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8-Azido-GTP + glucose 1-phosphate
8-Azido-GDPglucose + diphosphate
-
-
-
?
8-Azido-GTP + mannose 1-phosphate
8-Azido-GDP mannose + diphosphate
-
-
-
?
ATP + alpha-D-mannose 1-phosphate
ADPmannose + diphosphate
-
recombinant beta subunit of GDPmannose pyrophosphorylase, 18% of activity with GTP
-
?
ATP + alpha-D-mannose 1-phosphate
alpha-ADP-mannose + diphosphate
-
-
-
-
?
ATP + alpha-D-mannose 1-phosphate
diphosphate + ADP-mannose
about 8% of the activity with GTP
-
-
?
ATP + D-mannose 1-phosphate
diphosphate + ADP-mannose
-
-
-
?
CTP + alpha-D-mannose 1-phosphate
alpha-CDP-mannose + diphosphate
-
-
-
-
?
CTP + alpha-D-mannose 1-phosphate
diphosphate + CDP-alpha-D-mannose
-
recombinant beta subunit of GDPmannose pyrophosphorylase, 7% of activity with GTP
-
?
CTP + alpha-D-mannose 1-phosphate
diphosphate + CDP-mannose
about 8% of the activity with GTP
-
-
?
D-mannose 1-phosphate + GTP
GDP-D-mannose + diphosphate
-
-
-
-
?
dGTP + alpha-D-mannose 1-phosphate
dGDPmannose + diphosphate
dGTP + alpha-D-mannose 1-phosphate
diphosphate + dGDP-mannose
high activity
-
-
?
diphosphate + GDP-alpha-D-mannose
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
dTTP + alpha-D-mannose 1-phosphate
alpha-dTDP-mannose + diphosphate
-
-
-
-
?
GDP-glucose + diphosphate
D-glucose 1-phosphate + GTP
-
most effective substrate in direction of nucleoside triphosphate formation, in the reverse direction GTP is a better glucose acceptor than ITP
-
r
GDP-mannose + diphosphate
GTP + D-mannose 1-phosphate
GDPmannose + diphosphate
?
-
61% of the activity with GDPglucose
-
-
r
GTP + 2-deoxy-alpha-D-glucose-1-phosphate
GDP-2-deoxy-alpha-D-glucose + diphosphate
-
recombinant GDPmannose pyrophosphorylase, 15% of activity with mannose 1-phosphate
-
?
GTP + 2-O-methyl-alpha-D-mannose 1-phosphate
diphosphate + GDP-2-O-methyl-alpha-D-mannose
-
-
-
-
?
GTP + 3-deoxy-alpha-D-arabino-hexose-1-phosphate
GDP-3-deoxy-alpha-D-arabino-hexose + diphosphate
-
recombinant GDPmannose pyrophosphorylase, 70% of activity with mannose 1-phosphate
-
?
GTP + 3-O-methyl-alpha-D-mannose 1-phosphate
diphosphate + GDP-3-O-methyl-alpha-D-mannose
-
-
-
-
?
GTP + 4-deoxy-alpha-D-lyxo-hexose 1-phosphate
GDP-4-deoxy-alpha-D-lyxo-hexose + diphosphate
-
-
-
-
?
GTP + 4-deoxy-alpha-D-lyxo-hexose-1-phosphate
GDP-4-deoxy-alpha-D-lyxo-hexose + diphosphate
-
recombinant GDPmannose pyrophosphorylase, 22% of activity with mannose 1-phosphate
-
?
GTP + 4-O-methyl-alpha-D-mannose 1-phosphate
diphosphate + GDP-4-O-methyl-alpha-D-mannose
-
-
-
-
?
GTP + 6-O-methyl-alpha-D-mannose 1-phosphate
diphosphate + GDP-6-O-methyl-alpha-D-mannose
-
-
-
-
?
GTP + alpha-D-galactose 1-phosphate
GDP-alpha-D-galactose + diphosphate
-
-
-
-
?
GTP + alpha-D-glucosamine 1-phosphate
alpha-GDP-glucosamine + diphosphate
-
-
-
-
?
GTP + alpha-D-glucosamine 1-phosphate
diphosphate + GDP-alpha-D-glucosamine
-
-
-
?
GTP + alpha-D-glucose 1-phosphate
alpha-GDP-glucose + diphosphate
-
-
-
-
?
GTP + alpha-D-glucose 1-phosphate
diphosphate + GDP-glucose
-
-
-
-
?
GTP + alpha-D-lyxose-1-phosphate
GDP-alpha-D-lyxose + diphosphate
-
-
-
-
?
GTP + alpha-D-lyxose-1-phosphate
GDPalpha-D-lyxose + diphosphate
-
recombinant GDPmannose pyrophosphorylase, 12% of activity with mannose 1-phosphate
-
?
GTP + alpha-D-mannose 1-phosphate
alpha-GDP-mannose + diphosphate
-
in the presence of diphosphatase
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-D-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
GTP + alpha-D-mannose 1-phosphate + GTP
diphosphate + GDP-alpha-D-mannose
-
-
-
-
?
GTP + alpha-L-fucose 1-phosphate
GDP-alpha-L-fucose + diphosphate
-
-
-
-
?
GTP + alpha-N-acetyl-D-glucosamine 1-phosphate
GDP-alpha-N-acetyl-D-glucosamine + diphosphate
-
-
-
-
?
