Information on EC 2.7.7.13 - mannose-1-phosphate guanylyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
2.7.7.13
-
RECOMMENDED NAME
GeneOntology No.
mannose-1-phosphate guanylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
show the reaction diagram
PMI and GMP activities are most probably located in catalytically distinct domains
P07874
GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
show the reaction diagram
enzyme has both phosphomannose isomerase, i.e. PIM, and guanosine 5'-diphospho-D-mannose pyrophosphorylase, i.e. GMP, activity
P07874, -
GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
show the reaction diagram
bifunctional enzyme with both phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activity
-
GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
alginate biosynthesis I
-
alginate biosynthesis II
-
Amino sugar and nucleotide sugar metabolism
-
Biosynthesis of secondary metabolites
-
Fructose and mannose metabolism
-
GDP-mannose biosynthesis
-
L-ascorbate biosynthesis I (L-galactose pathway)
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
GTP:alpha-D-mannose-1-phosphate guanylyltransferase
The bacterial enzyme can also use ITP and dGTP as donors.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
BceA
-
bifunctional protein with phosphomannose isomerase and GDP-mannose pyrophosphorylase activities
BceA
Burkholderia cepacia IST408
-
bifunctional protein with phosphomannose isomerase and GDP-mannose pyrophosphorylase activities
-
BceA(J) protein
B4EMQ6
-
GDP-alpha-D-mannose pyrophosphorylase
-
-
GDP-D-mannose pyrophosphorylase
B4EMQ6
-
GDP-D-mannose pyrophosphorylase
-, Q06XM8
-
GDP-D-mannose pyrophosphorylase
Burkholderia cepacia IST408
-, Q06XM8
-
-
GDP-D-mannose pyrophosphorylase
-
-
GDP-Man pyrophosphorylase
-
-
GDP-Man pyrophosphorylase
-
-
GDP-Man pyrophosphorylase
-
-
-
GDP-mannose pyrophosphorylase
-
-
-
-
GDP-mannose pyrophosphorylase
-
-
GDP-mannose pyrophosphorylase
O22287, Q8H1Q7, Q9M2S0
-
GDP-mannose pyrophosphorylase
Arabidopsis thaliana Col-0
-
-
-
GDP-mannose pyrophosphorylase
Q4U3E8
-
GDP-mannose pyrophosphorylase
Aspergillus fumigatus YJ-407
Q4U3E8
-
-
GDP-mannose pyrophosphorylase
-
-
GDP-mannose pyrophosphorylase
-
-
GDP-mannose pyrophosphorylase
-
-
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
GDP-mannose pyrophosphorylase
P41940
-
GDP-mannose pyrophosphorylase
Saccharomyces cerevisiae FY23
P41940
-
-
GDP-mannose pyrophosphorylase
-
-
GDP-mannose pyrophosphorylase
-
-
GDP-mannose pyrophosphorylase
-
-
GDP-mannose pyrophosphorylase
-
-
-
GDP-ManPP
-
-
GDP-MP
A4I048
-
GMPase
Arabidopsis thaliana Col-0
-
-
-
GMPase
Saccharomyces cerevisiae FY23
P41940
-
-
GMPP
Aspergillus fumigatus YJ-407
Q4U3E8
-
-
GTP-alpha-D-Man-1-P guanylyltransferase
-
-
GTP-alpha-D-Man-1-P guanylyltransferase
-
-
-
GTP-mannose 1-phosphate guanylyltransferase
-
-
-
-
GTP-mannose-1-phosphate guanylyltransferase
-
-
-
-
guanidine diphosphomannose pyrophosphorylase
B9WNA1
-
guanidine diphosphomannose pyrophoyphorylase
-
-
guanidine diphosphomannose pyrophoyphorylase
-
-
-
guanosine 5'-diphosphate-mannose pyrophosphorylase
-
-
guanosine 5'-diphospho-D-mannose pyrophosphorylase
-
-
-
-
guanosine diphosphomannose pyrophosphorylase
-
-
-
-
guanosine triphosphate-mannose 1-phosphate guanylyltransferase
-
-
-
-
guanosine-diphospho-D-mannose pyrophosphorylase
A4I048
-
guanosine-diphospho-D-mannose pyrophosphorylase
Q9X0C3
-
guanylyltransferase, mannose 1-phosphate
-
-
-
-
mannose 1-phosphate guanylyltransferase (guanosine triphosphate)
-
-
-
-
mannose-1-phosphate guanyl transferase
-
-
mannose-1-phosphate guanylyltransferase
-
-
MPG transferase
O74624
-
PIM-GMP
-
-
-
RfbM
-
enzyme is encoded by the rfbM gene
CAS REGISTRY NUMBER
COMMENTARY
37278-24-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
syncytia induced by nematode Heterodera schachtii
UniProt
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
-
-
-
Manually annotated by BRENDA team
NRRL B1973
-
-
Manually annotated by BRENDA team
Arthrobacter sp. NRRL B1973
NRRL B1973
-
-
Manually annotated by BRENDA team
strain YJ-407, gene Afsrb1
UniProt
Manually annotated by BRENDA team
Aspergillus fumigatus YJ-407
strain YJ-407, gene Afsrb1
UniProt
Manually annotated by BRENDA team
strain J2315, gene bceA
UniProt
