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
2.7.9.2
-
RECOMMENDED NAME
GeneOntology No.
pyruvate, water dikinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
mechanism
-
ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
reaction sequence
-
ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
identification of phosphohistidine in phosphoenzyme intermediate
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
kinase, pyruvate-water di- (phosphorylating)
-
-
-
-
PEP synthase
-
-
-
-
PEP synthetase
-
-
-
-
phosphoenolpyruvate synthase
-
-
-
-
phosphoenolpyruvate synthetase
-
-
-
-
phosphoenolpyruvic synthase
-
-
-
-
phosphopyruvate synthetase, phosphopyruvate
-
-
-
-
pyruvate, water dikinase
-
-
-
-
pyruvate,water dikinase
-
-
-
-
synthetase, phosphopyruvate
-
-
-
-
water dikinase pyruvate
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9013-09-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene ppsA
SwissProt
Manually annotated by BRENDA team
gene ppsA; K-12
SwissProt
Manually annotated by BRENDA team
strain Bm, a mutant of strain B devoid of phosphoenolpyruvate carboxylase
-
-
Manually annotated by BRENDA team
Pseudomonas fluorescens ATCC 13525
-
-
-
Manually annotated by BRENDA team
hyperthermophilic archaeon
-
-
Manually annotated by BRENDA team
hyperthermophilic archaeon
-
-
Manually annotated by BRENDA team
Thermococcus kodakarensis KW128
strain KW128
-
-
Manually annotated by BRENDA team
strain Kra1
Uniprot
Manually annotated by BRENDA team
Thermoproteus tenax Kra1
strain Kra1
Uniprot
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
AMP + phosphoenolpyruvate + phosphate
ATP + pyruvate + H2O
show the reaction diagram
-
-
-
-
?
AMP + phosphoenolpyruvate + phosphate
ATP + pyruvate + H2O
show the reaction diagram
P42850
-
-
-
?
AMP + phosphoenolpyruvate + phosphate
ATP + pyruvate + H2O
show the reaction diagram
Pseudomonas fluorescens ATCC 13525
-
-
-
-
?
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
P23538
stereochemically specific reaction, 10times slower reaction rate than with pyruvate
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
-
-
?
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
Q70WQ8
-
-
-
ir
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
P23538
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
P23538
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
highly specific
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
absolutely specific for ATP, highly specific for pyruvate
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
phosphorylated enzyme as an intermediate
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
phosphorylated enzyme as an intermediate
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
equilibrium lies far to the side of phosphoenolpyruvate formation
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
equilibrium lies far to the side of phosphoenolpyruvate formation
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
in the reverse reaction dAMP yields 1% of the rate obtained with AMP, 3'-AMP gives no reaction, enzyme is essential for gluconeogenesis in Escherichia coli and Salmonella typhimurium during the growth on pyruvate, lactate, alanine or serine, in certain circumstances the enzyme may also provide phosphoenolpyruvate under glycolytic conditions
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
involved in gluconeogenesis
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
P23538
involved in gluconeogenesis
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
involved in gluconeogenesis
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
P23538
essential step in gluconeogenesis if pyruvate or lactate is used as carbon source
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
Thermococcus kodakarensis KW128
-
-
-
-
r
additional information
?
-
-
no activity with 2-keto-3-methylvalerate, 2-ketoisocaproate, 2-ketomalonate, phenylpyruvate, hydroxyphenylpyruvate, imidazolpyruvate, and indole-3-pyruvate
-
-
-
additional information
?
