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Information on EC 2.7.7.13 - mannose-1-phosphate guanylyltransferase
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2.7.7.13 mannose-1-phosphate guanylyltransferaseIUBMB Comments
The bacterial enzyme can also use ITP and dGTP as donors.
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Word Map
- 2.7.7.13
- asa
- phosphomannomutase
-
l-ascorbic
-
myasthenic
-
limb-girdle
- l-galactose
- dystroglycanopathies
-
gmpase
- gdp-l-galactose
-
mannose-containing
- alpha-dystroglycan
- l-galactono-1,4-lactone
- acerola
-
l-galactose-1-phosphate
-
smirnoff-wheeler
- medicine
- drug development
- synthesis
- agriculture
The enzyme appears in viruses and cellular organisms
Synonyms
BceA, BceA(J) protein, BceAJ, CYT1, GDP-alpha-D-mannose pyrophosphorylase, GDP-D-mannose pyrophosphorylase, GDP-Man pyrophosphorylase, GDP-mannose pyrophosphorylase, GDP-mannose pyrophosphorylase B, GDP-ManPP, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BceA
GDP-D-mannose pyrophosphorylase
GDP-Man pyrophosphorylase
GDP-mannose pyrophosphorylase
GDP-MP
GMP3
GMPase
GMPP
GMPPB
GTP-alpha-D-Man-1-P guanylyltransferase
GTP-mannose 1-phosphate guanylyltransferase
-
-
-
-
GTP-mannose-1-phosphate guanylyltransferase
-
-
-
-
guanidine diphosphomannose pyrophoyphorylase
guanosine 5'-diphospho-D-mannose pyrophosphorylase
-
-
-
-
guanosine diphosphate-mannose pyrophosphorylase
guanosine diphosphomannose pyrophosphorylase
-
-
-
-
guanosine triphosphate-mannose 1-phosphate guanylyltransferase
-
-
-
-
guanosine-diphospho-D-mannose pyrophosphorylase
guanylyltransferase, mannose 1-phosphate
-
-
-
-
LDBPK_230120
mannose 1-phosphate guanylyltransferase (guanosine triphosphate)
-
-
-
-
mannose-1-phosphate guanylyltransferase
PH0925
RfbM
VTC1-1
VTC1-3
additional information
BceA
-
bifunctional protein with phosphomannose isomerase and GDP-mannose pyrophosphorylase activities
BceA
-
bifunctional protein with phosphomannose isomerase and GDP-mannose pyrophosphorylase activities
-
GDP-mannose pyrophosphorylase
-
-
-
-
GDP-mannose pyrophosphorylase
-
type II phosphomannose isomerase, bifunctional phosphomannose isomerase/GDP-mannose pyrophosphorylase (manC), with both PMI (E.C. 5.3.1.8) and GMP (E.C.2.7.7.13) activities
guanosine-diphospho-D-mannose pyrophosphorylase
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
additional information
bifunctional protein (type II PMI family) with phosphomannose isomerase (PMI, EC 5.3.1.8) and GDP-mannose pyrophosphorylase (GMP, EC 2.7.7.13) activities
additional information
bifunctional protein (type II PMI family) with phosphomannose isomerase (PMI, EC 5.3.1.8) and GDP-mannose pyrophosphorylase (GMP, EC 2.7.7.13) activities
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
PMI and GMP activities are most probably located in catalytically distinct domains
GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
bifunctional enzyme with both phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activity
-
GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
enzyme has both phosphomannose isomerase, i.e. PIM, and guanosine 5'-diphospho-D-mannose pyrophosphorylase, i.e. GMP, activity
GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
GTP:alpha-D-mannose-1-phosphate guanylyltransferase
The bacterial enzyme can also use ITP and dGTP as donors.
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CAS REGISTRY NUMBER
COMMENTARY
37278-24-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
low activity
-
-
?
ATP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
about 8% of the activity with GTP
-
-
?
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
low activity
-
-
?
CTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
about 8% of the activity with GTP
-
-
?
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
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-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-D-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
phosphate + GDP-mannose
-
-
-
?
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
-
-
-
-
?
IDPmannose + diphosphate
ITP + mannose 1-phosphate
-
72% of activity with GDPglucose
-
r
UTP + alpha-D-mannose 1-phosphate
alpha-UDP-mannose + diphosphate
-
-
-
-
?
UTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
about 8% of the activity with GTP
-
-
?
UTP + alpha-D-mannose 1-phosphate
diphosphate + UDP-mannose
low activity
-
-
?
UTP + alpha-D-mannose 1-phosphate
UDPmannose + diphosphate
-
recombinant beta subunit of GDPmannose pyrophosphorylase, 12% of activity with GTP
-
?
dGTP + alpha-D-mannose 1-phosphate
dGDPmannose + diphosphate
-
8% of activity with GDP-mannose
-
r
dGTP + alpha-D-mannose 1-phosphate
dGDPmannose + diphosphate
Arthrobacter sp. NRRL B1973
-
8% of activity with GDP-mannose
-
r
dGTP + alpha-D-mannose 1-phosphate
dGDPmannose + diphosphate
-
34% of the activity with GTP
-
?
dGTP + alpha-D-mannose 1-phosphate
diphosphate + dGDP-mannose
-
-
-
?
dGTP + alpha-D-mannose 1-phosphate
diphosphate + dGDP-mannose
high activity
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
-
equilibrium constant: 2.5
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
Arthrobacter sp. NRRL B1973
-
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
-
recombiant 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
ITP + alpha-D-mannose 1-phosphate
IDPmannose + diphosphate
-
11% of activity with GDP-mannose
-
r
ITP + alpha-D-mannose 1-phosphate
IDPmannose + diphosphate
Arthrobacter sp. NRRL B1973
-
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-D-mannose
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
phosphate + GDP-mannose
-
-
-
?
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
-
-
-
?
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
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
?
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
-
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
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cu2+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Ca2+
GMP activity is strongly dependent on the presence of Ca2+ or Mn2+
Ca2+
GMP activity is strongly dependent on the presence of Ca2+ or Mn2+
Ca2+
GMP activity is specifically dependent on the presence of either Mn2+ or Ca2+
Ca2+
GDP-mannose pyrophosphorylase is strongly dependent on the presence of Ca2+ or Mn2+
Ca2+
-
the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+
Co2+
-
divalent cation required for activity, second best activator, maximal activation at 5 mM
Co2+
-
the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+
Cu2+
-
the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+
Mg2+
-
divalent cation required for activity, best metal activator Mg2+, maximal activation at 5-10 mM
Mg2+
-
no product formation is observed in the absence of sugar phosphates, Mg2+ or NTP. The enzyme activity remains high between 2-15 mM concentrations. The efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+
Mg2+
highly activates sugar-1-P NTase activity with substrate Man-1-P, only slightly activating with substrates Glc-1-P and GlcN-1-P
Mg2+
-
activity depends on the ratio of Mg2+ and GTP, maximum activity at a ratio of about 1
Mg2+
-
recombinant beta subunit of GDPmannose pyrophosphorylase, 50% of activation with Mn2+
Mg2+
absolute requirement for divalent cations, partially replaced by Mn2+ and Cu2+
Mn2+
GMP activity is strongly dependent on the presence of Ca2+ or Mn2+, the presence of 5 mM Mn2+, precipitation occurred in the reaction mixture
Mn2+
GMP activity is strongly dependent on the presence of Ca2+ or Mn2+
Mn2+
GMP activity is specifically dependent on the presence of either Mn2+ or Ca2+
Mn2+
GDP-mannose pyrophosphorylase is strongly dependent on the presence of Ca2+ or Mn2+
Mn2+
-
the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+
Mn2+
-
best metal activator of recombinant beta subunit of GDPmannose pyrophosphorylase, maximal activation at 0.5 mM
Zn2+
-
the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+
additional information
descending order of activation Mg2+, Ca2+, Mn2+, Co2+, Ni2+
additional information
-
no activation and activity by Ni2+, Mg2+, and Zn2+
additional information
no activation and activity by Ni2+, Mg2+, and Zn2+
additional information
the metal cofactor requirements of the multifunctional enzyme differ with the substrates used, overview
additional information
-
recombinant beta subunit of GDPmannose pyrophosphorylase is not activated by Co2+, Zn2+, Cu2+ and Fe2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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-(5-ethyl-1,3,4-thiadiazol-2-yl)-3a,4,7,7a-tetrahydro-1H-4,7-methanoisoindole-1,3(2H)-dione
-
-
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
-
6-(1-ethyl-3-propyl-1H-pyrazol-5-yl)-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
-
-
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
-
-
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-[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
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
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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
Late-onset limb-girdle muscular dystrophy caused by GMPPB mutations.