Manually annotated by BRENDA team
strain IST408
-
-
Manually annotated by BRENDA team
strain IST408, gene bceA
SwissProt
Manually annotated by BRENDA team
Burkholderia cepacia IST408
strain IST408
-
-
Manually annotated by BRENDA team
Burkholderia cepacia IST408
strain IST408, gene bceA
SwissProt
Manually annotated by BRENDA team
also known as hypocrea jecorina
SwissProt
Manually annotated by BRENDA team
clone JPCM5 (MCAN/ES/98/LLM-877)
UniProt
Manually annotated by BRENDA team
loss of virulence after deletion of GDPmannose pyrophosphorylase gene
-
-
Manually annotated by BRENDA team
acerola
-
-
Manually annotated by BRENDA team
genotypes Pokkali and IR64, gene OsMPG1
-
-
Manually annotated by BRENDA team
enzyme is encoded by the algA gene
SwissProt
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
a S288C strain
SwissProt
Manually annotated by BRENDA team
GDP-mannose pyrophosphorylase is encoded by VIG9
SwissProt
Manually annotated by BRENDA team
Saccharomyces cerevisiae genome database: U24437; overexpression corrects defects in dolichol-linked saccharide formation and protein glycosylation
SwissProt
Manually annotated by BRENDA team
Saccharomyces cerevisiae FY23
a S288C strain
SwissProt
Manually annotated by BRENDA team
strain P2, DSM 1617
-
-
Manually annotated by BRENDA team
strain P2, DSM 1617
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
unrooted relationship tree of MPG proteins from various organisms, phylogenetic analysis, overview
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
Arabidopsis thaliana Col-0
-
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
-
physiological function
B9WNA1, -
essential in bloodstream-form
physiological function
Q9X0C3, -
the enzyme catalyzes the formation of GDP-Man, a fundamental precursor for protein glycosylation and bacterial cell wall and capsular polysaccharide biosynthesis
physiological function
A4I048, -
the GDP-mannose pyrophosphorylase is involved in glycosylation and essential for amastigote survival
metabolism
A4I048, -
the enzyme catalyzes a step in the mannose activation pathways and glycoconjugate biosynthesis in Leishmania, overview
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
Q9X0C3, -
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
A4I048, -
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
P41940
overexpression of GDP-mannose pyrophosphorylase in red fruits of Solanum lycopersicum enhances L-ascorbate levels
additional information
-
overexpression of GDP-mannose pyrophosphorylase from Saccharomyces cerevisiae in red fruits of Solanum lycopersicum enhances L-ascorbate levels
additional information
Saccharomyces cerevisiae FY23
-
overexpression of GDP-mannose pyrophosphorylase in red fruits of Solanum lycopersicum enhances L-ascorbate levels
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
8-Azido-GTP + glucose 1-phosphate
8-Azido-GDPglucose + diphosphate
show the reaction diagram
-
-
-
?
8-Azido-GTP + mannose 1-phosphate
8-Azido-GDP mannose + diphosphate
show the reaction diagram
-
-
-
?
ATP + alpha-D-mannose 1-phosphate
ADPmannose + diphosphate
show the reaction diagram
-
recombinant beta subunit of GDPmannose pyrophosphorylase, 18% of activity with GTP
-
?
ATP + alpha-D-mannose 1-phosphate
alpha-ADP-mannose + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-mannose 1-phosphate
diphosphate + ADP-mannose
show the reaction diagram
B9WNA1, -
-
-
-
-
CTP + alpha-D-mannose 1-phosphate
diphosphate + CDP-alpha-D-mannose
show the reaction diagram
-
recombinant beta subunit of GDPmannose pyrophosphorylase, 7% of activity with GTP
-
?
CTP + alpha-D-mannose 1-phosphate
alpha-CDP-mannose + diphosphate
show the reaction diagram
-
-
-
-
?
D-mannose 1-phosphate + GTP
GDP-D-mannose + diphosphate
show the reaction diagram
-
-
-
-
?
dGTP + alpha-D-mannose 1-phosphate
dGDPmannose + diphosphate
show the reaction diagram
-
8% of activity with GDP-mannose
-
r
dGTP + alpha-D-mannose 1-phosphate
dGDPmannose + diphosphate
show the reaction diagram
-
34% of the activity with GTP
-
?
dGTP + alpha-D-mannose 1-phosphate
dGDPmannose + diphosphate
show the reaction diagram
Arthrobacter sp. NRRL B1973
-
8% of activity with GDP-mannose
-
r
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
show the reaction diagram
-, Q06XM8
-
-
-
?