GTP + D-mannose 1-phosphate
diphosphate + GDP-mannose
IDPmannose + diphosphate
ITP + mannose 1-phosphate
-
72% of activity with GDPglucose
-
r
ITP + alpha-D-mannose 1-phosphate
IDPmannose + diphosphate
ITP + glucose 1-phosphate
IDP-glucose + diphosphate
-
-
-
?
UTP + alpha-D-mannose 1-phosphate
alpha-UDP-mannose + diphosphate
-
-
-
-
?
UTP + alpha-D-mannose 1-phosphate
diphosphate + UDP-mannose
about 8% of the activity with GTP
-
-
?
UTP + alpha-D-mannose 1-phosphate
UDPmannose + diphosphate
-
recombinant beta subunit of GDPmannose pyrophosphorylase, 12% of activity with GTP
-
?
additional information
?
-
dGTP + alpha-D-mannose 1-phosphate
dGDPmannose + diphosphate
-
8% of activity with GDP-mannose
-
r
dGTP + alpha-D-mannose 1-phosphate
dGDPmannose + diphosphate
-
8% of activity with GDP-mannose
-
r
dGTP + alpha-D-mannose 1-phosphate
dGDPmannose + diphosphate
-
34% of the activity with GTP
-
?
diphosphate + GDP-alpha-D-mannose
GTP + alpha-D-mannose 1-phosphate
-
-
-
?
diphosphate + GDP-alpha-D-mannose
GTP + alpha-D-mannose 1-phosphate
-
-
-
?
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
-
-
-
?
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
-
-
-
?
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
-
-
-
-
?
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
-
-
-
?
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
-
-
-
?
GDP-mannose + diphosphate
GTP + D-mannose 1-phosphate
-
-
-
-
r
GDP-mannose + diphosphate
GTP + D-mannose 1-phosphate
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
-
60% activity with ITP, 2% activity with UTP, 1% activity with glucose-1-phosphate, and 2% activity with ATP and glucose-1-phosphate
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
best substrate
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
regulation of the enzyme expression, overview
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
the enzyme shows high specificity for synthesizing GDP-mannose, D-glucose 1-phosphate instead of alpha-D-mannose 1-phosphate is a poor substrate
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
regulation of the enzyme expression, overview
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
the enzyme shows high specificity for synthesizing GDP-mannose, D-glucose 1-phosphate instead of alpha-D-mannose 1-phosphate is a poor substrate
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
equilibrium constant: 2.5
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
equilibrium constant: 2.5
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
enzyme regulates GDP-D-mannose synthesis through feedback inhibition
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
no activity with glucose 1-phosphate, UTP, ATP and CTP
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
?
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
no activity with GDP-D-glucose, ADP-D-mannose and UDP-D-mannose
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
enzyme of alginate biosynthetic pathway
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
recombinant 37000 Da beta subunit of GDP-mannose pyrophosphorylase has only little GDPglucose synthetic activity but high GDP mannose synthetic activity
-
?
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
specific for mannose
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
no activity with ATP, CTP, TTP, UTP, ADP-alpha-D-glucose, ADP-alpha-D-mannose, CDP-alpha-D-choline, CDP-alpha-D-glucose, CDP-beta-L-fucose, GDP-alpha-D-glucose, dTPP-alpha-D-glucose, IDP-alpha-D-galactose, UDP-alpha-D-glucose, UDP-N-acetyl-alpha-D-glucosamine, UDP-alpha-D-mannose
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
overexpression leads to an increase in cellular GDPmannose levels
-
?
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
r
GTP + D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
r
GTP + D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
r
GTP + D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
ITP + alpha-D-mannose 1-phosphate
IDPmannose + diphosphate
-
11% of activity with GDP-mannose
-
r
ITP + alpha-D-mannose 1-phosphate
IDPmannose + diphosphate
-
11% of activity with GDP-mannose
-
r
ITP + alpha-D-mannose 1-phosphate
IDPmannose + diphosphate
-
15-20% of activity with GTP
-
r
ITP + alpha-D-mannose 1-phosphate
IDPmannose + diphosphate
-
44% of the activity with GTP
-
?
ITP + alpha-D-mannose 1-phosphate
IDPmannose + diphosphate
-
ITP is more effective than GTP with mannose 1-phosphate
-
r
ITP + alpha-D-mannose 1-phosphate
IDPmannose + diphosphate
-
recombinant beta subunit of GDPmannose pyrophosphorylase, 20% of activity with GTP
-
?
additional information
?
-
repression of GMPP in yeast leads to phenotypes including hyphal lysis, defective cell wall, and failure of polarized growth and branching site selection, and cell separation
-
-
?
additional information
?
-
-
repression of GMPP in yeast leads to phenotypes including hyphal lysis, defective cell wall, and failure of polarized growth and branching site selection, and cell separation
-
-
?
additional information
?
-
bifunctional protein, with phosphomannose isomerase and guanosine diphosphate-mannose pyrophosphorylase activities
-
-
?
additional information
?
-
-
bifunctional protein, with phosphomannose isomerase and guanosine diphosphate-mannose pyrophosphorylase activities
-
-
?
additional information
?
-
repression of GMPP in yeast leads to phenotypes including hyphal lysis, defective cell wall, and failure of polarized growth and branching site selection, and cell separation
-
-
?
additional information
?
-
bifunctional protein, with phosphomannose isomerase and guanosine diphosphate-mannose pyrophosphorylase activities
-
-
?
additional information
?
-
the enzyme of Burkholderia cenocepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
-
-
?
additional information
?
-
-
the enzyme of Burkholderia cepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
-
-
?
additional information
?
-
the enzyme of Burkholderia cepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
-
-
?
additional information
?
