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Information on EC 2.7.9.2 - pyruvate, water dikinase
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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
-
gluconeogenesis
-
carboxykinase
-
anaplerotic
- dahp
- pck
-
staphylothermus
- drug development
The enzyme appears in viruses and cellular organisms
Synonyms
phosphoenolpyruvate synthase, phosphoenolpyruvate synthetase, pep synthase, pep synthetase, phosphoenol pyruvate synthetase, water dikinase pyruvate, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
kinase, pyruvate-water di- (phosphorylating)
-
-
-
-
PEP synthase
PEP synthase
-
-
-
-
PEP synthetase
PEPS
phosphoenolpyruvate synthase
phosphoenolpyruvate synthetase
phosphoenolpyruvic synthase
-
-
-
-
phosphopyruvate synthetase, phosphopyruvate
-
-
-
-
Pps
PpsA
pyruvate, water dikinase
-
-
-
-
pyruvate,water dikinase
-
-
-
-
SSO2792
synthetase, phosphopyruvate
-
-
-
-
TK1292
water dikinase pyruvate
-
-
-
-
PEP synthetase
-
-
-
-
phosphoenolpyruvate synthase
-
-
-
-
phosphoenolpyruvate synthetase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
reaction sequence
-
ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
identification of phosphohistidine in phosphoenzyme intermediate
-
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
mechanism
Escherichia coli B / ATCC 11303
-
-
ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
reaction sequence
Escherichia coli B / ATCC 11303
-
-
ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
-
-
-
-
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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.
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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
AMP + phosphoenolpyruvate + phosphate
ATP + pyruvate + H2O
-
-
-
-
?
AMP + phosphoenolpyruvate + phosphate
ATP + pyruvate + H2O
-
the enzyme is involved in the production of pyruvate, phosphoenolpyruvate and ATP from glycerol in Pseudomonas fluorescens
-
-
?
AMP + phosphoenolpyruvate + phosphate
ATP + pyruvate + H2O
-
-
-
-
?
AMP + phosphoenolpyruvate + phosphate
ATP + pyruvate + H2O
-
the enzyme is involved in the production of pyruvate, phosphoenolpyruvate and ATP from glycerol in Pseudomonas fluorescens
-
-
?
AMP + phosphoenolpyruvate + phosphate
ATP + pyruvate + H2O
-
-
-
-
?
AMP + phosphoenolpyruvate + phosphate
ATP + pyruvate + H2O
-
-
-
?
AMP + phosphoenolpyruvate + phosphate
ATP + pyruvate + H2O
-
CMP, GMP, IMP, UMP, CDP, GDP, IDP, and UDP are inert as the acceptor. Diphosphate can not be substituted for phosphate. The enzyme does not catalyze the diphosphate-dependent formation of pyruvate from phosphoenolpyruvate and AMP
-
-
r
ATP + 3-fluoropyruvate + H2O
AMP + (Z)-fluorophosphoenolpyruvate + phosphate
stereochemically specific reaction
-
r
ATP + 3-fluoropyruvate + H2O
AMP + (Z)-fluorophosphoenolpyruvate + phosphate
10times slower reaction rate than with pyruvate
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
-
-
ir
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
highly specific
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
phosphorylated enzyme as an intermediate
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
equilibrium lies far to the side of phosphoenolpyruvate formation
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
in the reverse reaction dAMP yields 1% of the rate obtained with AMP, 3'-AMP gives no reaction
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
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
involved in gluconeogenesis
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
essential step in gluconeogenesis if pyruvate or lactate is used as carbon source
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
phospho-transfer mechanism, overview
-
-
ir
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
Escherichia coli B / ATCC 11303
-
highly specific
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
Escherichia coli B / ATCC 11303
-
in the reverse reaction dAMP yields 1% of the rate obtained with AMP, 3'-AMP gives no reaction
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
Escherichia coli B / ATCC 11303
-
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
-
-
-
?
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
absolutely specific for ATP, highly specific for pyruvate
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
phosphorylated enzyme as an intermediate
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
equilibrium lies far to the side of phosphoenolpyruvate formation
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
involved in gluconeogenesis
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
-
-
?
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
-
-
?
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
involved in gluconeogenesis
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
-
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
-
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
-
-
ir
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
-
-
ir
additional information
?
-
-
no activity with 2-keto-3-methylvalerate, 2-ketoisocaproate, 2-ketomalonate, phenylpyruvate, hydroxyphenylpyruvate, imidazolpyruvate, and indole-3-pyruvate
-
-
?
additional information
?