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
show the reaction diagram
B4EMQ6, -
-
-
-
?
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
show the reaction diagram
Burkholderia cepacia IST408
-, Q06XM8
-
-
-
?
dTTP + alpha-D-mannose 1-phosphate
alpha-dTDP-mannose + diphosphate
show the reaction diagram
-
-
-
-
?
GDP-glucose + diphosphate
D-glucose 1-phosphate + GTP
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
r
GDPmannose + diphosphate
?
show the reaction diagram
-
61% of the activity with GDPglucose
-
-
r
GTP + 2-deoxy-alpha-D-glucose-1-phosphate
GDP-2-deoxy-alpha-D-glucose + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
GTP + 3-deoxy-alpha-D-arabino-hexose-1-phosphate
GDP-3-deoxy-alpha-D-arabino-hexose + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
GTP + 4-deoxy-alpha-D-lyxo-hexose-1-phosphate
GDP-4-deoxy-alpha-D-lyxo-hexose + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
GTP + 6-O-methyl-alpha-D-mannose 1-phosphate
diphosphate + GDP-6-O-methyl-alpha-D-mannose
show the reaction diagram
-
-
-
-
?
GTP + alpha-D-galactose 1-phosphate
GDP-alpha-D-galactose + diphosphate
show the reaction diagram
-
-
-
-
?
GTP + alpha-D-glucosamine 1-phosphate
alpha-GDP-glucosamine + diphosphate
show the reaction diagram
-
-
-
-
?
GTP + alpha-D-glucose 1-phosphate
alpha-GDP-glucose + diphosphate
show the reaction diagram
-
-
-
-
?
GTP + alpha-D-lyxose-1-phosphate
GDPalpha-D-lyxose + diphosphate
show the reaction diagram
-
recombinant GDPmannose pyrophosphorylase, 12% of activity with mannose 1-phosphate
-
?
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
-
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
-
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
P07874
-
-
-
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
P41940
-
-
-
-
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
P41940
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-, O74624
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
O93827
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-, Q9Y725
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
no activity with glucose 1-phosphate, UTP, ATP and CTP
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
P07874, -
no activity with GDP-D-glucose, ADP-D-mannose and UDP-D-mannose
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
specific for mannose, 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
show the reaction diagram
-
equilibrium constant: 2.5
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
enzyme regulates GDP-D-mannose synthesis through feedback inhibition
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
P07874, -
enzyme of alginate biosynthetic pathway
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
O74624
overexpression leads to an increase in cellular GDPmannose levels
-
-
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
Arthrobacter sp. NRRL B1973
-
-, equilibrium constant: 2.5
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
P41940
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
Q9X0C3, -
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
A4I048, -
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
-
regulation of the enzyme expression, overview, 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
show the reaction diagram
Saccharomyces cerevisiae FY23
P41940
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
-
-, regulation of the enzyme expression, overview, 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-alpha-D-mannose
show the reaction diagram
-, Q06XM8
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
show the reaction diagram
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
show the reaction diagram
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
show the reaction diagram
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
show the reaction diagram
-
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
show the reaction diagram
Burkholderia cepacia IST408
-, Q06XM8
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
alpha-GDP-mannose + diphosphate
show the reaction diagram
-
in the presence of diphosphatase
-
-
r
GTP + alpha-D-mannose 1-phosphate + GTP
diphosphate + GDP-alpha-D-mannose
show the reaction diagram
-
-
-
-
?
GTP + alpha-L-fucose 1-phosphate
GDP-alpha-L-fucose + diphosphate
show the reaction diagram
-
-
-
-
?
GTP + alpha-N-acetyl-D-glucosamine 1-phosphate
GDP-alpha-N-acetyl-D-glucosamine + diphosphate
show the reaction diagram
-
-
-
-
?