-
-
the enzyme of Burkholderia cepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
-
-
?
additional information
?
-
the enzyme of Burkholderia cepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
-
-
?
additional information
?
-
-
GDP-MP high-throughput screening assay method devlopment and evaluation, overview
-
-
?
additional information
?
-
-
truncated GDP-mannose pyrophosphorylase domain of the whole length enzyme shows almost 100fold less sugar nucleotidyltransferase activity with only GTP and mannose 1-phosphate as substrates. The enzyme accepts all five naturally occurring NTPs (ATP, CTP, GTP, dTTP and UTP) and a range of sugar-1-phosphates (glucose-, mannose-, galactose-, glucosamine-, N-acetylglucosamine- and fucose-1-phosphate)
-
-
?
additional information
?
-
enzyme can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase enzyme, e.g. PH0923. No substrates: fructose 1-phosphate, alpha-D-galactose 1-phosphate, N-acetyl-D-glucosamine 1-phosphate
-
-
?
additional information
?
-
a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities
-
-
?
additional information
?
-
no activity with dATP, dCTP, and dTTP, and no activity with fructose-1-phosphate, alpha-D-galactose-1-phosphate, and N-acetyl-D-glucosamine-1-phosphate
-
-
?
additional information
?
-
enzyme can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase enzyme, e.g. PH0923. No substrates: fructose 1-phosphate, alpha-D-galactose 1-phosphate, N-acetyl-D-glucosamine 1-phosphate
-
-
?
additional information
?
-
a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities
-
-
?
additional information
?
-
no activity with dATP, dCTP, and dTTP, and no activity with fructose-1-phosphate, alpha-D-galactose-1-phosphate, and N-acetyl-D-glucosamine-1-phosphate
-
-
?
additional information
?
-
enzyme can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase enzyme, e.g. PH0923. No substrates: fructose 1-phosphate, alpha-D-galactose 1-phosphate, N-acetyl-D-glucosamine 1-phosphate
-
-
?
additional information
?
-
a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities
-
-
?
additional information
?
-
no activity with dATP, dCTP, and dTTP, and no activity with fructose-1-phosphate, alpha-D-galactose-1-phosphate, and N-acetyl-D-glucosamine-1-phosphate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-D-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
additional information
?
-
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
-
-
-
?
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
-
-
-
?
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
regulation of the enzyme expression, overview
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
regulation of the enzyme expression, overview
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
enzyme regulates GDP-D-mannose synthesis through feedback inhibition
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
?
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
enzyme of alginate biosynthetic pathway
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
overexpression leads to an increase in cellular GDPmannose levels
-
?
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
-
r
additional information
?
-
repression of GMPP in yeast leads to phenotypes including hyphal lysis, defective cell wall, and failure of polarized growth and branching site selection, and cell separation
-
-
?
additional information
?
-
-
repression of GMPP in yeast leads to phenotypes including hyphal lysis, defective cell wall, and failure of polarized growth and branching site selection, and cell separation
-
-
?
additional information
?
-
repression of GMPP in yeast leads to phenotypes including hyphal lysis, defective cell wall, and failure of polarized growth and branching site selection, and cell separation
-
-
?
additional information
?
-
the enzyme of Burkholderia cenocepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
-
-
?
additional information
?
-
-
the enzyme of Burkholderia cepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
-
-
?
additional information
?
-
the enzyme of Burkholderia cepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
-
-
?
additional information
?
-
-
the enzyme of Burkholderia cepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
-
-
?
additional information
?
-
the enzyme of Burkholderia cepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
-
-
?
additional information
?
-
-
truncated GDP-mannose pyrophosphorylase domain of the whole length enzyme shows almost 100fold less sugar nucleotidyltransferase activity with only GTP and mannose 1-phosphate as substrates. The enzyme accepts all five naturally occurring NTPs (ATP, CTP, GTP, dTTP and UTP) and a range of sugar-1-phosphates (glucose-, mannose-, galactose-, glucosamine-, N-acetylglucosamine- and fucose-1-phosphate)
-
-
?
additional information
?
-
a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities
-
-
?
additional information
?
-
a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities
-
-
?
additional information
?
-
a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities
-
-
?
