNAc
-
37C
0.00042
-
UDP-GlcNAc
-
pH 7.5, 37C
0.0005
-
UDP-GlcNAc
-
pH 7.4, 30C
0.0045
-
UDP-GlcNAc
-
pH 7.6, 37C
0.015
-
UDP-GlcNAc
-
pH 7.5
0.18
-
dolichyl phosphate
-
pH 7.5
additional information
-
additional information
-
Km-value for dolichyl phosphate: 0.005 mg/0.1 ml
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.2
7.6
-
-
7.4
7.6
-
-
7.4
7.6
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
8.5
-
pH 6.5: about 60% of maximal activity, pH 8.5: about 35% of maximal activity
7
8.7
-
pH 6.0: no activity, pH 7.0: 85% of maximal activity, pH 8.7: 64% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
-
with 0.5% Triton X-100 in the assay mixture
60
-
-
with either dioleoylphosphatidylethanolamine or cardiolipin in the assay mixture
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
40
-
0C: no activity, 15C: 11% of maximal activity, 25C: 73% of maximal activity, 35C: 96% of maximal activity, 40C: 57% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
the tunicamycin resistant cells have a greater than 40fold increase in the activity of the enzyme UDP-GlcNAc:dolichyl-P GlcNAc1P transferase. Increase in enzyme activity is due to an increased production of the enzyme
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme has multiple transmembrane spans and a critical cytosolic loop
Manually annotated by BRENDA team
-
an enzyme with multiple transmembrane spans
Manually annotated by BRENDA team
-
enzyme with multiple transmembrane spans
Manually annotated by BRENDA team
Saccharomyces cerevisiae X2180-1A
-
-
-
Manually annotated by BRENDA team
-
microsomal membranes
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae X2180-1A
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
34000
-
-
monomer, determined by SDS-PAGE and Western blot analysis
44700
-
-
-
46000
-
-
determined by SDS-PAGE and Western Blot analysis
46470
-
-
theoretical
50000
-
-
determined by SDS-PAGE and Western Blot analysis
67000
-
-
assumed to be a dimeric form, determined by SDS-PAGE and Western blot analysis
70000
-
-
suggested to be a biological precursor or the degraded native enzyme, determined by SDS-PAGE and Western blot analysis
330000
360000
-
large molecular mass of the enzyme can be due to aggregation of the hydrophobic, membrane-derived enzyme rather than resulting from subunit interaction, gel filtration
additional information
-
-
ALG7 1.5 kb mRNAs appears to be initiated at a start site downstream from that used by the 1.9 and 2.2 kb species and located bentween two in-frame ATG codons. Translation of these transcripts in vitro provides supporting evidence that the 1.5 and 1.9 kb transcripts are translationally competent, giving rise to related protein isoforms with different lengths of their NH2-terminal domains. The 1.9 kb mRNA serves in the synthesis of 36000 Da and 24000 Da species, as well as a low abundance 32000 Da protein. The 1.5 kb transcript gives rise to a translation product of 32000 Da
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 39000, SDS-PAGE
?
-
x * 51400, calculation from nucleotide sequence
?
Aspergillus niger N402
-
x * 51400, calculation from nucleotide sequence
-
dimer
-
2 * 34000, the 67000 Da enzyme form is a homodimer of UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase or perhaps a hetero-oligomer with another microsomal component
additional information
-
results indicate that either 70000 MW band in SDS-PAGE is a precursor form of the enzyme or this polypeptide, representing the native enzyme or its subunit, is proteolyzed to smaller, enzymatically active peptides of 50000 Da and 46000 Da during purification
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
the enzyme is not a glycoprotein of the asparagine-linked type
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
1 h, stable
35
-
-
the enzyme from tunicamycin-resistant cells is significantly less stable than the wild-type enzyme
40
-
-
the enzyme from tunicamycin-resistant cells is significantly less stable than the wild-type enzyme
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified enzyme is resistant to digestion with either endo-beta-N-acetylglucosaminidase H or F
-
a 1:4 dilution leads to a 65% loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C or -70C, stable for 2 weeks
-
4C, completely stable for 9-10 days. No significant loss of activity after 63 days in presence of NaN3
-
4C, solubilized enzyme loses most of its activity within 12 h
-
-20C, solubilized enzyme loses 96% of its activity after 6 days, only 20% loss of activity after 6 days in presence of 0.07 mM UDP-GlcNAc
-
0-4C, 20% glycerol, 0.02 mg phosphatidylglycerol/mg of protein, less than 20% loss of activity after 6 days. In absence of both glycerol and phosphatidylglycerol the enzyme is quite unstable and loses most of its activity within 24 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
for expression in Saccharomyces cerevisiae
-
plasmid shuffling procedure in Schizosaccharomyces pombe for analyzing site-directed mutations in the cDNA of L-G1PT for their effect on enzymatic activity
-
for expression in Saccharomyces cerevisiae
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
R303K
-
catalytically inactive mutant
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
Y170C
-
mutant enzyme has almost no activity
Y256A/F286S
-
mutation allows plasmid shuffling, indicating that the residue is not essential for activity
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