GTP + D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
-
-
-
-
r
GTP + D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
B9WNA1, -
-
-
-
-
GTP + D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
-
-
-
-
r
IDPmannose + diphosphate
ITP + mannose 1-phosphate
show the reaction diagram
-
72% of activity with GDPglucose
-
r
ITP + alpha-D-mannose 1-phosphate
IDPmannose + diphosphate
show the reaction diagram
-
15-20% of activity with GTP
-
r
ITP + alpha-D-mannose 1-phosphate
IDPmannose + diphosphate
show the reaction diagram
-
44% of the activity with GTP
-
-
ITP + alpha-D-mannose 1-phosphate
IDPmannose + diphosphate
show the reaction diagram
-
ITP is more effective than GTP with mannose 1-phosphate
-
r
ITP + alpha-D-mannose 1-phosphate
IDPmannose + diphosphate
show the reaction diagram
-
11% of activity with GDP-mannose
-
r
ITP + alpha-D-mannose 1-phosphate
IDPmannose + diphosphate
show the reaction diagram
-
recombinant beta subunit of GDPmannose pyrophosphorylase, 20% of activity with GTP
-
-
ITP + alpha-D-mannose 1-phosphate
IDPmannose + diphosphate
show the reaction diagram
Arthrobacter sp. NRRL B1973
-
11% of activity with GDP-mannose
-
r
UTP + alpha-D-mannose 1-phosphate
UDPmannose + diphosphate
show the reaction diagram
-
recombinant beta subunit of GDPmannose pyrophosphorylase, 12% of activity with GTP
-
?
UTP + alpha-D-mannose 1-phosphate
alpha-UDP-mannose + diphosphate
show the reaction diagram
-
-
-
-
?
ITP + glucose 1-phosphate
IDP-glucose + diphosphate
show the reaction diagram
-
-
-
?
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
?
-
-, Q4U3E8
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
?
-
B4EMQ6, -
the enzyme of Burkholderia cenocepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
-
-
-
additional information
?
-
-, Q06XM8
the enzyme of Burkholderia cepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
-
-
-
additional information
?
-
-, Q4U3E8
bifunctional protein, with phosphomannose isomerase and guanosine diphosphate-mannose pyrophosphorylase activities
-
-
-
additional information
?
-
-
GDP-MP high-throughput screening assay method devlopment and evaluation, overview
-
-
-
additional information
?
-
Burkholderia cepacia IST408
-, Q06XM8
the enzyme of Burkholderia cepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
-
-
-
additional information
?
-
Aspergillus fumigatus YJ-407
Q4U3E8
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, bifunctional protein, with phosphomannose isomerase and guanosine diphosphate-mannose pyrophosphorylase activities
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
show the reaction diagram
-, Q06XM8
-
-
-
?
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
show the reaction diagram
B4EMQ6, -
-
-
-
?
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
show the reaction diagram
Burkholderia cepacia IST408
-, Q06XM8
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
-
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
-
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
P07874
-
-
-
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
P41940
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-, O74624
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
O93827
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-, Q9Y725
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
-
enzyme regulates GDP-D-mannose synthesis through feedback inhibition
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
P07874, -
enzyme of alginate biosynthetic pathway
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
O74624
overexpression leads to an increase in cellular GDPmannose levels
-
-
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
P41940
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
Q9X0C3, -
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
A4I048, -
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
-
regulation of the enzyme expression, overview
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
show the reaction diagram
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
Arthrobacter sp. NRRL B1973
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
Saccharomyces cerevisiae FY23
P41940
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
-
-, regulation of the enzyme expression, overview
-
-
r
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
?
-
-, Q4U3E8
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
?
-
B4EMQ6, -
the enzyme of Burkholderia cenocepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
-
-
-
additional information
?
-
-, Q06XM8
the enzyme of Burkholderia cepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
-
-
-
additional information
?
-
Burkholderia cepacia IST408
-, Q06XM8
the enzyme of Burkholderia cepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
-
-
-
additional information
?