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(4E)-4-[(6-chloro-1,3-benzodioxol-5-yl)methylidene]-1-(3,4-dimethylphenyl)pyrazolidine-3,5-dione
-
-
(4Z)-1-(4-fluorophenyl)-4-[(5-methyltetrahydrofuran-2-yl)methylidene]pyrazolidine-3,5-dione
-
-
2-(2,5-dioxo-2,5-dihydro-1H-pyrrol-1-yl)-3-methylbutanoic acid
-
2-(5-ethyl-1,3,4-thiadiazol-2-yl)-3a,4,7,7a-tetrahydro-1H-4,7-methanoisoindole-1,3(2H)-dione
-
-
2-methyl-9H-pyrido[2,3-b]indole
-
-
3-(2,3-dihydroimidazo[2,1-b][1,3]thiazol-5-yl)-1H-indole
-
-
3-(2-ethyl-5-methyl-2H-pyrrol-3-yl)-6-(4-methylphenyl)[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
-
3-(azetidin-1-yl)-N-(imidazo[1,2-a]pyridin-3-ylmethyl)propan-1-amine
-
3-[2-(4-methoxyphenyl)ethyl]-2H-1,2,4-benzothiadiazine 1,1-dioxide
-
-
4-(4-benzylpiperazin-1-yl)-7-chloroquinoline
-
-
4-[3-(3-aminopyrrolidin-1-yl)propoxy]benzoic acid
-
4-[4-(4-tert-butylbenzyl)piperazin-1-yl]-7-chloroquinoline
-
-
4-[4-(biphenyl-4-ylmethyl)piperazin-1-yl]-7-chloroquinoline
-
-
4-[4-[(4-tert-butylphenyl)methyl]piperazin-1-yl]-7-chloroquinoline
5-(2-amino-1,3-thiazol-4-yl)-2-hydroxybenzyl acetate
-
5-methyl-2-(2-phenylethyl)-1H-benzimidazole
-
-
6-(1-ethyl-3-propyl-1H-pyrazol-5-yl)-3-phenyl[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
-
6-(2,4-dichlorophenyl)-3-phenyl[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
-
6-(2-chloro-6-fluorobenzyl)-3-(2-ethyl-5-methyl-2H-pyrrol-3-yl)[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
-
6-(2-chloro-6-fluorobenzyl)-3-phenyl[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
-
6-(4-chlorophenyl)-3-(2-methylbenzyl)[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
-
6-(4-fluorophenyl)-3-(4-methoxyphenyl)[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
-
6-[[(4,6-dimethylpyrimidin-2-yl)sulfanyl]methyl]-3-phenyl[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
-
7-chloro-4-(4-methylpiperazin-1-yl)quinoline
-
-
7-methoxy-4-oxo-4H-thiochromene-3-carboxylic acid
-
-
8-(dimethylamino)-7-hydroxy-3-(1-phenyl-1H-pyrazol-4-yl)-4H-chromen-4-one
-
-
9-(3,4-dimethoxyphenyl)-2,3-dihydroimidazo[1,2-c]thieno[3,2-e]pyrimidine
-
-
diphosphate
-
strong product inhibition
ethyl (2Z)-(hydroxyimino)(1H-tetrazol-5-yl)ethanoate
-
-
GDP
-
0.4 mM, 50% inhibition
GMP
-
0.4 mM, 50% inhibition
mannose 1-phosphate
-
noncompetitive inhibition of GDP-glucose phosphorolysis
methyl 1-cyano-2-hydroxy-9,10-dimethoxy-4-oxo-6,7-dihydro-4H-pyrido[2,1-a]isoquinoline-3-carboxylate
-
-
tetrapropan-2-yl [5-(1-[2-[(quinolin-2-yl)methoxy]ethyl]-1H-1,2,3-triazol-4-yl)pent-1-yne-4,4-diyl]bis(phosphonate)
[4-(7-chloroquinolin-4-yl)piperazin-1-yl](4-methylphenyl)methanone
-
-
4-[4-[(4-tert-butylphenyl)methyl]piperazin-1-yl]-7-chloroquinoline
-
competitive inhibitor
4-[4-[(4-tert-butylphenyl)methyl]piperazin-1-yl]-7-chloroquinoline
-
competitive inhibitor
4-[4-[(4-tert-butylphenyl)methyl]piperazin-1-yl]-7-chloroquinoline
-
competitive inhibitor
EDTA
no activity is detected when 2 mM EDTA is added to the dialysis buffer
GDP-glucose
-
2.5 mM, 50% inhibition
GDP-glucose
-
inhibition of GDP-mannose phosphorolysis
GDP-mannose
-
competitive vs. GTP, uncompetitive vs. mannose 1-phosphate
GDP-mannose
-
strong product inhibition
GDP-mannose
-
noncompetitive inhibition of GDP-glucose phosphorolysis
GDP-mannose
feedback inhibition
glucose 1-phosphate
-
10 mM, 50% inhibition
glucose 1-phosphate
-
inhibition of GDP-mannose phosphorolysis
miltefosine
-
-
tetrapropan-2-yl [5-(1-[2-[(quinolin-2-yl)methoxy]ethyl]-1H-1,2,3-triazol-4-yl)pent-1-yne-4,4-diyl]bis(phosphonate)
-
competitive inhibitor
tetrapropan-2-yl [5-(1-[2-[(quinolin-2-yl)methoxy]ethyl]-1H-1,2,3-triazol-4-yl)pent-1-yne-4,4-diyl]bis(phosphonate)
-
competitive inhibitor
additional information
-
high-throughput GDP-MP inhibitor large-scale screening, overview
-
additional information
not inhibited by dithiothreitol up to 5 mM
-
additional information
-
not inhibited by dithiothreitol up to 5 mM
-
additional information
the C-terminal 114 residue region of the PH0925 protein inhibits the Man-1-P GTase activity. The phosphomannoseisomerase activity is abolished by deletion of the C-terminal 14 residues
-
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Argininosuccinic Aciduria
Both the concentration and redox state of glutathione and ascorbate influence the sensitivity of arabidopsis to cadmium.
Chagas Disease
Trypanosoma cruzi Phosphomannomutase and Guanosine Diphosphate-Mannose Pyrophosphorylase Ligandability Assessment.
Cystic Fibrosis
Alginate biosynthetic enzymes in mucoid and nonmucoid Pseudomonas aeruginosa: overproduction of phosphomannose isomerase, phosphomannomutase, and GDP-mannose pyrophosphorylase by overexpression of the phosphomannose isomerase (pmi) gene.
Epilepsy, Generalized
Congenital muscular dystrophy and generalized epilepsy caused by GMPPB mutations.
Epileptic Syndromes
Congenital muscular dystrophy and generalized epilepsy caused by GMPPB mutations.
Eye Abnormalities
Mutations in GDP-mannose pyrophosphorylase B cause congenital and limb-girdle muscular dystrophies associated with hypoglycosylation of ?-dystroglycan.