Leishmaniasis
GDP-Mannose Pyrophosphorylase: A Biologically Validated Target for Drug Development Against Leishmaniasis.
mannose-1-phosphate guanylyltransferase deficiency
Muscle involvement in limb-girdle muscular dystrophy with GMPPB deficiency (LGMD2T).
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 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
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
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.
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15.2
3-deoxy-D-arabino-hexose 1-phosphate
-
pH 8.0, 25°C, recombinant enzyme
0.94
4-deoxy-alpha-D-lyxo-hexose 1-phosphate
-
pH 8.0, 25°C, recombinant enzyme
0.094
alpha-D-glucose 1-phosphate
-
cosubstrate GTP, Vmax: 14 micromol/min/mg
0.0161
alpha-D-mannose 1-phosphate
pH 7.6, 85°C, recombinant enzyme
0.062
alpha-D-mannose 1-phosphate
-
cosubstrate GTP, Vmax: 0.63 micromol/min/mg
0.063
alpha-D-mannose 1-phosphate
-
GDP-mannose synthesis
0.072
alpha-D-mannose 1-phosphate
-
cosubstrate GTP, Vmax: 50 micromol/min/mg
0.12
alpha-D-mannose 1-phosphate
-
cosubstrate ATP, Vmax: 11 micromol/min/mg
0.15
alpha-D-mannose 1-phosphate
-
cosubstrate UTP, Vmax: 14 micromol/min/mg
0.16
alpha-D-mannose 1-phosphate
-
cosubstrate CTP, Vmax: 11 micromol/min/mg
0.168
alpha-D-mannose 1-phosphate
-
pH 7.5, 37°C, cosubstrate GTP
0.19
alpha-D-mannose 1-phosphate
-
cosubstrate TTP, Vmax: 6 micromol/min/mg
2.9
GDP-alpha-D-mannose
pH 7.6, 10 mM Mn2+, temperature not specified in the publication
0.024
GDP-mannose
pH 7.6, recombinant enzyme, in presence of 5 mM Mg2+ and 2 mM diphosphate
2.9
GDP-mannose
pH 7.6, recombinant enzyme, presence of 10 mM Mn2+
2.9
GDP-mannose
pH 7.6, temperature not specified in the publication
0.000039
GDPmannose
-
pH 7.5, 37°C, recombinant beta subunit of GDPmannose pyrophosphorylase, cosubstrate diphosphate
0.36
GTP
-
pH 7.5, 37°C, recombinant beta subunit of GDPmannose pyrophosphorylase, cosubstrate mannose 1-phosphate
0.2
mannose 1-phosphate
-
pH 7.5, 37°C, recombinant beta subunit of GDPmannose pyrophosphorylase, cosubstrate GTP
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
195.9
GDP-alpha-D-mannose
pH 7.6, 10 mM Mn2+, temperature not specified in the publication
195.9
GDP-mannose
pH 7.6, recombinant enzyme, presence of 10 mM Mn2+
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
195.9
GDP-mannose
pH 7.6, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
GDP-mannose
mixed-type inhibition with respect to mannose 1-phosphate
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00106 - 0.1
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)
0.02
4-[4-[(4-tert-butylphenyl)methyl]piperazin-1-yl]-7-chloroquinoline
Homo sapiens
-
pH and temperature not specified in the publication
0.03068
4-[4-[(4-tert-butylphenyl)methyl]piperazin-1-yl]-7-chloroquinoline
Leishmania donovani
-
pH and temperature not specified in the publication
0.04925
4-[4-[(4-tert-butylphenyl)methyl]piperazin-1-yl]-7-chloroquinoline
Leishmania mexicana
-
pH and temperature not specified in the publication
0.00208
miltefosine
Leishmania donovani
-
pH and temperature not specified in the publication
0.02374
miltefosine
Leishmania mexicana
-
pH and temperature not specified in the publication
0.00106
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)
Leishmania donovani
-
pH and temperature not specified in the publication
0.1
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)
Leishmania mexicana
-
IC50 above 0.1 mM, pH and temperature not specified in the publication
additional information
additional information
Trypanosoma brucei
IC50 values for ATP and CTP above 0.625 mM
-
additional information
additional information
Trypanosoma brucei
-
IC50 values for ATP and CTP above 0.625 mM
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.8
with ATP, CTP, or UTP and alpha-D-mannose 1-phosphate, purified His-tagged recombinant enzyme, pH 7.6, 85°C
10.2
7.3
substrates GTP, alpha-D-glucosamine 1-phosphate, pH 7.6, 85°C
8.2
10.2
with GTP and alpha-D-mannose 1-phosphate, purified His-tagged recombinant enzyme, pH 7.6, 85°C
