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Enzyme Nomenclature
Information on EC 4.1.1.38 - phosphoenolpyruvate carboxykinase (diphosphate)
for references in articles please use BRENDA:EC4.1.1.38
Word Map on EC 4.1.1.38
- 4.1.1.38
-
4.1.1.31
-
6.4.1.1
-
dikinase
-
entamoeba
-
carboxylases
- thiosulfate
- sulfobacillus
-
phototrophic
- pep-carboxylase
-
calvin
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
4.1.1.38
-
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RECOMMENDED NAME
GeneOntology No.
phosphoenolpyruvate carboxykinase (diphosphate)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
diphosphate + oxaloacetate = phosphate + phosphoenolpyruvate + CO2
-
-
-
-
diphosphate + oxaloacetate = phosphate + phosphoenolpyruvate + CO2
in the reverse direction the addition of CO2 is only to the si face of phosphoenolpyruvate
-
diphosphate + oxaloacetate = phosphate + phosphoenolpyruvate + CO2
the mechanism involves the formation of pentavalent diphosphoenolpyruvate which then is carboxylated to yield oxaloacetate and diphosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
decarboxylation
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
diphosphate:oxaloacetate carboxy-lyase (transphosphorylating; phosphoenolpyruvate-forming)
Also catalyses the reaction: phosphoenolpyruvate + phosphate = pyruvate + diphosphate.
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CAS REGISTRY NUMBER
COMMENTARY
9013-12-1
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
phosphate + phosphoenolpyruvate + CO2
?
-
enzyme is involved in autotrophic CO2 fixation
-
-
-
phosphate + phosphoenolpyruvate + CO2
?
-
the reaction is the source of the C4-dicarboxylic acids for anabolic reactions and for formation of succinate when it is the end product of the fermentation
-
-
-
phosphate + phosphoenolpyruvate + CO2
?
-
enzyme is involved in an oxaloacetate anaplerotic system
-
-
-
phosphate + phosphoenolpyruvate + CO2
?
-
the reaction is the source of the C4-dicarboxylic acids for anabolic reactions and for formation of succinate when it is the end product of the fermentation
-
-
-
phosphate + phosphoenolpyruvate + CO2
?
-
the reaction is the source of the C4-dicarboxylic acids for anabolic reactions and for formation of succinate when it is the end product of the fermentation
-
-
-
phosphate + phosphoenolpyruvate + CO2
?
-
ligand induced subunit interactions play a role in the control of the propionic acid fermentation
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-
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phosphate + phosphoenolpyruvate + CO2
?
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enzyme is involved in an oxaloacetate anaplerotic system
-
-
-
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
-
-
-
-
?
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
-
-
-
-
r
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
-
the enzyme is an acid-induced chromosomally encoded virulence factor in Agrobacterium tumefaciens
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-
r
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
-
-
-
?
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
-
-
-
-
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
-
-
-
-
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
-
-
-
-
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
-
-
-
r
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
-
-
-
r
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
-
-
-
-
?
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + phosphate
pyruvate + diphosphate
-
-
-
-
phosphoenolpyruvate + phosphate
pyruvate + diphosphate
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-
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ir
phosphoenolpyruvate + phosphate
pyruvate + diphosphate
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the addition of a proton to yield pyruvate is nonstereospecific, suggesting that enolpyruvate is ketonized after leaving the enzyme
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-
phosphoenolpyruvate + phosphate
pyruvate + diphosphate
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the pentavalent diphosphoenolpyruvate breaks down irreversibly to enolpyruvate and diphosphate
-
ir
phosphoenolpyruvate + phosphate
pyruvate + diphosphate
-
reaction is catalyzed in absence of CO2
-
ir
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
-
the enzyme is an acid-induced chromosomally encoded virulence factor in Agrobacterium tumefaciens
-
-
r
phosphate + phosphoenolpyruvate + CO2
?
-
enzyme is involved in autotrophic CO2 fixation
-
-
-
phosphate + phosphoenolpyruvate + CO2
?
-
the reaction is the source of the C4-dicarboxylic acids for anabolic reactions and for formation of succinate when it is the end product of the fermentation
-
-
-
phosphate + phosphoenolpyruvate + CO2
?
-
enzyme is involved in an oxaloacetate anaplerotic system
-
-
-
phosphate + phosphoenolpyruvate + CO2
?
-
the reaction is the source of the C4-dicarboxylic acids for anabolic reactions and for formation of succinate when it is the end product of the fermentation
-
-
-
phosphate + phosphoenolpyruvate + CO2
?
-
the reaction is the source of the C4-dicarboxylic acids for anabolic reactions and for formation of succinate when it is the end product of the fermentation
-
-
-
phosphate + phosphoenolpyruvate + CO2
?
-
ligand induced subunit interactions play a role in the control of the propionic acid fermentation
-
-
-
phosphate + phosphoenolpyruvate + CO2
?
-
enzyme is involved in an oxaloacetate anaplerotic system
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Co2+
-
can partially replace Mn2+ or Mg2+ in activation
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glycylglycine
-
higher inhibition at pH 7.8 than at pH 6.5
Imidodiphosphate
-
competitive with respect to diphosphate
Methylene diphosphonate
-
competitive with respect to diphosphate
thiols
-
formation of pyruvate from phosphoenolpyruvate and phosphate
Tris-HCl
-
higher inhibition at pH 7.8 than at pH 6.5
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.5
-
formation of phosphoenolpyruvate from oxaloacetate and diphosphate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8.5
-
pH 5.5: about 35% of maximal activity, pH 8.5: about 55% of maximal activity, formation of oxalacetate
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activity at different phases of growth with lactate; higher activity with lactate as substrate than with glucose as substrate
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activity at different phases of growth with lactate; higher activity with lactate as substrate than with glucose as substrate
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activity at different phases of growth with lactate
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
-
monomeric enzyme form,equilibrium sedimentation
224000
-
dimeric enzyme form, equilibrium sedimentation
378000
-
tetrameric enzyme form, equilibrium sedimentation
430000
430000
-
low speed sedimentation without reaching equilibrium
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 100000, the enzyme exists as monomer, dimer or tetramer, equilibrium sedimentation
monomer
tetramer
-
4 * 100000, the enzyme exists as monomer, dimer or tetramer, equilibrium sedimentation
additional information
-
the dissociation of the tetrameric enzyme and association of monomeric enzyme to dimeric forms occurs during catalysis of the forward reaction, caused by the product oxaloacetate, or by malate or fumarate. The monomeric form and the dimeric form are less active than the tetrameric enzyme form
monomer
-
1 * 100000, the enzyme exists as monomer, dimer or tetramer, equilibrium sedimentation
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.2
-
25°C, 0.2 M NaHCO3, 60% loss of activity after 30 min, rapid loss of activity above pH 8.2
33091
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.05 M phosphate buffer, 0.01 M or 0.001 M thiol, 0.01 mg protein per ml, stable
-
30 h dialysis against phosphate buffer containing 1 mM mercaptoethanol, with a change of buffer at 15 h, stable
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli K-12 has no effect on succinate fermentation. In phosphoenolpyruvate carboxylase mutant strain of Escherichia coli K-12 (ppc::kan), PEPCK overexpression increases succinate production 6.5fold
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LINKS TO OTHER DATABASES (specific for EC-Number 4.1.1.38)
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