Hypersensitivity
A mutation in GDP-mannose pyrophosphorylase causes conditional hypersensitivity to ammonium, resulting in Arabidopsis root growth inhibition, altered ammonium metabolism, and hormone homeostasis.
Hypersensitivity
GDP-mannose pyrophosphorylase is a genetic determinant of ammonium sensitivity in Arabidopsis thaliana.
Hypersensitivity
Toward the mechanism of NH(4) (+) sensitivity mediated by Arabidopsis GDP-mannose pyrophosphorylase.
Infections
Ascorbic acid deficiency in arabidopsis induces constitutive priming that is dependent on hydrogen peroxide, salicylic acid, and the NPR1 gene.
Intellectual Disability
Expanding the phenotype of GMPPB mutations.
Intellectual Disability
Late-onset limb-girdle muscular dystrophy caused by GMPPB mutations.
Leishmaniasis
GDP-Mannose Pyrophosphorylase: A Biologically Validated Target for Drug Development Against Leishmaniasis.
Leishmaniasis
Insight into the self-association of key enzymes from pathogenic species.
mannose-1-phosphate guanylyltransferase deficiency
Muscle involvement in limb-girdle muscular dystrophy with GMPPB deficiency (LGMD2T).
Muscle Weakness
Mutations in GMPPB Presenting with Pseudometabolic Myopathy.
Muscular Diseases
Broad phenotypic spectrum and genotype-phenotype correlations in GMPPB-related dystroglycanopathies: an Italian cross-sectional study.
Muscular Diseases
Elucidation of the Genetic Cause in Dutch Limb Girdle Muscular Dystrophy Families: A 27-Year's Journey.
Muscular Diseases
Mutations in GMPPB Presenting with Pseudometabolic Myopathy.
Muscular Diseases
Trouble at the junction: When myopathy and myasthenia overlap.
Muscular Dystrophies
160 kb deletion in ISPD unmasking a recessive mutation in a patient with Walker-Warburg syndrome.
Muscular Dystrophies
A homozygous mutation in GMPPB leads to centronuclear myopathy with combined pre- and postsynaptic defects of neuromuscular transmission.
Muscular Dystrophies
Clinical and electrophysiological evaluation of myasthenic features in an alpha-dystroglycanopathy cohort (FKRP-predominant).
Muscular Dystrophies
Congenital muscular dystrophy and generalized epilepsy caused by GMPPB mutations.
Muscular Dystrophies
Early and long-term effect of the treatment with pyridostigmine in patients with GMPPB-related congenital myasthenic syndrome.
Muscular Dystrophies
GMPPB-Associated Dystroglycanopathy: Emerging Common Variants with Phenotype Correlation.
Muscular Dystrophies
Integrative data mining highlights candidate genes for monogenic myopathies.
Muscular Dystrophies
ISPD mutations account for a small proportion of Italian Limb Girdle Muscular Dystrophy cases.
Muscular Dystrophies
Late-onset limb-girdle muscular dystrophy caused by GMPPB mutations.
Muscular Dystrophies
Mutations in GMPPB cause congenital myasthenic syndrome and bridge myasthenic disorders with dystroglycanopathies.
Muscular Dystrophies
Novel mutations in the C-terminal region of GMPPB causing limb-girdle muscular dystrophy overlapping with congenital myasthenic syndrome.
Muscular Dystrophies, Limb-Girdle
Expanding the phenotype of GMPPB mutations.
Muscular Dystrophies, Limb-Girdle
ISPD mutations account for a small proportion of Italian Limb Girdle Muscular Dystrophy cases.
Muscular Dystrophies, Limb-Girdle
Late-onset limb-girdle muscular dystrophy caused by GMPPB mutations.
Muscular Dystrophies, Limb-Girdle
Limb-girdle muscular dystrophy due to GMPPB mutations: A case report and comprehensive literature review.
Muscular Dystrophies, Limb-Girdle
Lysosomal degradation of GMPPB is associated with limb-girdle muscular dystrophy type 2T.
Muscular Dystrophies, Limb-Girdle
Muscle involvement in limb-girdle muscular dystrophy with GMPPB deficiency (LGMD2T).
Muscular Dystrophies, Limb-Girdle
Mutations in GDP-mannose pyrophosphorylase B cause congenital and limb-girdle muscular dystrophies associated with hypoglycosylation of ?-dystroglycan.
Muscular Dystrophies, Limb-Girdle
Mutations in GMPPA Cause a Glycosylation Disorder Characterized by Intellectual Disability and Autonomic Dysfunction.
Muscular Dystrophies, Limb-Girdle
Novel mutations in the C-terminal region of GMPPB causing limb-girdle muscular dystrophy overlapping with congenital myasthenic syndrome.
Muscular Dystrophies, Limb-Girdle
Two patients with GMPPB mutation: The overlapping phenotypes of limb-girdle myasthenic syndrome and limb-girdle muscular dystrophy dystroglycanopathy.
Myasthenic Syndromes, Congenital
A homozygous mutation in GMPPB leads to centronuclear myopathy with combined pre- and postsynaptic defects of neuromuscular transmission.
Myasthenic Syndromes, Congenital
Broad phenotypic spectrum and genotype-phenotype correlations in GMPPB-related dystroglycanopathies: an Italian cross-sectional study.
Myasthenic Syndromes, Congenital
Clinical features of the myasthenic syndrome arising from mutations in GMPPB.
Myasthenic Syndromes, Congenital
Early and long-term effect of the treatment with pyridostigmine in patients with GMPPB-related congenital myasthenic syndrome.
