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 ACCESSION NO.
LITERATURE
ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
reaction sequence
-
ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
mechanism; reaction sequence
-
ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
identification of phosphohistidine in phosphoenzyme intermediate
-
ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Carbon fixation pathways in prokaryotes
-
gluconeogenesis I
-
glycolysis I (from glucose-6P)
-
glycolysis II (from fructose-6P)
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
kinase, pyruvate-water di- (phosphorylating)
-
-
-
-
mlrA
P42850
gene name
PEP synthase
P42850
-
PEP synthase
Thermococcus kodakarensis KW128
-
-
-
PEP synthase
-
-
-
-
PEP synthetase
-
-
-
-
PEP synthetase
-
-
PEPS
Pseudomonas fluorescens ATCC 13525
-
-
-
PEPS
-
-
phoephoenolpyruvate synthase
-
-
phoephoenolpyruvate synthase
Pseudomonas fluorescens ATCC 13525
-
-
-
phosphoenol pyruvate synthetase
P23538
-
phosphoenolpyruvate synthase
-
-
-
-
phosphoenolpyruvate synthase
P42850
-
phosphoenolpyruvate synthase
-
-
phosphoenolpyruvate synthase
Thermococcus kodakarensis KW128
-
-
-
phosphoenolpyruvate synthetase
-
-
-
-
phosphoenolpyruvate synthetase
P23538
-
phosphoenolpyruvate synthetase
-
-
phosphoenolpyruvate synthetase
-
-
phosphoenolpyruvic synthase
-
-
-
-
phosphopyruvate synthetase, phosphopyruvate
-
-
-
-
Pps
Thermococcus kodakarensis KW128
-
-
-
PpsA
P23538
-
pyruvate, water dikinase
-
-
-
-
pyruvate,water dikinase
-
-
-
-
synthetase, phosphopyruvate
-
-
-
-
TK1292
Thermococcus kodakarensis KW128
-
-
-
water dikinase pyruvate
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9013-09-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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 ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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+
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 ACCESSION NO.
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
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]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.9
-
-
purified enzyme
14.9
-
-
purified enzyme
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
-
-
pyruvate formation
6.8
-
P23538
pyruvate formation
7.5
-
-
at 80C; pyruvate formation
8.4
-
-
phosphoenolpyruvate formation
8.4
-
P23538
phosphoenolpyruvate formation
9
-
-
at 80C; phosphoenolpyruvate formation
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
90
-
-
at pH 8.4; phosphoenolpyruvate formation
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
90
-
optimum at 90C, 0.2% of the optimal activity at 30C
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
87520
-
-
calculated from amino acid sequence
88000
-
Q70WQ8, -
SDS-PAGE, recombinant enzyme, phosphoenzyme intermediate form
90500
-
Q70WQ8, -
calculated from amino acid sequence
94000
-
Q70WQ8, -
SDS-PAGE, recombinant enzyme, nonphosphorylated form
150000
-
-
sedimentation equilibrium studies
180000
-
-
gel filtration
180000
-
-
-
250000
-
-
gel filtration
600000
-
Q70WQ8, -
above 600000, gel filtration
690000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
P23538
x * 87430, calculation from nucleotide sequence
?
P42850
x * 78000, SDS-PAGE
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 ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
6.8
-
purified enzyme, most stable at, rapid loss of activity above pH 6.8 and below pH 5.5
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
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 ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
LITERATURE
recombinant enzyme from overexpression, purification in a single chromatographic step
P23538
Q-sepharose chromatography
Q70WQ8, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
enhanced transcription of the mfrA gene in the presence of maltose
P42850