-
neither GTP, CTP, ITP nor UTP is active as phosphoryl donor
-
-
?
additional information
?
-
-
neither GTP, CTP, ITP nor UTP is active as phosphoryl donor
-
-
?
additional information
?
-
neither GTP, CTP, ITP nor UTP is active as phosphoryl donor
-
-
?
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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
AMP + phosphoenolpyruvate + phosphate
ATP + pyruvate + H2O
-
the enzyme is involved in the production of pyruvate, phosphoenolpyruvate and ATP from glycerol in Pseudomonas fluorescens
-
-
?
AMP + phosphoenolpyruvate + phosphate
ATP + pyruvate + H2O
-
the enzyme is involved in the production of pyruvate, phosphoenolpyruvate and ATP from glycerol in Pseudomonas fluorescens
-
-
?
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
-
-
ir
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
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
involved in gluconeogenesis
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
essential step in gluconeogenesis if pyruvate or lactate is used as carbon source
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
Escherichia coli B / ATCC 11303
-
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
-
involved in gluconeogenesis
-
-
r
ATP + pyruvate + H2O
AMP + phosphoenolpyruvate + phosphate
-
involved in gluconeogenesis
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
requires divalent cations in the forward reaction, 93% of the activity with Mg2+
Mg2+
Mn2+
Ni2+
-
requires divalent cations in the forward reaction, 15% of the activity with Mg2+
additional information
Mg2+
-
divalent metal ion Mg2+ or Mn2+ required for forward reaction
Mg2+
-
requires divalent cations in the forward reaction, Mg2+ is most effective
Mn2+
-
divalent metal ion Mg2+ or Mn2+ required for forward reaction
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
additional information
activity of PEPS does not depend on monovalent cations such as K+ and NH4+
additional information
-
activity of PEPS does not depend on monovalent cations such as K+ and NH4+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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+
Sodium fluoride
inhibition through the formation of a MgF3- complex within the enzyme active site
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
ATP
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 70°C
0.4
pyruvate
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 70°C
additional information
additional information
-
Km-values, both reaction directions, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.683
pyruvate
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 70°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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 70°C
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 70°C
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 70°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
7.5
8.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
90
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain Bm, a mutant of strain B devoid of phosphoenolpyruvate carboxylase
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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
metabolism
-
the enzyme that may be responsible for the production of ATP from AMP formed by ADP-dependent glucokinase and phosphofructokinase reactions in the modified Embden-Meyerhof pathway of Pyrococcus furiosus
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
180000
77000
-
2 * 77000, enzyme tends to dissociate to monomers at low protein concentration
88000
SDS-PAGE, recombinant enzyme, phosphoenzyme intermediate form
92000
-
8 * 92000, SDS-PAGE, 30% of the enzyme is purified as a large inactive complex of about 1640 kDa
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
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
multimer
-
enzyme forms an unusually large tetraeisosameric complex of 2494 kDa, structure analysis by cryoelectron micrography
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
-
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
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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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
-
the enzyme retains 92% of full activity upon heating at 90°C for 30 min
22
-
retains full activity for several days if stored at room temperature in the presence of EDTA and Mg2+
4
-
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
-
20 min, 17% remaining activity, in presence of 1 M sucrose: 96% remaining activity
90
90
-
the enzyme retains its full activity upon heating at 90°C for 30 min
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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
-
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
-
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
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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 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, subcloning in Escherichia coli strain JM19, recombinant overexpression in Escherichia coli strain B0013, coexpression with genes aroG and tktA
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enhanced transcription of the mfrA gene in the presence of maltose
higher specific activity when cultures are grown in maltose medium
upregulated in H2O2-stressed cultures
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
the enzyme is of interest as a target for antibiotic development
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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
brenda
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
brenda
Cooper, R.A.; Kornberg, H.L.
Net formation of phosphoenolpyruvate from pyruvate by Escherichia coli
Biochim. Biophys. Acta
104
618-620
1965
Escherichia coli
brenda
Cooper, R.A.; Kornberg, H.L.
Phosphorylated enzyme as an intermediate in the phosphoenolpyruvate synthase reaction
Biochem. J.
105
49c-50c
1967
Escherichia coli
-
brenda
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
-
brenda
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
brenda
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)
brenda
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
brenda
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)
-
brenda
Harauz, G.
Symmetry in the 2.25 MDa homomultimeric phosphoenolpyruvate synthase from Staphylothermus marinus: analyses of negatively stained preparations
Micron
29
161-173
1998
Staphylothermus marinus
-
brenda
Hutchins, A.M.; Holden, J.F.; Adams, M.W.