Myasthenic Syndromes, Congenital
Late-onset limb-girdle muscular dystrophy caused by GMPPB mutations.
Myasthenic Syndromes, Congenital
Lysosomal degradation of GMPPB is associated with limb-girdle muscular dystrophy type 2T.
Myasthenic Syndromes, Congenital
Mutations in GMPPB cause congenital myasthenic syndrome and bridge myasthenic disorders with dystroglycanopathies.
Myasthenic Syndromes, Congenital
Novel mutations in the C-terminal region of GMPPB causing limb-girdle muscular dystrophy overlapping with congenital myasthenic syndrome.
Myasthenic Syndromes, Congenital
Trouble at the junction: When myopathy and myasthenia overlap.
Myopathies, Structural, Congenital
A homozygous mutation in GMPPB leads to centronuclear myopathy with combined pre- and postsynaptic defects of neuromuscular transmission.
Parasitic Diseases
Insight into the self-association of key enzymes from pathogenic species.
Rhabdomyolysis
Expanding the phenotype of GMPPB mutations.
Sarcoglycanopathies
Elucidation of the Genetic Cause in Dutch Limb Girdle Muscular Dystrophy Families: A 27-Year's Journey.
Walker-Warburg Syndrome
Broad phenotypic spectrum and genotype-phenotype correlations in GMPPB-related dystroglycanopathies: an Italian cross-sectional study.
Walker-Warburg Syndrome
Clinical and electrophysiological evaluation of myasthenic features in an alpha-dystroglycanopathy cohort (FKRP-predominant).
Walker-Warburg Syndrome
Steroid therapy in an alpha-dystroglycanopathy due to GMPPB gene mutations: A case report.
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evolution
-
unrooted relationship tree of MPG proteins from various organisms, phylogenetic analysis, overview
evolution
four members of GMP gene family are encoded in the tomato genome, which constitutively expressed in various tissues in distinct expression patterns
evolution
the enzyme belongs to the mannose-6-phosphate isomerase type 2 family
evolution
-
the enzyme belongs to the mannose-6-phosphate isomerase type 2 family
-
evolution
-
the enzyme belongs to the mannose-6-phosphate isomerase type 2 family
-
malfunction
-
the ascorbic acid-deficient Arabidopsis thaliana mutant vtc1-1 is defective in GDP-mannose pyrophosphorylase and exhibits conditional hypersensitivity to ammonium, a phenomenon that is independent of ascorbic acid deficiency. Defective N-glycosylation in vtc1-1 contributes to cell wall, membrane and cell cycle defects, resulting in root growth inhibition in the presence of NH4+, GDP-mannose deficiency does not generally lead to and is not the primary cause of NH4+ sensitivity. GDP-mannose deficiency results in an up-regulation of ER stress genes, enhanced programmed cell death and defective cell cycle proliferation in vtc1-1 triggered by NH4+, overview. Root development in the presence of NH4+ is fully recovered in vtc1-1 containing one wild-type copy of VTC1
malfunction
enzyme deficiency leads to reduced alpha-dystroglycan glycosylation in the muscle biopsies of affected individuals and in available fibroblasts. Mutations in GDP-mannose pyrophosphorylase B (GMPPB) can result in muscular dystrophy variants with hypoglycosylated alpha-dystroglycan. Overexpression of wild-type GMPPB in fibroblasts from an affected individual partially restores glycosylation of alpha-dystroglycan in muscle. Five of the identified missense mutations cause formation of aggregates in the cytoplasm or near membrane protrusions. Enzyme mutant phenotypes with brain and muscle abnormalities, overview
malfunction
overexpression of OsVTC1-8 does not restore the ascorbic acid synthesis of the vtc1-1 mutant in Arabidopsis
malfunction
reducing ascorbic acid leads to leaf lesion and defence response in knock-down of the ascorbic acid biosynthetic enzyme GDP-D-mannose pyrophosphorylase gene in tomato plant. Constitutive overexpression of SlGMP3 increases the total ascorbic acid contents in the fully expanded leaves and red ripe fruits, with enhanced tolerance to oxidative stress in SlGMP3 overexpressing plants. In SlGMP2/3-knockdown lines, the total ascorbic acid contents in leaves, immature green fruits, and breaker fruits decrease dramatically. With the developments of fruit, the ascorbic acid levels increase up to 46% in breaker stage compared with immature green stage in wild-type plants, whereas no major difference is observed between two stages of SlGMP2/3-knockdown lines. In SlGMP2/3-knockdown transgenic line KD17, SlGME2 and SlGGP1 are significantly up-regulated (over one fold) compared with the wild-type plants. The spontaneous lesions on the leaves of SlGMP2/3-knockdown plants develop in a similar manner as a hypersensitive response after pathogen attack. Impairment of the photosynthetic system in SlGMP2/3-knockdown plants, overview
malfunction
the lack of a functional bceA gene does not affect exopolysaccharide production yield in a non-polar insertion bceA mutant. The in silico search for putative bceA homologues reveals the presence of 2-5 bceA orthologues in the Burkholderia genomes available. This suggests that in Burkholderia cepacia IST408 putative bceA functional homologues may compensate the bceA mutation
malfunction
-
the lack of a functional bceA gene does not affect exopolysaccharide production yield in a non-polar insertion bceA mutant. The in silico search for putative bceA homologues reveals the presence of 2-5 bceA orthologues in the Burkholderia genomes available. This suggests that in Burkholderia cepacia IST408 putative bceA functional homologues may compensate the bceA mutation
-
malfunction
-