8.2
with dGTP and alpha-D-mannose 1-phosphate, purified His-tagged recombinant enzyme, pH 7.6, 85°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
GDP-mannose synthesis, forward reaction is very sensitive to pH fluctuation
7 - 8
-
recombinant protein exhibits relatively high activity around pH 6.0 and 9.5, with a maximum in the range of pH 7.0-8.0 in phosphate buffer
7.5
7.6
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 100
-
temperature dependence of the enzymatic activity is analyzed between 0 and 100°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.03
6.45
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme with phosphomannose isomerase and sugar-1-phosphate nucleotidylyltransferase activities, EC 5.3.1.8 and EC 2.7.7.13, respectively
GenBank
brenda
syncytia induced by nematode Heterodera schachtii
UniProt
brenda
loss of virulence after deletion of GDPmannose pyrophosphorylase gene
-
-
brenda
phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase is a bifunctional enzyme catalyzing both phosphomannose isomerase, i.e. PIM, and guanosine 5'-diphospho-D-mannose pyrophosphorylase, i.e. GMP, reactions
SwissProt
brenda
bifunctional enzyme with phosphomannose isomerase and sugar-1-phosphate nucleotidylyltransferase activities, EC 5.3.1.8 and EC 2.7.7.13, respectively
GenBank
brenda
GDP-mannose pyrophosphorylase is encoded by VIG9
SwissProt
brenda
Saccharomyces cerevisiae genome database: U24437; overexpression corrects defects in dolichol-linked saccharide formation and protein glycosylation
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
transcript abundance in all the organs of acerola examined, with the fruit having the highest expression. The relative transcript abundance of Malpighia glabra GDP-D-mannose pyrophosphorylase mRNA levels in the fruits changes as the ripening process progresses, with the unripe green fruits having the highest relative mRNA level, and the lowest is found in the fruits at advanced ripening stage
brenda
high light-induced expression level
brenda
high dark-induced expression level
brenda
additional information
OsVTC1-8 transcript level is low in both leaves and roots
brenda
additional information
OsVTC1-8 transcript level is low in both leaves and roots
brenda
additional information
OsVTC1-8 transcript level is low in both leaves and roots
brenda
additional information
SlGMP3 transcript levels are high in stems, flowers, and young leaves, whereas low in roots, and fruits at breaker and red ripe stages, expression patterns, overview
brenda
additional information
-
SlGMP3 transcript levels are high in stems, flowers, and young leaves, whereas low in roots, and fruits at breaker and red ripe stages, expression patterns, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
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
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
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
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
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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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37000
39700
42000
43000
45000
-
2 * 45000, His-tagged version, gel filtration, SDS-PAGE
54000
gel filtration, phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase is a bifunctional enzyme catalyzing both the phosphomannose isomerase, i.e. PIM, and guanosine 5'-diphospho-D-mannose pyrophosphorylase, i.e. GMP, reaction
55000
55716
x * 56000, recombinant enzyme, SDS-PAGE, x * 55716, sequence caculation
56000
42000
2 * 42000, SDS-PAGE, 2 * 41769.10, ESI-MS (41769.32 theoretical mass)
43000
-
43000 Da alpha subunit or a combinantion of alpha and beta subunit constitutes the GDPglucose pyrophosphorylase activity, the 37000 Da beta subunit constituts the GDPmannose pyrophosphorylase activity
56000
x * 56000, recombinant enzyme, SDS-PAGE, x * 55716, sequence caculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
homodimer
2 * 42000, SDS-PAGE, 2 * 41769.10, ESI-MS (41769.32 theoretical mass)
additional information
?
