Information on EC 4.1.1.38 - phosphoenolpyruvate carboxykinase (diphosphate)

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

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EC NUMBER
COMMENTARY hide
4.1.1.38
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RECOMMENDED NAME
GeneOntology No.
phosphoenolpyruvate carboxykinase (diphosphate)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
diphosphate + oxaloacetate = phosphate + phosphoenolpyruvate + CO2
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylation
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-
-
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decarboxylation
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Pyruvate metabolism
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-
Metabolic pathways
-
-
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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 hide
9013-12-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DSM 1030
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
no activity in Clostridium thermocellum
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-
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Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphate + phosphoenolpyruvate + CO2
?
show the reaction diagram
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
show the reaction diagram
phosphoenolpyruvate + phosphate
pyruvate + diphosphate
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphate + phosphoenolpyruvate + CO2
?
show the reaction diagram
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
show the reaction diagram
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the enzyme is an acid-induced chromosomally encoded virulence factor in Agrobacterium tumefaciens
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-
r
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphosphate
glycylglycine
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higher inhibition at pH 7.8 than at pH 6.5
Imidodiphosphate
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competitive with respect to diphosphate
Methylene diphosphonate
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competitive with respect to diphosphate
phosphoenolpyruvate
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at high concentration
SO42-
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competitive against phosphate
thiols
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formation of pyruvate from phosphoenolpyruvate and phosphate
Tris-HCl
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higher inhibition at pH 7.8 than at pH 6.5
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
specific requirement, no activity with GDP and IDP
phosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.036 - 5
phosphoenolpyruvate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1 - 8
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formation of oxaloacetate
7 - 7.5
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formation of phosphoenolpyruvate from oxaloacetate and diphosphate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.5
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pH 5.5: about 35% of maximal activity, pH 8.5: about 55% of maximal activity, formation of oxalacetate
6 - 8.5
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half-maximal activity at pH 6.0 and pH 8.5
7.2 - 8.5
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80% of maximal activity at pH 7.2 and at pH 8.5
7.4 - 8.2
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about 50% of maximal activity at pH 7.4 and at pH 8.2
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
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gel filtration
100000
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monomeric enzyme form,equilibrium sedimentation
224000
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dimeric enzyme form, equilibrium sedimentation
378000
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tetrameric enzyme form, equilibrium sedimentation
430000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 100000, the enzyme exists as monomer, dimer or tetramer, equilibrium sedimentation
monomer
tetramer
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4 * 100000, the enzyme exists as monomer, dimer or tetramer, equilibrium sedimentation
additional information
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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
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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inactivation, even at 0°C
33091
4.5
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25°C, 5 h, little loss of activity
33091
8.2
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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
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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)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)