Phosphoenolpyruvate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
183
709-715
2001
Pyrococcus furiosus
brenda
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
brenda
Tjaden, B.; Plagens, A.; Doerr, C.; Siebers, B.; Hensel, R.
Phosphoenolpyruvate synthetase and pyruvate, phosphate dikinase of Thermoproteus tenax: key pieces in the puzzle of archaeal carbohydrate metabolism
Mol. Microbiol.
60
287-298
2006
Thermoproteus tenax (Q70WQ8), Thermoproteus tenax, Thermoproteus tenax Kra1 (Q70WQ8)
brenda
Imanaka, H.; Yamatsu, A.; Fukui, T.; Atomi, H.; Imanaka, T.
Phosphoenolpyruvate synthase plays an essential role for glycolysis in the modified Embden-Meyerhof pathway in Thermococcus kodakarensis
Mol. Microbiol.
61
898-909
2006
Thermococcus kodakarensis, Thermococcus kodakarensis KW128
brenda
Burnell, J.N.
Cloning and characterization of Escherichia coli DUF299: a bifunctional ADP-dependent kinase-Pi-dependent pyrophosphorylase from bacteria
BMC Biochem.
11
1-1
2010
Zea mays
brenda
Auger, C.; Appanna, V.; Castonguay, Z.; Han, S.; Appanna, V.D.
A facile electrophoretic technique to monitor phosphoenolpyruvate-dependent kinases
Electrophoresis
33
1095-1101
2012
Pseudomonas fluorescens, Pseudomonas fluorescens ATCC 13525
brenda
Sakuraba, H.; Utsumi, E.; Schreier, H.J.; Ohshima, T.
Transcriptional regulation of phosphoenolpyruvate synthase by maltose in the hyperthermophilic archaeon, Pyrococcus furiosus
J. Biosci. Bioeng.
92
108-113
2001
Pyrococcus furiosus (P42850), Pyrococcus furiosus
brenda
Haferkamp, P.
Biochemical studies of enzymes involved in glycolysis of the thermoacidophilic crenarchaeon Sulfolobus solfataricus
PH. D. Thesis Universität Duisburg-Essen
2011
0000
2011
Saccharolobus solfataricus (Q97V40), Saccharolobus solfataricus DSM 1617 (Q97V40)
-
brenda
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
brenda
Chen, X.; Li, M.; Zhou, L.; Shen, W.; Algasan, G.; Fan, Y.; Wang, Z.
Metabolic engineering of Escherichia coli for improving shikimate synthesis from glucose
Biores. Technol.
166
64-71
2014
Escherichia coli (P23538), Escherichia coli
brenda
Theriot, C.; Tove, S.; Grunden, A.
Characterization of two proline dipeptidases (prolidases) from the hyperthermophilic archaeon Pyrococcus horikoshii
Appl. Microbiol. Biotechnol.
86
177-188
2010
Pyrococcus horikoshii
brenda
Schäfer, T.; Schönheit, P.
Gluconeogenesis from pyruvate in the hyperthermophilic archaeon Pyrococcus furiosus involvement of reactions of the Embden-Meyerhof pathway
Arch. Microbiol.
159
354-363
1993
Pyrococcus furiosus (P42850)
-
brenda
Adams, M.; Holden, J.; Menon, A.; Schut, G.; Grunden, A.; Hou, C.; Hutchins, A.; Jenney F.E., J.; Kim, C.; Ma, K.; Pan, G.; Roy, R.; Sapra, R.; Story, S.; Verhagen, M.
Key role for sulfur in peptide metabolism and in regulation of three hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
183
716-724
2001
Pyrococcus furiosus (P42850)
brenda
Barbier, T.; Zuniga-Ripa, A.; Moussa, S.; Plovier, H.; Sternon, J.F.; Lazaro-Anton, L.; Conde-Alvarez, R.; De Bolle, X.; Iriarte, M.; Moriyon, I.; Letesson, J.J.
Brucella central carbon metabolism an update
Crit. Rev. Microbiol.
44
182-211
2018
no activity in Brucella sp.
brenda
Alhasawi, A.; Thomas, S.C.; Appanna, V.D.
Metabolic networks to generate pyruvate, PEP and ATP from glycerol in Pseudomonas fluorescens
Enzyme Microb. Technol.
85
51-56
2016
Pseudomonas fluorescens, Pseudomonas fluorescens 13525
brenda
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