Information on EC 2.7.9.2 - pyruvate, water dikinase

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

EC NUMBER
COMMENTARY hide
2.7.9.2
-
RECOMMENDED NAME
GeneOntology No.
pyruvate, water dikinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Carbon fixation pathways in prokaryotes
-
-
gluconeogenesis
-
-
gluconeogenesis I
-
-
glycolysis I (from glucose 6-phosphate)
-
-
glycolysis II (from fructose 6-phosphate)
-
-
Metabolic pathways
-
-
Methane metabolism
-
-
Microbial metabolism in diverse environments
-
-
Pyruvate metabolism
-
-
reductive TCA cycle I
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:pyruvate,water phosphotransferase
A manganese protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9013-09-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
hyperthermophilic archaeon
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain KW128
-
-
Manually annotated by BRENDA team
strain KW128
-
-
Manually annotated by BRENDA team
strain Kra1
Uniprot
Manually annotated by BRENDA team
strain Kra1
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
AMP + phosphoenolpyruvate + phosphate
ATP + pyruvate + H2O
show the reaction diagram
ATP + 2-ketobutyrate + H2O
?
show the reaction diagram
-
8% of the activity with pyruvate
-
-
?
ATP + 2-oxoglutarate + H2O
?
show the reaction diagram
-
2% of the activity with pyruvate
-
-
?
ATP + 3-fluoropyruvate + H2O
AMP + (Z)-fluorophosphoenolpyruvate + phosphate
show the reaction diagram
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
enzyme contains 1 Ca atom per subunit
Co2+
-
requires divalent cations in the forward reaction, 93% of the activity with Mg2+
Iron
-
0.1-0.4 g-atoms per subunit, no functional part of the enzyme
K+
-
50% increased activity at 100 mM
NH4+
-
48% increased activity at 100 mM
Ni2+
-
requires divalent cations in the forward reaction, 15% of the activity with Mg2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
3-phosphoglyceraldehyde
5'-adenylylmethylene diphosphonate
-
competitive to ATP
ADP-glucose
-
weak
ATP
-
excess of ATP inhibits at high concentrations of MgCl2 or MnCl2
Ca2+
-
inhibits Mn2+-activated enzyme
iodoacetate
-
-
Mg2+
-
divalent metal ion Mg2+ or Mn2+ required for forward reaction, inhibition at high concentrations of Mg2+ or Mn2+
Mn2+
-
divalent metal ion Mg2+ or Mn2+ required for forward reaction, inhibition at high concentrations of Mg2+ or Mn2+
oxalacetate
-
-
phosphoenolpyruvate
-
competitive to ATP
sulfhydryl reagents
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
the DUF99-encoded protein catalyzes both the ADP-dependent inactivation and the Pi-dependent activation of phosphoenolpyruvate synthetase
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
AMP
-
pH 8.4, 80C
0.028 - 1
ATP
10.5 - 38.4
phosphate
0.4
phosphoenolpyruvate
-
pH 8.4, 80C
0.083 - 0.54
pyruvate
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.7
AMP
Pyrococcus furiosus
-
pH 8.4, 80C
0.25 - 1330
ATP
11.9
phosphate
Pyrococcus furiosus
-
pH 8.4, 80C
12.6
phosphoenolpyruvate
Pyrococcus furiosus
-
pH 8.4, 80C
0.41 - 1570
pyruvate
additional information
additional information
Escherichia coli
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.53
ATP
Sulfolobus solfataricus
Q97V40
65C, pH not specified in the publication; 70C, pH not specified in the publication
4
0.75 - 1.04
pyruvate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
2-oxoglutarate
in 100 mM Tris/HCl, pH 7.0, in the presence of 20 mM beta-mercaptoethanol, 6 mM pyruvate, 10 mM ATP and 10 mM MgCl2, at 70C
0.0021
5'-adenylylmethylene diphosphonate
-
pH 6.8
2.6
ADP
in 100 mM Tris/HCl, pH 7.0, in the presence of 20 mM beta-mercaptoethanol, 6 mM pyruvate, 10 mM ATP and 10 mM MgCl2, at 70C
0.5
AMP
in 100 mM Tris/HCl, pH 7.0, in the presence of 20 mM beta-mercaptoethanol, 6 mM pyruvate, 10 mM ATP and 10 mM MgCl2, at 70C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.9
-
purified enzyme
14.9
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
at 80C; pyruvate formation
9
-
at 80C; phosphoenolpyruvate formation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
90
-
at pH 8.4; phosphoenolpyruvate formation
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 90
-
optimum at 90C, 0.2% of the optimal activity at 30C
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
5% of total cytoplasmic protein
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Neisseria meningitidis serogroup B (strain MC58)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
87520
-
calculated from amino acid sequence
88000
SDS-PAGE, recombinant enzyme, phosphoenzyme intermediate form
90500
calculated from amino acid sequence
94000
SDS-PAGE, recombinant enzyme, nonphosphorylated form
150000
-
sedimentation equilibrium studies
180000
250000
-
gel filtration
600000
above 600000, gel filtration
690000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 77000, enzyme tends to dissociate to monomers at low protein concentration
multimer
octamer
-
8 * 92000, SDS-PAGE, 30% of the enzyme is purified as a large inactive complex of about 1640 kDa
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6.8
-
purified enzyme, most stable at, rapid loss of activity above pH 6.8 and below pH 5.5
645468, 645472
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
80% remaining activity after 3 days, 67% remaining activity after 1 month, pH 6.8, inactivation is reversible by prolonged incubation at 30C
22
-
retains full activity for several days if stored at room temperature in the presence of EDTA and Mg2+
30
-
stable at
55
-
20 min, 17% remaining activity, in presence of 1 M sucrose: 96% remaining activity
70
-
10 min, no remaining activity
90
-
t1/2: 9 h
additional information
-
slightly cold-labile
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol stabilizes the purified enzyme
-
KCl destabilizes
-
sucrose, 1.0 M, stabilizes against inactivation by heat, acidic pH, and during storage
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 10 mM Tris-HCl buffer, pH 6.8, containing 1 M sucrose, 0.2 mM EDTA, 0.2 mM dithioerythritol, no loss of activity after 1 year
-
4C, dephosphorylated form of enzyme, 50 mM Tris/HCl, pH 6.8, 0.2 mM EDTA, 0.2 mM DTT, 1 M sucrose, stable over a period of 12 months
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unstable if stored in ice, but retains full activity for several days if stored at room temperature in the presence of EDTA and Mg2+
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Q-sepharose chromatography
recombinant enzyme from overexpression, purification in a single chromatographic step
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, sequence homology with other phosphohistidine-containing enzymes, including pyruvate,phosphate dikinase from plants and Bacteroides symbiosus and Enzyme I of the bacterial PEP:carbohydrate phosphotransferase system
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli strains DH5alpha and BL21-CodonPlus(DE3)-RIL
expression in Corynebacterium glutamicum. Simultaneous expression of phosphoenolpyruvate synthetase and UDP-glucose diphosphorylase does not result in a further increases in trehalose yield compared to expression of UDP-glucose phosphorylase alone
expression in Escherichia coli
gene ppsA, overexpression in strain BL21 (DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enhanced transcription of the mfrA gene in the presence of maltose
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