-
Aspergillus fumigatus YJ-407
Q4U3E8
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-, Q06XM8
GMP activity is strongly dependent on the presence of Ca2+ or Mn2+; strongly dependent
Ca2+
B4EMQ6, -
GMP activity 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+
-
slight activation at about 10 mM
Co2+
-
divalent cation required for activity, second best activator, maximal activation at 5 mM
Co2+
B4EMQ6, -
activates slightly
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+
Q9X0C3, -
essential divalent cation
Mg2+
P07874, -
Mg2+ or Mn2+ required for activity
Mg2+
-
maximal activation at 5 mM
Mg2+
-
activity depends on the ratio of Mg2+ and GTP, maximum activity at a ratio of about 1
Mg2+
-
divalent cation required for activity, best metal activator Mg2+, maximal activation at 5-10 mM
Mg2+
-
recombinant beta subunit of GDPmannose pyrophosphorylase, 50% of activation with Mn2+
Mg2+
-
required for activity
Mg2+
B4EMQ6, -
activates
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+
-, Q4U3E8
-
Mg2+
B9WNA1, -
absolute requirement for divalent cations, partially replaced by Mn2+ and Cu2+
Mn2+
P07874, -
Mg2+ or Mn2+ required for activity
Mn2+
-
70% of activity with Mg2+, inhibition at 10 mM and higher
Mn2+
-
best metal activator of recombinant beta subunit of GDPmannose pyrophosphorylase, maximal activation at 0.5 mM
Mn2+
-
30% of activity with Mg2+
Mn2+
-, Q06XM8
GMP activity is strongly dependent on the presence of Ca2+ or Mn2+; strongly dependent
Mn2+
B4EMQ6, -
GMP activity is strongly dependent on the presence of Ca2+ or Mn2+, the presence of 5 mM Mn2+, precipitation occurred in the reaction mixture
Ni2+
B4EMQ6, -
activates slightly
Zn2+
-
the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+
Mn2+
-
the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+
additional information
-
recombinant beta subunit of GDPmannose pyrophosphorylase is not activated by Co2+, Zn2+, Cu2+ and Fe2+
additional information
-, Q06XM8
no activation and activity by Ni2+, Mg2+, and Zn2+
additional information
B4EMQ6, -
descending order of activation Mg2+, Ca2+, Mn2+, Co2+, Ni2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
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-[2-(4-methoxyphenyl)ethyl]-2H-1,2,4-benzothiadiazine 1,1-dioxide
-
-
4-(4-benzylpiperazin-1-yl)-7-chloroquinoline
-
-
4-[4-(4-tert-butylbenzyl)piperazin-1-yl]-7-chloroquinoline
-
-
4-[4-(biphenyl-4-ylmethyl)piperazin-1-yl]-7-chloroquinoline
-
-
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
-
-
ammonium sulfate
-
-
diphosphate
-
strong product inhibition
ethyl (2Z)-(hydroxyimino)(1H-tetrazol-5-yl)ethanoate
-
-
GDP
-
0.4 mM, 50% inhibition
GDP-6-deoyxmannose
B9WNA1, -
-
GDP-glucose
-
inhibition of GDP-mannose phosphorolysis
GDP-glucose
-
2.5 mM, 50% inhibition
GDP-mannose
-
competitive vs. GTP, uncompetitive vs. mannose 1-phosphate
GDP-mannose
-
-
GDP-mannose
-
noncompetitive inhibition of GDP-glucose phosphorolysis
GDP-mannose
-
strong product inhibition
GDP-mannose
B9WNA1, -
feedback inhibition
glucose 1-phosphate
-
inhibition of GDP-mannose phosphorolysis
glucose 1-phosphate
-
10 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
-
-
[4-(7-chloroquinolin-4-yl)piperazin-1-yl](4-methylphenyl)methanone
-
-
additional information
P07874, -
not inhibited by dithiothreitol up to 5 mM
-
additional information
-
high-throughput GDP-MP inhibitor large-scale screening, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
41.1
-
2-deoxy-D-glucose 1-phosphate
-
pH 8.0, 25C, recombinant enzyme
15.2
-
3-deoxy-D-arabino-hexose 1-phosphate
-
pH 8.0, 25C, recombinant enzyme
0.94
-
4-deoxy-D-lyxo-hexose 1-phosphate
-
pH 8.0, 25C, recombinant enzyme
0.29
-
ATP
B9WNA1, -
-
0.094
-
D-glucose 1-phosphate
-
cosubstrate GTP, Vmax: 14 micromol/min/mg
0.012
-
D-mannose 1-phosphate
B9WNA1, -
-
0.0205
-
D-mannose 1-phosphate
P07874, -
pH 8.0, 25C
0.062
-
D-mannose 1-phosphate
-
cosubstrate GTP, Vmax: 0.63 micromol/min/mg
0.063
-
D-mannose 1-phosphate
-
GDP-mannose synthesis
0.072
-
D-mannose 1-phosphate
-
cosubstrate GTP, Vmax: 50 micromol/min/mg
0.12
-
D-mannose 1-phosphate
-
cosubstrate ATP, Vmax: 11 micromol/min/mg
0.15
-
D-mannose 1-phosphate
-
cosubstrate UTP, Vmax: 14 micromol/min/mg
0.16
-
