Information on EC 4.1.1.38 - phosphoenolpyruvate carboxykinase (diphosphate)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
4.1.1.38
-
RECOMMENDED NAME
GeneOntology No.
phosphoenolpyruvate carboxykinase (diphosphate)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
diphosphate + oxaloacetate = phosphate + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
diphosphate + oxaloacetate = phosphate + phosphoenolpyruvate + CO2
show the reaction diagram
in the reverse direction the addition of CO2 is only to the si face of phosphoenolpyruvate
-
diphosphate + oxaloacetate = phosphate + phosphoenolpyruvate + CO2
show the reaction diagram
the mechanism involves the formation of pentavalent diphosphoenolpyruvate which then is carboxylated to yield oxaloacetate and diphosphate
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
decarboxylation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Pyruvate metabolism
-
SYSTEMATIC NAME
IUBMB Comments
diphosphate:oxaloacetate carboxy-lyase (transphosphorylating; phosphoenolpyruvate-forming)
Also catalyses the reaction: phosphoenolpyruvate + phosphate = pyruvate + diphosphate.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
carboxykinase, phosphopyruvate (pyrophosphate)
-
-
-
-
PEP carboxykinase
-
-
-
-
PEP carboxylase
-
-
-
-
PEP carboxyphosphotransferase
-
-
-
-
PEPCTrP
-
-
-
-
phosphoenolpyruvate carboxykinase
-
-
-
-
phosphoenolpyruvate carboxykinase (pyrophosphate)
-
-
-
-
Phosphoenolpyruvate carboxylase
-
-
-
-
phosphoenolpyruvate carboxylase (pyrophosphate)
-
-
-
-
phosphoenolpyruvate carboxyphosphotransferase
-
-
-
-
phosphoenolpyruvate carboxytransphosphorylase
-
-
-
-
phosphoenolpyruvic carboxykinase
-
-
-
-
phosphoenolpyruvic carboxykinase (pyrophosphate)
-
-
-
-
Phosphoenolpyruvic carboxylase
-
-
-
-
phosphoenolpyruvic carboxylase (pyrophosphate)
-
-
-
-
phosphoenolpyruvic carboxytransphosphorylase
-
-
-
-
phosphopyruvate carboxykinase
-
-
-
-
phosphopyruvate carboxylase
-
-
-
-
phosphopyruvate carboxylase (pyrophosphate)
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9013-12-1
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
show the reaction diagram
-
-
-
r
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
show the reaction diagram
-
-
-
r
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
show the reaction diagram
-
-
-
?
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
show the reaction diagram
-
-
-
-
r
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
show the reaction diagram
-
the enzyme is an acid-induced chromosomally encoded virulence factor in Agrobacterium tumefaciens
-
-
r
phosphate + phosphoenolpyruvate + CO2
?
show the reaction diagram
-
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
?
show the reaction diagram
-
enzyme is involved in an oxaloacetate anaplerotic system
-
-
-
phosphate + phosphoenolpyruvate + CO2
?
show the reaction diagram
-
ligand induced subunit interactions play a role in the control of the propionic acid fermentation
-
-
-
phosphate + phosphoenolpyruvate + CO2
?
show the reaction diagram
-
enzyme is involved in autotrophic CO2 fixation
-
-
-
phosphoenolpyruvate + phosphate
pyruvate + diphosphate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + phosphate
pyruvate + diphosphate
show the reaction diagram
-
-
-
ir
phosphoenolpyruvate + phosphate
pyruvate + diphosphate
show the reaction diagram
-
the addition of a proton to yield pyruvate is nonstereospecific, suggesting that enolpyruvate is ketonized after leaving the enzyme
-
-
phosphoenolpyruvate + phosphate
pyruvate + diphosphate
show the reaction diagram
-
the pentavalent diphosphoenolpyruvate breaks down irreversibly to enolpyruvate and diphosphate
-
ir
phosphoenolpyruvate + phosphate
pyruvate + diphosphate
show the reaction diagram
-
reaction is catalyzed in absence of CO2
-
ir
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
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
show the reaction diagram
-
the enzyme is an acid-induced chromosomally encoded virulence factor in Agrobacterium tumefaciens
-
-
r
phosphate + phosphoenolpyruvate + CO2
?
show the reaction diagram
-
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
?
show the reaction diagram
-
enzyme is involved in an oxaloacetate anaplerotic system
-
-
-
phosphate + phosphoenolpyruvate + CO2
?
show the reaction diagram
-
ligand induced subunit interactions play a role in the control of the propionic acid fermentation
-
-
-
phosphate + phosphoenolpyruvate + CO2
?
show the reaction diagram
-
enzyme is involved in autotrophic CO2 fixation
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
can partially replace Mn2+ or Mg2+ in activation
Co2+
-
Mn2+, Mg2+ or Co2+ required
Mg2+
-
Mn2+, Mg2+ or Co2+ required
Mg2+
-
and Mn2+ are required for maximal activity
Mn2+
-
Mn2+, Mg2+ or Co2+ required
Mn2+
-
and Mg2+ are required for maximal activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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
phosphoenolpyruvate
-
at high concentration
SO42-
-
competitive against phosphate
thiols
-
formation of pyruvate from phosphoenolpyruvate and phosphate
Tris-HCl
-
higher inhibition at pH 7.8 than at pH 6.5
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ADP
-
specific requirement, no activity with GDP and IDP
phosphate
-
stimulates
phosphate
-
stimulates
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.036
-
phosphoenolpyruvate
-
-
0.55
-
phosphoenolpyruvate
-
-
5
-
phosphoenolpyruvate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.1
8
-
formation of oxaloacetate
7
7.5
-
formation of phosphoenolpyruvate from oxaloacetate and diphosphate
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
6
8.5
-
half-maximal activity at pH 6.0 and pH 8.5
7.2
8.5
-
80% of maximal activity at pH 7.2 and at pH 8.5
7.4
8.2
-
about 50% of maximal activity at pH 7.4 and at pH 8.2
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
activity at different phases of growth with lactate; higher activity with lactate as substrate than with glucose as substrate
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60000
-
-
gel filtration
100000
-
-
monomeric enzyme form,equilibrium sedimentation
224000
-
-
dimeric enzyme form, equilibrium sedimentation
378000
-
-
tetrameric enzyme form, equilibrium sedimentation
430000
-
-
low speed sedimentation without reaching equilibrium
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 100000, the enzyme exists as monomer, dimer or tetramer, equilibrium sedimentation
monomer
-
1 * 100000, the enzyme exists as monomer, dimer or tetramer, equilibrium sedimentation
tetramer
-
4 * 100000, the enzyme exists as monomer, dimer or tetramer, equilibrium sedimentation
monomer
-
1 * 60000, SDS-PAGE
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
inactivation, even at 0°C
4.5
-
-
25°C, 5 h, little loss of activity
8.2
-
-
25°C, 0.2 M NaHCO3, 60% loss of activity after 30 min, rapid loss of activity above pH 8.2
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-