-
Q70WQ8
neither GTP, CTP, ITP nor UTP is active as phosphoryl donor
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
enzyme is essential for gluconeogenesis in Escherichia coli and Salmonella typhimurium during the growth on pyruvate, lactate, alanine or serine, in certain circumstances the enzyme may also provide phosphoenolpyruvate under glycolytic conditions
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
involved in gluconeogenesis
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
P23538
involved in gluconeogenesis
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
involved in gluconeogenesis
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
P23538
essential step in gluconeogenesis if pyruvate or lactate is used as carbon source
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
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
Mg2+
-
divalent metal ion Mg2+ or Mn2+ required for forward reaction; inhibition at high concentrations of Mg2+ or Mn2+
Mg2+
-
divalent metal ion Mg2+ or Mn2+ required for forward reaction; Mg2+ is more effective
Mg2+
-
requires divalent cations in the forward reaction, Mg2+ is most effective; slightly inhibitory above 10 mM
Mg2+
Q70WQ8
10 mM, required
Mn2+
-
3 to 4 mol of Mn2+ bound per mol of enzyme; divalent metal ion Mg2+ or Mn2+ required for forward reaction; inhibition at high concentrations of Mg2+ or Mn2+
Mn2+
-
4.2 to 5.6 equivalent binding sites for Mn2+ per mol of enzyme; divalent metal ion Mg2+ or Mn2+ required for forward reaction; Mg2+ is more effective
NH4+
-
48% increased activity at 100 mM
Ni2+
-
requires divalent cations in the forward reaction, 15% of the activity with Mg2+
Mn2+
-
requires divalent cations in the forward reaction, 95% of the activity with Mg2+
additional information
-
enzyme contains sulfhydryl groups essential for activity
additional information
-
Ca2+ and Sr2+ cannot substitute for Mg2+ in the catalytic reaction; not affected by Na+
additional information
Q70WQ8
activity of PEPS does not depend on monovalent cations such as K+ and NH4+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
-
-
2-oxoglutarate
Q70WQ8
strong inhibition at 1 mM
3-phosphoglyceraldehyde
-
-
3-phosphoglyceraldehyde
-
weak
5'-adenylylmethylene diphosphonate
-
competitive to ATP
ADP
Q70WQ8
strong inhibition at 1 mM
ADP-glucose
-
weak
AMP
Q70WQ8
strong inhibition at 1 mM
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+
oxalacetate
-
-
phosphoenolpyruvate
-
competitive to ATP
sulfhydryl reagents
-
-
Mn2+
-
divalent metal ion Mg2+ or Mn2+ required for forward reaction, inhibition at high concentrations of Mg2+ or Mn2+
additional information
-
no inhibition by arsenate
-
additional information
-
not affected by Na+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
IMAGE
1
AMP
-
pH 8.4, 80C
0.028
ATP
-
pH 8.0, 25C
0.39
ATP
-
pH 8.4, 80C
10.5
phosphate
-
pH 6.8, 23C
38.4
phosphate
-
pH 8.4, 80C
0.4
phosphoenolpyruvate
-
pH 8.4, 80C
0.083
pyruvate
-
pH 8.0, 25C
0.11
pyruvate
-
pH 8.4, 80C
0.4
pyruvate
Q70WQ8
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
1
ATP
Q70WQ8
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
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics; Km-values, both reaction directions, overview
-
additional information
additional information
-
kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.7
AMP
-
pH 8.4, 80C
11.9
phosphate
-
pH 8.4, 80C
12.6
phosphoenolpyruvate
-
pH 8.4, 80C
0.683
pyruvate
Q70WQ8
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
1570
pyruvate
-
pH 8.4, 80C
1330
ATP
-
pH 8.4, 80C
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
2-oxoglutarate
Q70WQ8
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
Q70WQ8
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
Q70WQ8
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
LITERATURE
8.9
-
purified enzyme
14.9
-
purified enzyme
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
-
pyruvate formation
7.5
-
at 80C; pyruvate formation
8.4
-
phosphoenolpyruvate formation
9
-
at 80C; phosphoenolpyruvate formation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
assay at
90
-
at pH 8.4; phosphoenolpyruvate formation
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 90
-
optimum at 90C, 0.2% of the optimal activity at 30C
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
5% of total cytoplasmic protein
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Neisseria meningitidis serogroup B (strain MC58)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
87520
-
calculated from amino acid sequence
676074
88000
Q70WQ8
SDS-PAGE, recombinant enzyme, phosphoenzyme intermediate form
676065
90500
Q70WQ8
calculated from amino acid sequence
676065
94000
Q70WQ8
SDS-PAGE, recombinant enzyme, nonphosphorylated form
676065
150000
-
sedimentation equilibrium studies
645475
180000
-
gel filtration
645471
180000
-
-
645472
250000
-
gel filtration
645475
600000
Q70WQ8
above 600000, gel filtration
676065
690000
-
gel filtration
645478
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
P42850
x * 78000, SDS-PAGE
?
P23538
x * 87430, calculation from nucleotide sequence
dimer
-
2 * 77000, enzyme tends to dissociate to monomers at low protein concentration
multimer
-
enzyme forms an unusually large tetraeisosameric complex of 2494 kDa, structure analysis by cryoelectron micrography
multimer
Q70WQ8
native enzyme, gel filtration
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
LITERATURE
phosphoprotein
-
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
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
645475
22
-
retains full activity for several days if stored at room temperature in the presence of EDTA and Mg2+
645470
30
-
stable at
645475
55
-
20 min, 17% remaining activity, in presence of 1 M sucrose: 96% remaining activity
645468
70
-
10 min, no remaining activity
645468
90
-
t1/2: 9 h
645478
additional information
-
slightly cold-labile
645475
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
-
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
recombinant enzyme from overexpression, purification in a single chromatographic step
P23538
Q-sepharose chromatography
Q70WQ8
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
P23538
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
P23538
gene ppsA, overexpression in strain BL21 (DE3)
P23538
expression in Escherichia coli
P42850
expressed in Escherichia coli
-
expressed in Escherichia coli strains DH5alpha and BL21-CodonPlus(DE3)-RIL
Q70WQ8
expressed in Escherichia coli BL21(DE3) cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enhanced transcription of the mfrA gene in the presence of maltose
P42850