D-mannose 1-phosphate
-
cosubstrate CTP, Vmax: 11 micromol/min/mg
0.19
-
D-mannose 1-phosphate
-
cosubstrate TTP, Vmax: 6 micromol/min/mg
0.12
-
dGDP-mannose
-
pH 8.2, 37C
0.089
-
diphosphate
-
pyrophosphorolysis
0.09
-
diphosphate
-
pH 8.2, 37C
0.33
-
diphosphate
-
pH 7.5, 37C, cosubstrate GDPglucose
0.356
-
diphosphate
-
pH 7.5, 37C, cosubstrate GDPmannose
0.5
-
diphosphate
-
pH 7.5, 37C, cosubstrate GDPmannose
2.9
-
diphosphate
-, Q06XM8
in the presence of 10 mM Mn2+
0.001
-
GDP-alpha-D-mannose
-
pH 7.8, 37C
0.024
-
GDP-mannose
B4EMQ6, -
pH 7.6, recombinant enzyme, in presence of 5 mM Mg2+ and 2 mM diphosphate
0.052
-
GDP-mannose
-
pH 8.2, 37C
0.202
-
GDP-mannose
-
pyrophosphorolysis
2.9
-
GDP-mannose
-, Q06XM8
pH 7.6, recombinant enzyme, presence of 10 mM Mn2+
0.000039
-
GDPmannose
-
pH 7.5, 37C, recombinant beta subunit of GDPmannose pyrophosphorylase, cosubstrate diphosphate
0.0142
-
GDPmannose
P07874, -
pH 7.0, 25C
0.02
-
GDPmannose
-
pH 7.5, 37C
0.1
-
GDPmannose
-
pH 8.0, 37C, cosubstrate diphosphate
0.14
-
GDPmannose
-
pH 7.5, 37C, cosubstrate diphosphate
0.78
-
GDPmannose
P41940
pH 7.8, 37C
2.85
-
glucose 1-phosphate
-
pH 7.5, 37C, cosubstrate GTP
0.0035
-
GTP
-
pH 7.8, 37C
0.0295
-
GTP
P07874, -
pH 8.0, 25C
0.04
-
GTP
-
pH 8.0, 25C
0.041
-
GTP
P07874
25C, cosubstrate mannose 1-phosphate
0.067
-
GTP
B9WNA1, -
-
0.1
-
GTP
-
pH 7.5, 37C, cosubstrate mannose 1-phosphate
0.113
-
GTP
-
pH 7.5, 37C, cosubstrate mannose 1-phosphate
0.13
-
GTP
-
pH 8.2, 37C
0.236
-
GTP
-
GDP-mannose synthesis
0.36
-
GTP
-
pH 7.5, 37C, recombinant beta subunit of GDPmannose pyrophosphorylase, cosubstrate mannose 1-phosphate
1
-
GTP
-
pH 7.5, 37C, cosubstrate glucose 1-phosphate
1
-
GTP
-
pH 7.8, 37C, cosubstrate diphosphate
3.3
-
IDP-mannose
-
pH 8.2, 37C
0.28
-
ITP
-
pH 8.2, 37C
13.8
-
lyxose 1-phosphate
-
pH 8.0, 25C, recombinant enzyme
0.0004
-
mannose 1-phosphate
-
pH 7.8, 37C
0.0082
-
mannose 1-phosphate
P07874
25C, cosubstrate GTP
0.01
-
mannose 1-phosphate
-
-
0.014
-
mannose 1-phosphate
-
pH 8.0, 25C, recombinant enzyme
0.015
-
mannose 1-phosphate
-
pH 8.0, 25C
0.022
-
mannose 1-phosphate
-
pH 8.0, 37C, cosubstrate GTP
0.035
-
mannose 1-phosphate
-
pH 8.2, 37C
0.13
-
mannose 1-phosphate
-
pH 7.5, 37C, cosubstrate GTP
0.168
-
mannose 1-phosphate
-
pH 7.5, 37C, cosubstrate GTP
0.2
-
mannose 1-phosphate
-
pH 7.5, 37C, recombinant beta subunit of GDPmannose pyrophosphorylase, cosubstrate GTP
0.002
-
Mg2+
-
pH 8.0, 25C
0.466
-
Mg2+
-
GDP-mannose synthesis; pyrophosphorolysis
1.9
-
Mg2+
-
pH 8.2, 37C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6.85
-
diphosphate
-, Q06XM8
in the presence of 10 mM Mn2+
195.9
-
diphosphate
-, Q06XM8
in the presence of 10 mM Mn2+
195.9
-
GDP-mannose
-, Q06XM8
pH 7.6, recombinant enzyme, presence of 10 mM Mn2+
22.1
-
GDPmannose
-
pH 8.0, 37C, cosubstrate diphosphate
10.3
-
mannose 1-phosphate
-
pH 8.0, 37C, cosubstrate GTP
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.85
-
ammonium sulfate
-
-
0.016
-
diphosphate
-
pH 8.0, 25C
11
-
GDP-glucose
-
pH 7.5, 37C
0.00125
-
GDP-mannose
B9WNA1, -
competitive inhibitor with respect to GTP
0.002
-
GDP-mannose
B9WNA1, -
mixed-type inhibition with respect to mannose 1-phosphate
0.009
-
GDP-mannose
-
pH 8.0, 25C
0.015
-
GDP-mannose
-
competitive vs. GTP
0.024
-
GDP-mannose
-
pH 7.5, 37C
0.12
-
GDP-mannose
-
uncompetitive vs. mannose 1-phosphate
2.5
-
glucose 1-phosphate
-
pH 7.5, 37C
0.06
-
mannose 1-phosphate
-
pH 7.5, 37C
0.001
-
Mg2+
-
pH 8.0, 25C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.013
-
GDP-6-deoxymannose
B9WNA1, -
-
0.008
-
GDP-mannose
B9WNA1, -
feedback inhibition
additional information
-
additional information
B9WNA1, -
IC50 values for ATP and CTP above 0.625 mM
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.34
-
B9WNA1, -
-
2.75
-
-
recombinant enzyme
9.25
-
-
-
24.1
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
7.5
-
GTP synthesis
6
7.5
-
-
6
8.5
-
GDPmannose synthesis
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
9
-
GTP synthesis
7
-
-
GDP-mannose synthesis, forward reaction is very sensitive to pH fluctuation
7.5
-
-
reverse reaction, assay at
7.5
-
-, Q4U3E8
assay at
7.5
-
-
assay at
7.5
-
P41940
assay at
7.5
-
-
assay at
7.6
-
-
forward reaction, assay at