x * 56000, recombinant enzyme, SDS-PAGE, x * 55716, sequence caculation
dimer
-
2 * 45000, His-tagged version, gel filtration, SDS-PAGE
additional information
the enzyme's amino acid sequence contains several conserved motifs: 1. the pyrophosphorylase signature sequence 38GGXGXRLXPLX5PK54, 2. the GMP active site 210FVEKP214, 3. the zinc-binding motif 436QXH438 and the putative PMI active site 465EN(Q/E)SX (Y/F)I471
additional information
sugar-1-phosphate nucleotidylyltransferase activity is located in the region from the N-terminus to the 345th residue, and the C-terminal 114 residue region inhibits the Man-1-P guanylyltransferase activity. The N-terminal region plays an important role in the solubility of the entire protein and in the acquisition of the correct structure
additional information
-
sugar-1-phosphate nucleotidylyltransferase activity is located in the region from the N-terminus to the 345th residue, and the C-terminal 114 residue region inhibits the Man-1-P guanylyltransferase activity. The N-terminal region plays an important role in the solubility of the entire protein and in the acquisition of the correct structure
-
additional information
-
sugar-1-phosphate nucleotidylyltransferase activity is located in the region from the N-terminus to the 345th residue, and the C-terminal 114 residue region inhibits the Man-1-P guanylyltransferase activity. The N-terminal region plays an important role in the solubility of the entire protein and in the acquisition of the correct structure
-
additional information
-
43000 Da alpha subunit or a combinantion of alpha and beta subunit constitutes the GDPglucose pyrophosphorylase activity, the 37000 Da beta subunit constituts the GDPmannose pyrophosphorylase activity
additional information
the enzyme has two separate domains: a N-terminal Rossman fold-like domain and a C-terminal left-handed beta-helix domain
additional information
-
the enzyme has two separate domains: a N-terminal Rossman fold-like domain and a C-terminal left-handed beta-helix domain
additional information
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
the enzyme has two separate domains: a N-terminal Rossman fold-like domain and a C-terminal left-handed beta-helix domain
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ligand-free enzyme, sitting drop vapor diffusion method, using 0.1 M bis-Tris pH 6.5, 25% (w/v) PEG 3350, 0.2 M lithium sulfate. Enzyme bound to GTP and D-mannose 1-phosphate, sitting drop vapor diffusion method, using 0.1 M magnesium formate, 15% (w/v) PEG 3350
comparison of structural models of the GDP-mannose diphosphorylases from human and Leishmania donovani. The human active site is site very similar to the Leishmania donovani one. Leishmania donovani GDP-mannose diphosphorylase makes more interactions with its substrate than the human enzyme does
comparison of structural models of the GDP-mannose diphosphorylases from human and Leishmania donovani. Residues Leu14, Val15, Ala60, Leu92 and Pro97 surround the hydrophobic bicycle of the nucleotide, while the amine groups of the latter interact with Glu88. The ribose ring belonging to the substrate is bound to protein residues Asn116 and Ser117. The magnesium ion is chelated by Asp118 and Asp226, and the diphosphate group makes electrostatic interactions with residues Arg21 and Lys31, which belong to the GGXGXRLXPLX5PK diphosphorylase signature
enzyme in apo form, in complex with substrates mannose-1-phosphate, or with GTP, or bound to the end product GDP-Mannose and Mg2+, sitting drop vapour diffusion method, for apoenzyme: mixing of equal volumes of 20 mg/ml protein in 10 mM Tris, pH 8.0, 150 mM NaCl with reservoir solution containing 35% v/v 2-methyl-2,4-pentanediol, 0.1 M phosphate citrate, pH 7.5, for enzyme complexes: preincubation of 12.5 or 25 mg/ml protein in 10 mM HEPES, pH 7.5, 100 mM NaCl, 10 mM MgCl2, with a 16:1 alpha-D-mannose 1-phosphate or a 8:1 GTP and GDP-Man molar excess of ligand for 30 min at room temperature, protein to well solution ratio of 3:1, the well solution containing 30-35% 2-methyl-2,4-pentanediol, 0.1 M sodium acetate, pH 4.6, 20 mM MgCl2, or in a 2:1 ratio with weel solution containing 30% 2-methyl-2,4-pentanediol, 0.1 M sodium acetate, pH 5.0, 20 mM MgCl2, X-ray diffraction structure determination and analysis at 2.1-2.95 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D27H/V330I
mutation identified in patient with muscular dystrophy
P22S/D334N
mutation identified in patient with muscular dystrophy
R74*/D334N
mutation identified in patient with muscular dystrophy
K175E
approx. 9% of wild-type activity, 600fold increase in Km for mannose 1-phosphate
K175Q
approx. 40% of wild-type activity, 3200fold increase in Km for mannose 1-phosphate