the ascorbic acid-deficient Arabidopsis thaliana mutant vtc1-1 is defective in GDP-mannose pyrophosphorylase and exhibits conditional hypersensitivity to ammonium, a phenomenon that is independent of ascorbic acid deficiency. Defective N-glycosylation in vtc1-1 contributes to cell wall, membrane and cell cycle defects, resulting in root growth inhibition in the presence of NH4+, GDP-mannose deficiency does not generally lead to and is not the primary cause of NH4+ sensitivity. GDP-mannose deficiency results in an up-regulation of ER stress genes, enhanced programmed cell death and defective cell cycle proliferation in vtc1-1 triggered by NH4+, overview. Root development in the presence of NH4+ is fully recovered in vtc1-1 containing one wild-type copy of VTC1
-
metabolism
the enzyme catalyzes a step in the mannose activation pathways and glycoconjugate biosynthesis in Leishmania, overview
metabolism
enzyme OsVTC1-1 and OsVTC1-3 have higher GMPase activities than enzyme OsVTC1-8 in vitro. Only OsVTC1-1 and OsVTC1-3 are involved in ascorbic acid synthesis in rice
metabolism
GDP-mannose pyrophosphorylase which catalyzes the conversion of D-mannose-1-P to GDP-D-mannose in AsA biosynthetic pathway. GDP-D-mannose pyrophosphorylase is a vital enzyme in the Smirnoff-Wheeler's pathway for the biosynthesis of ascorbic acid in plants
metabolism
the enzyme is involved in L-ascorbic acid biosynthesis in plants
metabolism
isoform VTC1-1 is involved in ascorbic acid synthesis in rice leaves
metabolism
isoform VTC1-3 is involved in ascorbic acid synthesis in rice roots
metabolism
the bceA gene is part of the exopolysaccharide biosynthetic cluster
metabolism
-
the bceA gene is part of the exopolysaccharide biosynthetic cluster
-
physiological function
essential in bloodstream-form
physiological function
the enzyme catalyzes the formation of GDP-Man, a fundamental precursor for protein glycosylation and bacterial cell wall and capsular polysaccharide biosynthesis
physiological function
the GDP-mannose pyrophosphorylase is involved in glycosylation and essential for amastigote survival
physiological function
in VTC1-1 RNAi plants, the ascorbic acid content of rice leaves decreases, and the ascorbic acid production induced by light is limited. The overexpression of isoform VTC1-1 or OsVTC1-3 restores the ascorbic acid synthesis of a vtc1-1 mutant in Arabidopsis thaliana
physiological function
VTC1-3 RNAi lines alter ascorbic acid synthesis levels in rice roots, but not in the leaves or under the light/dark treatment. The overexpression of isooform VTC1-1 or OsVTC1-3 restores the ascorbic acid synthesis of a vtc1-1 mutant in Arabidopsis thaliana
physiological function
enzyme OsVTC1-1 may be involved in the ascorbic acid synthesis, which takes place in leaves. Overexpression of OsVTC1-1 restores the ascorbic acid synthesis of the vtc1-1 mutant in Arabidopsis
physiological function
enzyme OsVTC1-3 may be responsible for ascorbic acid synthesis in roots. Overexpression of OsVTC1-3 restores the ascorbic acid synthesis of the vtc1-1 mutant in Arabidopsis
physiological function
knockdown of GMPPB in zebrafish causes structural muscle defects with decreased motility, eye abnormalities, and reduced glycosylation of alpha-dystroglycan
physiological function
-
over-expression of isoform Gmp3 increases total L-ascorbic acid contents and enhances the tolerance to oxidative stress in tomato. Knock-down of Gmp3 significantly decreases L-ascorbic acid contents below the threshold level and alters the phenotype of tomato plants with lesions and further senescence. This symptom could result from failing to instantly deplete the reactive oxygen species as decline of free radical scavenging activity. More reactive oxygen species accumulate in the leaves and then trigger expressions of defence-related genes. Symptoms occur on the leaves similar to hypersensitive responses against pathogens
physiological function
the enzyme catalyzes the formation of GDP-mannose from GTP and mannose-1-phosphate. GDP-mannose is required for O-mannosylation of proteins, including alpha-dystroglycan, and it is the substrate of cytosolic mannosyltransferases
physiological function
the overexpression of VTC1-1 restores the ascorbic acid synthesis of a VTC1-1 mutant in Arabidopsis. In VTC1-1 RNAi plants, the ascorbic acid content of rice leaves decreases, and the ascorbic acid production induced by light is limited
physiological function
the overexpression of VTC1-3 restores the ascorbic acid synthesis of a VTC1-1 mutant in Arabidopsis. Isoform VTC1-3 RNAi lines alter ascorbic acid synthesis levels in rice roots, but not in the leaves or under the light/dark treatment
physiological function
over-expression of GMP3 increases total ascorbate contents and enhances the tolerance to oxidative stress in tomato. Knock-down of GMP3 significantly decreases ascorbate contents below the threshold level and alters the phenotype of tomato plants with lesions and further senescence. In the mutant, reactive oxygen species accumulate in the leaves and then trigger expressions of defence-related genes. The photosynthesis rate of leaves falls dramatically
physiological function
the enzyme is involved in cepacian production yield and rheological properties and in the size of biofilms formed
physiological function
-
the enzyme is involved in cepacian production yield and rheological properties and in the size of biofilms formed
-
physiological function
-
the enzyme catalyzes the formation of GDP-Man, a fundamental precursor for protein glycosylation and bacterial cell wall and capsular polysaccharide biosynthesis
-
additional information
a common motif of amino acids binds to the mannose moiety of the substrate and is specific to the catalytic site of the parasite enzyme, molecular dynamics and homology modeling, overview. Sequence comparison to the human enzyme
additional information
-
a common motif of amino acids binds to the mannose moiety of the substrate and is specific to the catalytic site of the parasite enzyme, molecular dynamics and homology modeling, overview. Sequence comparison to the human enzyme