7.6
-
-, Q06XM8
assay at
7.6
-
B4EMQ6, -
assay at
8.2
-
-
assay at
additional information
-
B9WNA1, -
neutral pH optimum
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-, Q4U3E8
assay at
35
-
-
forward reaction, assay at
37
-
P07874, -
assay at
37
-
-
assay at
37
-
-
assay at
60
-
-
reverse reaction, assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
100
-
temperature dependence of the enzymatic activity is analyzed between 0 and 100C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.03
-
-, Q06XM8
calculated from amino acid sequence
6.45
-
-
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
low enzyme activity levels in green and red fruits
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
-
-
-
Manually annotated by BRENDA team
O22287, Q8H1Q7, Q9M2S0
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
expression of genes OsMPG1, OsMPG2, OsMPG3 and OsMPG4
Manually annotated by BRENDA team
B9WNA1, -
in bloodstream-form
Manually annotated by BRENDA team
-
expression of genes OsMPG1, OsMPG2, OsMPG3 and OsMPG4
Manually annotated by BRENDA team
-
expression of gene OsMPG2
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
39700
-
-
calculated from amino acid sequence
40520
-
-
calculated from amino acid sequence
42000
-
-
SDS-PAGE
53000
-
-
SDS-PAGE
54000
-
P07874, -
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
-
-, Q06XM8
SDS-PAGE
70000
-
-
gel filtration
108000
-
-
recombinant enzyme, gel filtration
412000
-
-
sucrose velocity sedimentation
450000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 37000 + x * 43000 SDS-PAGE
?
P41940
x * 39565, deduced from nucleotide sequence
?
O93827
x * 39974, deduced from nucleotide sequence
?
-, Q9Y725
x * 39298, deduced from nucleotide sequence
?
-
x * 46400, deduced from nucleotide sequence
?
-
x * 55000, SDS-PAGE; x * 55303, deduced from nucleotide sequence
?
-
x * 42000, SDS-PAGE
?
B4EMQ6, -
x * 56000, recombinant enzyme, SDS-PAGE, x * 55716, sequence caculation
?
-
x * 42000, SDS-PAGE
-
dimer
-
2 * 54045, recombinant enzyme, deduced from nucleotide sequence; 2 * 55000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 37000, SDS-PAGE
dimer
-
2 * 45000, His-tagged version, gel filtration, SDS-PAGE
homodimer
B9WNA1, -
2 * 42000, SDS-PAGE, 2 * 41769.10, ESI-MS (41769.32 theoretical mass)
monomer
P07874, -
1 * 56000, SDS-PAGE
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
B4EMQ6, -
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
Q9X0C3, -
the enzyme has two separate domains: a N-terminal Rossman fold-like domain and a C-terminal left-handed beta-helix domain
additional information
-
domain organization, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
Q9X0C3, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
7.7
-
most stable at
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
48
-
-
30 min, 50% loss of activity
80
-
-
hyperthermostable, the enzyme remains stable for over 300 min without losing its activity when stored at 80C
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0C, 1 week, 50% loss of activity
-
frozen, several months, little loss of activity
-
4C, 25% glycerol, 47 d, 25% loss of activity
-
4C, 3 M ammonium sulfate, 47 d, 40% loss of activity, 122 d, 50% loss of activity
-
4C, ammonium sulfate suspension, several months, no loss of activity
-
4C, stable for a few days, purified enzyme
-
frozen, 20 mM Tris-HCl, pH 7.5, 1 mM 2-mercaptoethanol, 1 mM EDTA, several months, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
protamine sulfate, Sephadex G-25, DEAE-cellulose
-
recombinant enzyme from Escherichia coli strain BL21(DE3)
-, Q4U3E8
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity
B4EMQ6, -
Hi-Trap column chromatography; recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-, Q06XM8
recombinant enzyme, Ni-nitrilotriacetic acid column, Superdex 200
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by metal affinity chromatograhy
-
affinity chromatography using Talon-Co2+ resin, gel filtration
-
DEAE-52, ammonium sulfate, propyl-agarose, methyl-agrose, Sephadex G-200, hydroxyapatite
-
Biogel, Q-Sepharose, Sephacryl-200
P07874, -
Ni-affinity column
-
GST-fusion protein, glutathione-Sepharose 4B beads
P41940