K20Q
enzyme is unable to support alginate synthesis although it shows no significant differences in Vmax and Km as compared to wild-type
R19H
approx. 50% of wild-type activity, 8fold increase in Km for mannose 1-phosphate
R19K
approx. 50% of wild-type activity, 2 and 6fold increase in Km for mannose 1-phosphate and GTP, respectively
R19L
approx. 50% of wild-type activity, 5fold increase in Km for mannose 1-phosphate and GTP, respectively
S12A
approx. 44% of wild-type activity, 2 and 3fold decrease in Km for mannose 1-phosphate and GTP, respectively
additional information
additional information
construction of the conditional inactivation mutant strain YJ-gmpp by replacement of the native Afsrb1 promoter with an inducible Aspergillus nidulans alcA promoter. 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, inactivation phenotype, overview. The alkali-soluble alpha-glucan and alkali-insoluble beta-glucan contents remain unchanged in strain YJ-gmpp depleted of Afsrb1, while the alkali-soluble protein and alkali-insoluble chitin contents are 1.3 and 2.0fold higher, respectively, than those of the wild-type
additional information
-
construction of the conditional inactivation mutant strain YJ-gmpp by replacement of the native Afsrb1 promoter with an inducible Aspergillus nidulans alcA promoter. 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, inactivation phenotype, overview. The alkali-soluble alpha-glucan and alkali-insoluble beta-glucan contents remain unchanged in strain YJ-gmpp depleted of Afsrb1, while the alkali-soluble protein and alkali-insoluble chitin contents are 1.3 and 2.0fold higher, respectively, than those of the wild-type
additional information
-
construction of the conditional inactivation mutant strain YJ-gmpp by replacement of the native Afsrb1 promoter with an inducible Aspergillus nidulans alcA promoter. 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, inactivation phenotype, overview. The alkali-soluble alpha-glucan and alkali-insoluble beta-glucan contents remain unchanged in strain YJ-gmpp depleted of Afsrb1, while the alkali-soluble protein and alkali-insoluble chitin contents are 1.3 and 2.0fold higher, respectively, than those of the wild-type
-
additional information
-
OsMPG1 is localized in the cytoplasm and its overexpression confers salinity stress tolerance in transgenic tobacco
additional information
generation of OsVTC1-1 silenced mutant plants by RNAi method
additional information
generation of OsVTC1-1 silenced mutant plants by RNAi method
additional information
generation of OsVTC1-1 silenced mutant plants by RNAi method
additional information
generation of OsVTC1-3 silenced mutant plants by RNAi method
additional information
generation of OsVTC1-3 silenced mutant plants by RNAi method
additional information
generation of OsVTC1-3 silenced mutant plants by RNAi method
additional information
generation of OsVTC1-8 silenced mutant plants by RNAi method
additional information
generation of OsVTC1-8 silenced mutant plants by RNAi method
additional information
generation of OsVTC1-8 silenced mutant plants by RNAi method
additional information
construction of several truncated mutants of the PH0925 protein, that show altered kinetics compared to the wild-type enzyme, overview
additional information
-
construction of several truncated mutants of the PH0925 protein, that show altered kinetics compared to the wild-type enzyme, overview
-
additional information
-
construction of several truncated mutants of the PH0925 protein, that show altered kinetics compared to the wild-type enzyme, overview
-
additional information
generation of GMP3 overexpressing and RNAi knockdown lines
additional information
-
generation of GMP3 overexpressing and RNAi knockdown lines
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
-
hyperthermostable, the enzyme remains stable for over 300 min without losing its activity when stored at 80°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 3 M ammonium sulfate, 47 d, 40% loss of activity, 122 d, 50% loss of activity
-
frozen, 20 mM Tris-HCl, pH 7.5, 1 mM 2-mercaptoethanol, 1 mM EDTA, several months, no loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
acid treatment, protamine sulfate, ammonium sulfate, DEAE-cellulose, Sephadex G-200, hydroxylapatite, Blue Sepharose
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affinity chromatography using Talon-Co2+ resin, gel filtration
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blue-Sepharose, DEAE-Sepharose, phenyl-Sepharose, agarose-GTP affinity chromatography
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DEAE-52, ammonium sulfate, propyl-agarose, methyl-agrose, Sephadex G-200, hydroxyapatite