additional information
-
OsMPG1 is able to provide tolerance towards salinity stress at the seedling level when overexpressed in tobacco plants
additional information
-
overexpression of GDP-mannose pyrophosphorylase from Saccharomyces cerevisiae in red fruits of Solanum lycopersicum enhances L-ascorbate levels
additional information
overexpression of GDP-mannose pyrophosphorylase in red fruits of Solanum lycopersicum enhances L-ascorbate levels
additional information
-
the C-6 hydroxy group of the alpha-D-mannose 1-phosphate substrate is not required for binding to the enzyme
additional information
the enzyme has two separate domains: a N-terminal Rossman fold-like domain and a C-terminal left-handed beta-helix domain. Two molecules associate into a dimer through a tail-to-tail arrangement of the C-terminal domains. Substrate and product binding are associated with significant changes in the conformation of loop regions lining the active center and in the relative orientation of the two domains, active site structure, overview
additional information
-
the enzyme has two separate domains: a N-terminal Rossman fold-like domain and a C-terminal left-handed beta-helix domain. Two molecules associate into a dimer through a tail-to-tail arrangement of the C-terminal domains. Substrate and product binding are associated with significant changes in the conformation of loop regions lining the active center and in the relative orientation of the two domains, active site structure, overview
additional information
the sugar-1-phosphate nucleotidylyltransferase activity is located in the region from the N-terminus to the 345th residue, the Man-1-P GTase activity is located in the C-terminal 114 residue region of the PH0925 protein, the phosphomannose isomerase requires the the C-terminal 14 residues
additional information
-
the sugar-1-phosphate nucleotidylyltransferase activity is located in the region from the N-terminus to the 345th residue, the Man-1-P GTase activity is located in the C-terminal 114 residue region of the PH0925 protein, the phosphomannose isomerase requires the the C-terminal 14 residues
-
additional information
-
overexpression of GDP-mannose pyrophosphorylase in red fruits of Solanum lycopersicum enhances L-ascorbate levels
-
additional information
-
the sugar-1-phosphate nucleotidylyltransferase activity is located in the region from the N-terminus to the 345th residue, the Man-1-P GTase activity is located in the C-terminal 114 residue region of the PH0925 protein, the phosphomannose isomerase requires the the C-terminal 14 residues
-
additional information
-
the enzyme has two separate domains: a N-terminal Rossman fold-like domain and a C-terminal left-handed beta-helix domain. Two molecules associate into a dimer through a tail-to-tail arrangement of the C-terminal domains. Substrate and product binding are associated with significant changes in the conformation of loop regions lining the active center and in the relative orientation of the two domains, active site structure, overview
-
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Rice GDP-mannose pyrophosphorylase OsVTC1-1 and OsVTC1-3 play different roles in ascorbic acid synthesis
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Oryza sativa Japonica Group (Q6Z9A3), Oryza sativa Japonica Group (Q84JH5), Oryza sativa Japonica Group (Q941T9)
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Reducing AsA leads to leaf lesion and defence response in knock-down of the AsA biosynthetic enzyme GDP-D-mannose pyrophosphorylase gene in tomato plant
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8
e61987
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Homo sapiens (Q9Y5P6)
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8
e61987
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200-206
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Burkholderia cepacia (Q06XM8), Burkholderia cepacia, Burkholderia cepacia IST408 (Q06XM8), Burkholderia cepacia IST408
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Badejo, A.A.; Jeong, S.T.; Goto-Yamamoto, N.; Esaka, M.
Cloning and expression of GDP-D-mannose pyrophosphorylase gene and ascorbic acid content of acerola (Malpighia glabra L.) fruit at ripening stages
Plant Physiol. Biochem.
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Malpighia glabra (A0EJL9), Malpighia glabra
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Zhao, S.; Liu, L.
Expression and crystallographic studies of the Arabidopsis thaliana GDP-D-mannose pyrophosphorylase VTC1
Acta Crystallogr. Sect. F
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Arabidopsis thaliana (O22287), Arabidopsis thaliana
brenda
Zmuda, F.; Shepherd, S.; Ferguson, M.; Gray, D.; Torrie, L.; De Rycker, M.
Trypanosoma cruzi phosphomannomutase and guanosine diphosphate-mannose pyrophosphorylase ligandability assessment
Antimicrob. Agents Chemother.
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Trypanosoma cruzi (Q4CMK4), Trypanosoma cruzi, Trypanosoma cruzi CL Brener (Q4CMK4)
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Pomel, S.; Mao, W.; Ha-Duong, T.; Cave, C.; Loiseau, P.
GDP-mannose pyrophosphorylase A biologically validated target for drug development against leishmaniasis
Front. Cell. Infect. Microbiol.
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Homo sapiens, Leishmania donovani, Leishmania mexicana
brenda
Gogoi, P.; Mordina, P.; Kanaujia, S.P.
Exploiting the rationale behind substrate recognition by promiscuous thermophilic NDP-sugar pyrophosphorylase for expanding glycorandomization an in silico study
J. Biomol. Struct. Dyn.
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6099-6111
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Pyrococcus horikoshii (O58649)
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