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Information on EC 2.7.9.2 - pyruvate, water dikinase and Organism(s) Escherichia coli and UniProt Accession P23538
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2.7.9.2 pyruvate, water dikinaseIUBMB Comments
A manganese protein.
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Word Map
- 2.7.9.2
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gluconeogenesis
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carboxykinase
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anaplerotic
- dahp
- pck
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staphylothermus
- drug development
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphoenolpyruvate synthase, phosphoenolpyruvate synthetase, pep synthase, pep synthetase, phosphoenol pyruvate synthetase, water dikinase pyruvate, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
kinase, pyruvate-water di- (phosphorylating)
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PEP synthase
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PEP synthetase
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phosphoenolpyruvate synthase
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phosphoenolpyruvate synthetase
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phosphoenolpyruvic synthase
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phosphopyruvate synthetase, phosphopyruvate
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pyruvate, water dikinase
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pyruvate,water dikinase
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synthetase, phosphopyruvate
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water dikinase pyruvate
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
phosphoenolpyruvate synthase catalyzes the conversion of pyruvate to phosphoenolpyruvate (PEP) using a two-step mechanism invoking a phosphorylated-His intermediate
ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
reaction sequence
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ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
identification of phosphohistidine in phosphoenzyme intermediate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:pyruvate,water phosphotransferase
A manganese protein.
CAS REGISTRY NUMBER
COMMENTARY
9013-09-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 3-fluoropyruvate + H2O
AMP + (Z)-fluorophosphoenolpyruvate + phosphate
stereochemically specific reaction
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r
ATP + 3-fluoropyruvate + H2O
AMP + (Z)-fluorophosphoenolpyruvate + phosphate
10times slower reaction rate than with pyruvate
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r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
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ir
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
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r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
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r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
involved in gluconeogenesis
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r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
essential step in gluconeogenesis if pyruvate or lactate is used as carbon source
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r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
phospho-transfer mechanism, overview
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ir
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
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highly specific
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r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
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phosphorylated enzyme as an intermediate
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r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
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equilibrium lies far to the side of phosphoenolpyruvate formation
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r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
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in the reverse reaction dAMP yields 1% of the rate obtained with AMP, 3'-AMP gives no reaction
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r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
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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
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r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
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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
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r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
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ir
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
involved in gluconeogenesis
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r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
essential step in gluconeogenesis if pyruvate or lactate is used as carbon source
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
Mn2+
additional information
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enzyme contains sulfhydryl groups essential for activity
Mg2+
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divalent metal ion Mg2+ or Mn2+ required for forward reaction
Mn2+
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divalent metal ion Mg2+ or Mn2+ required for forward reaction
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Sodium fluoride
inhibition through the formation of a MgF3- complex within the enzyme active site
Mg2+
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divalent metal ion Mg2+ or Mn2+ required for forward reaction, inhibition at high concentrations of Mg2+ or Mn2+
Mn2+