recombinant enzyme, Q-Sepharose FF, Phenyl-Sepharose, diafiltration, Sephadex G 75, Sephadex G 200, ammonium sulfate
-
recombinant enzyme, ultrafiltration, Q-Sepharose
-
recombinant enzyme from Escherichia coli to homogeneity by glutathione sepharose affinity chromatography
-
acid treatment, protamine sulfate, ammonium sulfate, DEAE-cellulose, Sephadex G-200, hydroxylapatite, Blue Sepharose
-
blue-Sepharose, DEAE-Sepharose, phenyl-Sepharose, agarose-GTP affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain Origami (DE3) pLysS by nickel affinity chromatography and gel filtration
Q9X0C3, -
batch absorption to nickel-agarose
B9WNA1, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens
O22287, Q8H1Q7, Q9M2S0
gene Afsrb1, expression in Escherichia coli strain BL21(DE3)
-, Q4U3E8
gene bceA, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
B4EMQ6, -
expressed in Escherichia coli BL21(DE3) cells; 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)
-, Q06XM8
expression in Escherichia coli
O93827
expression in Escherichia coli
-, Q9Y725
expression in Escherichia coli
-
cloning of cDNA
-, O74624
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
-
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
-
His-tagged version expressed in Escherichia coli BL21(DE3)
-
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
-
expression of wild-type and several PMI-GMP mutants in algA mutant 8853
P07874
expressed in Escherichia coli BL21 Codon Plus (DE3)-RIPL strain
-
expression of GST-fusion protein in Escherichia coli
P41940
gene MPG1, recombinant overexpression in Solanum lycopersicum ripe, fruits show enhanced L-ascorbate levels
P41940
expression in Escherichia coli strain BL21(DE3)pLysS
-
overexpression in Escherichia coli
-
recombinant functional overexpression of Saccharomyces cerevisiae gene MPG1 in Solanum lycopersicum, fruits show 17-31fold enhanced enzyme activity and L-ascorbate levels
-
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; fused to glutathione S-transferase, expression in Escherichia coli, TOP10F'
-
expression of GST-GDPmannose pyrophosphorylase fusion protein in Escherichia coli
-
expression of His-tagged enzyme in Escherichia coli strain Origami (DE3) pLysS
Q9X0C3, -
His tagged version expressed in Escherichia coli BL21
B9WNA1, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K175E
P07874
approx. 9% of wild-type activity, 600fold increase in Km for mannose 1-phosphate
K175Q
P07874
approx. 40% of wild-type activity, 3200fold increase in Km for mannose 1-phosphate
K175R
P07874
470fold increase in mannose 1-phosphate Km value
K20Q
P07874
enzyme is unable to support alginate synthesis although it shows no significant differences in Vmax and Km as compared to wild-type
R19H
P07874
approx. 50% of wild-type activity, 8fold increase in Km for mannose 1-phosphate
R19K
P07874
approx. 50% of wild-type activity, 2 and 6fold increase in Km for mannose 1-phosphate and GTP, respectively
R19L
P07874
approx. 50% of wild-type activity, 5fold increase in Km for mannose 1-phosphate and GTP, respectively
S12A
P07874
approx. 44% of wild-type activity, 2 and 3fold decrease in Km for mannose 1-phosphate and GTP, respectively
additional information
-, Q4U3E8
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
Aspergillus fumigatus YJ-407
-
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
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
to homogeneity
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
B4EMQ6, -
the enzyme is a potential target for antimicrobial drug design, i.e. in the treatment of cystic fibrosis caused by Burkholderia cenocepacia
drug development
A4I048, -
the enzyme is a target for inhibitor design for anti-leishmanial therapy
synthesis
-
an N-acetylhexosamine 1-kinase from Bifidobacterium infantis (NahK_15697), a guanosine 5'-diphosphate (GDP)-mannose pyrophosphorylase from Pyrococcus furiosus (PFManC), and an Escherichia coli inorganic pyrophosphatase (EcPpA) are used efficiently for a one-pot three enzyme synthesis of GDP-mannose, GDP-glucose, their derivatives, and GDP-talose from simple monosaccharides and derivatives in preparative scale
synthesis
-
enzyme can be used for the synthesis of GDPmannose deoxy derivatives