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HisTrap Ni affinity column chromatography and Superdex 200 gel filtration
recombinant enzyme from Escherichia coli to homogeneity by glutathione sepharose affinity chromatography
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recombinant enzyme, Q-Sepharose FF, Phenyl-Sepharose, diafiltration, Sephadex G 75, Sephadex G 200, ammonium sulfate
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity
recombinant His-tagged enzyme from Escherichia coli strain Origami (DE3) pLysS by nickel affinity chromatography and gel filtration
recombinant His-tagged PH0925 protein from Escherichia coli strain BL21-Codon Plus(DE3)-RIL by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by metal affinity chromatograhy
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and anaylsis, expression analysis and regulation of the expression, functional expression as GST-tagged enzyme in Escherichia coli strain BL21 under conditions suitable to reduce the formation of inclusion bodies using the vector pTgroE of the yeast Vig9 protein, overview
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells and Arabidopsis thaliana
expression in Escherichia coli
expression of GST-GDPmannose pyrophosphorylase fusion protein in Escherichia coli
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expression of His-tagged enzyme in Escherichia coli strain Origami (DE3) pLysS
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
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expression of wild-type and several PMI-GMP mutants in algA mutant 8853
fused to glutathione S-transferase, expression in Escherichia coli, TOP10F'
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gene bceA, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene bceA, the gene is part of the Burkholderia cepacia IST408 exopolysaccharide biosynthetic cluster, physical organization, unrooted phylogenetic tree, DNA and amino acid sequence determination, analysis, and comparisons, overview. Expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene GMP3, DNA and amino acid sequence determination and analysis, located on chromosome 3, quantitative real-time RT-PCR expression analysis,
gene MPG1, recombinant overexpression in Solanum lycopersicum ripe, fruits show enhanced L-ascorbate levels
gene OsVTC1-1, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene OsVTC1-3, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene OsVTC1-8, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene PH0925, recombinant expression of His-tagged enzyme PH0925 in Escherichia coli strain BL21-Codon Plus(DE3)-RIL
genes OsMPG1, OsMPG2, OsMPG3 and OsMPG4, DNA and amino acid sequence, chromosomal locations, and alternative spliced forms determination and analysis, genetic organization, genomic distribution of MPG genes on rice chromosomes, and phylogenetic analysis, expression analysis, recombinant expression of GFP-tagged full-length MPG1 in Nicotiana tabacum using the Agrobacterium tumefaciens, strain LBA4404, transfection system. Functional complementation of yeast MPG1 YDL055C mutant by expression of OsMPG1, OsMPG2, OsMPG3 and OsMPG4 genes
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His-tagged version expressed in Escherichia coli BL21(DE3)
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overexpression reveals changes in cell wall assembly, restores defects in O-glycosylation, but not those in N-glycosylation, that occur in Kluyveromyces lactis cells depleted for the hexokinase Rag5p, overexpression also enhances heterologous protein secretion in Kluyveromyces lactis
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recombinant functional overexpression of Saccharomyces cerevisiae gene MPG1 in Solanum lycopersicum, fruits show 17-31fold enhanced enzyme activity and L-ascorbate levels
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of isoform VTC1-1 is induced by light
the expression of isoform VTC1-1 is inhibited by dark
the expression of isoform VTC1-3 is quickly induced by dark
the expression of OsVTC1-1 is induced in roots in the light
the expression of OsVTC1-1 is inhibited in roots in the dark
the expression of OsVTC1-3 is induced in roots in the dark
the expression of OsVTC1-3 is inhibited in roots in the light
transcript abundance in all the organs of acerola examined, with the fruit having the highest expression. The relative transcript abundance of Malpighia glabra GDP-D-mannose pyrophosphorylase mRNA levels in the fruits changes as the ripening process progresses, with the unripe green fruits having the highest relative mRNA level, and the lowest is found in the fruits at advanced ripening stage