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divalent metal ion Mg2+ or Mn2+ required for forward reaction, inhibition at high concentrations of Mg2+ or Mn2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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Km-values, both reaction directions, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
the enzyme is essential for growth of Escherichia coli on 3-carbon sources such as pyruvate. The production of phosphoenolpyruvate synthase has also been linked to bacterial virulence and antibiotic resistance
metabolism
formation of phosphoenolpyruvate is an initial step in gluconeogenesis
metabolism
phosphoenolpyruvate produced by the enzyme is required in the shikimate biosynthesis, pathway overview. The expression levels of the enzyme transketolase I (encoded by tktA) and phosphoenolpyruvate synthase (encoded by ppsA) have a critical impact on the phosphoenolpyruvate and erythrose-4-phosphate availability, which are important determinants for in vivo 3-deoxy-D-arabinoheptulosonate-7-phosphate synthase activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
180000
77000
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2 * 77000, enzyme tends to dissociate to monomers at low protein concentration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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2 * 77000, enzyme tends to dissociate to monomers at low protein concentration
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
three critical enzymes of mutated 3-deoxy-D-arabinoheptulosonate-7-phosphate (DAHP) synthase (encoded by aroGfbr), PEP synthase (encoded by ppsA), and transketolase A (encoded by tktA) are modularly overexpressed in Escherichia coli and the resulting recombinant strain produces increased levels of shikimate in an optimized fed-batch fermentation process, overview
additional information
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three critical enzymes of mutated 3-deoxy-D-arabinoheptulosonate-7-phosphate (DAHP) synthase (encoded by aroGfbr), PEP synthase (encoded by ppsA), and transketolase A (encoded by tktA) are modularly overexpressed in Escherichia coli and the resulting recombinant strain produces increased levels of shikimate in an optimized fed-batch fermentation process, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 6.8
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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
22
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retains full activity for several days if stored at room temperature in the presence of EDTA and Mg2+
4
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80% remaining activity after 3 days, 67% remaining activity after 1 month, pH 6.8, inactivation is reversible by prolonged incubation at 30°C
55
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20 min, 17% remaining activity, in presence of 1 M sucrose: 96% remaining activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sucrose, 1.0 M, stabilizes against inactivation by heat, acidic pH, and during storage
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 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
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4°C, 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+
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
gene ppsA, subcloning in Escherichia coli strain JM19, recombinant overexpression in Escherichia coli strain B0013, coexpression with genes aroG and tktA
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
the enzyme is of interest as a target for antibiotic development
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Berman, K.M.; Cohn, M.
Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent metal ions
J. Biol. Chem.
245
5309-5318
1970
Escherichia coli
Berman, K.M.; Cohn, M.
Phosphoenolpyruvate synthetase. Partial reactions studied with adenosine triphosphate analogues and the inorganic phosphate-H2 18O exchange reaction
J. Biol. Chem.
245
5319-5325
1970
Escherichia coli
Cooper, R.A.; Kornberg, H.L.
Net formation of phosphoenolpyruvate from pyruvate by Escherichia coli
Biochim. Biophys. Acta
104
618-620
1965
Escherichia coli
Cooper, R.A.; Kornberg, H.L.
Phosphorylated enzyme as an intermediate in the phosphoenolpyruvate synthase reaction
Biochem. J.
105
49c-50c
1967
Escherichia coli
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Cooper, R.A.; Kornberg, H.L.
Phosphoenolpyruvate synthetase and pyruvate, phosphate dikinase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
10
631-649
1974
Escherichia coli, Escherichia coli B / ATCC 11303
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Chulavatnatol, M.; Atkinson, D.E.
Phosphoenolpyruvate synthetase from Escherichia coli. Effects of adenylate energy charge and modifier concentrations
J. Biol. Chem.
248
2712-2715
1973
Escherichia coli, Escherichia coli B / ATCC 11303
Niersbach, M.; Kreuzaler, F.; Geerse, R.H.; Postma, P.W.; Hirsch, H.J.
Cloning and nucleotide sequence of the Escherichia coli K-12 ppsA gene, encoding PEP synthase
Mol. Gen. Genet.
231
332-336
1992
Escherichia coli (P23538)
Narindrasorasak, S.; Bridger, W.A.
Phosphoenolypyruvate synthetase of Escherichia coli: molecular weight, subunit composition, and identification of phosphohistidine in phosphoenzyme intermediate
J. Biol. Chem.
252
3121-3127
1977
Escherichia coli
Jakeman, D.L.; Evans, J.N.S.
Overexpression, purification, and use of phosphoenol pyruvate synthetase in the synthesis of PEP analogs
Bioorg. Chem.
26
245-253
1998
Escherichia coli (P23538)
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Padilla, L.; Agosin, E.
Heterologous expression of Escherichia coli ppsA (phosphoenolpyruvate synthetase) and galU (UDP-glucose pyrophosphorylase) genes in Corynebacterium glutamicum, and its impact on trehalose synthesis
Metab. Eng.
7
260-268
2005
Escherichia coli (P23538), Escherichia coli
McCormick, N.E.; Jakeman, D.L.
On the mechanism of phosphoenolpyruvate synthetase (PEPs) and its inhibition by sodium fluoride: potential magnesium and aluminum fluoride complexes of phosphoryl transfer
Biochem. Cell Biol.
93
236-240
2015
Escherichia coli (P23538), Escherichia coli
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