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Information on EC 4.1.1.38 - phosphoenolpyruvate carboxykinase (diphosphate)
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4.1.1.38 phosphoenolpyruvate carboxykinase (diphosphate)IUBMB Comments
Also catalyses the reaction: phosphoenolpyruvate + phosphate = pyruvate + diphosphate.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
carboxykinase, phosphopyruvate (pyrophosphate), PCK, PEP carboxykinase, PEP carboxylase, PEP carboxyphosphotransferase, PEPCK, PEPCK1, PEPCK2, PEPCK3, PEPCTrP, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carboxykinase, phosphopyruvate (pyrophosphate)
-
-
-
-
PEP carboxykinase
-
-
-
-
PEP carboxylase
-
-
-
-
PEP carboxyphosphotransferase
-
-
-
-
PEPCTrP
-
-
-
-
phosphoenolpyruvate carboxykinase
-
-
-
-
phosphoenolpyruvate carboxykinase (pyrophosphate)
-
-
-
-
Phosphoenolpyruvate carboxylase
-
-
-
-
phosphoenolpyruvate carboxylase (pyrophosphate)
-
-
-
-
phosphoenolpyruvate carboxyphosphotransferase
-
-
-
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phosphoenolpyruvate carboxytransphosphorylase
-
-
-
-
phosphoenolpyruvic carboxykinase
-
-
-
-
phosphoenolpyruvic carboxykinase (pyrophosphate)
-
-
-
-
Phosphoenolpyruvic carboxylase
-
-
-
-
phosphoenolpyruvic carboxylase (pyrophosphate)
-
-
-
-
phosphoenolpyruvic carboxytransphosphorylase
-
-
-
-
phosphopyruvate carboxykinase
-
-
-
-
phosphopyruvate carboxylase
-
-
-
-
phosphopyruvate carboxylase (pyrophosphate)
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
diphosphate + oxaloacetate = phosphate + phosphoenolpyruvate + CO2
the mechanism involves the formation of pentavalent diphosphoenolpyruvate which then is carboxylated to yield oxaloacetate and diphosphate
-
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
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
decarboxylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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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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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
-
-
?
phosphate + phosphoenolpyruvate + CO2
?
-
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
-
-
r
phosphate + phosphoenolpyruvate + CO2
diphosphate + oxaloacetate
-
-
-
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
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-
-
?
phosphoenolpyruvate + phosphate
pyruvate + diphosphate
-
-
-
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
-
?
phosphoenolpyruvate + phosphate
pyruvate + diphosphate
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the pentavalent diphosphoenolpyruvate breaks down irreversibly to enolpyruvate and diphosphate
-
ir
phosphoenolpyruvate + phosphate
pyruvate + diphosphate
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reaction is catalyzed in absence of CO2
-
ir
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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
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glycylglycine
-
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
thiols
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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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hyperglycemia
Fasting hyperglycemia is not associated with increased expression of PEPCK or G6Pc in patients with Type 2 Diabetes.
Insulin Resistance
PEPCK1 Antisense Oligonucleotide Prevents Adiposity and Impairs Hepatic Glycogen Synthesis in High-Fat Male Fed Rats.
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activity at different phases of growth with lactate
brenda
-
higher activity with lactate as substrate than with glucose as substrate
brenda
-
activity at different phases of growth with lactate
brenda
-
higher activity with lactate as substrate than with glucose as substrate
brenda
-
activity at different phases of growth with lactate
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PEPCK_PROFF
1131
0
127040
Swiss-Prot
-
PECK1_ENTHI
1151
0
130909
Swiss-Prot
other Location (Reliability: 2)
PECK2_ENTHI
1153
0
131117
Swiss-Prot
other Location (Reliability: 1)
PECK3_ENTHI
1153
0
131013
Swiss-Prot
other Location (Reliability: 1)
A0A644TCC3_9ZZZZ
1156
0
129618
TrEMBL
other Location (Reliability: 4)
A0A344UUE8_9ACTN
1133
0
124363
TrEMBL
-
A0A645CET6_9ZZZZ
217
0
24720
TrEMBL
other Location (Reliability: 1)
A0A644VP05_9ZZZZ
1152
0
131456
TrEMBL
other Location (Reliability: 1)
A0A645A5M5_9ZZZZ
689
0
76102
TrEMBL
other Location (Reliability: 3)
A0A644TQE2_9ZZZZ
1173
0
132934
TrEMBL
other Location (Reliability: 3)
A0A644W4C4_9ZZZZ
1149
0
130816
TrEMBL
other Location (Reliability: 2)
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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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SUBUNIT
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
trimer
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lochmueller, H.; Wood, H.G.; Davis, J.J.
Phosphoenolpyruvate carboxytransphosphorylase. II. Crystallization and properties
J. Biol. Chem.
241
5678-5691
1966
Propionibacterium freudenreichii subsp. shermanii
brenda
Willard, J.M.; Rose, I.A.
Formation of enolpyruvate in the phosphoenolpyruvate carboxytransphosphorylase reaction
Biochemistry
12
5241-5246
1973
Propionibacterium freudenreichii subsp. shermanii
brenda
Perl, M.
Phosphoenol-pyruvate-carboxylase activity in cotton and Sorghum seeds and its relation to seedling development
Planta
139
239-243
1978
Gossypium hirsutum, Sorghum bicolor
brenda
O'Brien, W.E.; Wood, H.G.
Carboxytransphosphorylase. 8. Ligand-mediated interaction of subunits as a possible control mechanism in Propionibacteria
J. Biol. Chem.
249
4917-4925
1974
Propionibacterium freudenreichii subsp. shermanii
brenda
O'Brien, W.E.; Singleton, R.; Wood, H.G.
Phosphoenolpyruvate carboxytransphosphorylase. An investigation of the mechanism with 18 O
Biochemistry
12
5247-5253
1973
Propionibacterium freudenreichii subsp. shermanii
brenda
Wood, H.G.; Goss, N.H.
Phosphorylation enzymes of the propionic acid bacteria and the roles of ATP inorganic pyrophosphate, and polyphosphates
Proc. Natl. Acad. Sci. USA
82
312-315
1985
Acidipropionibacterium acidipropionici, Propionibacterium freudenreichii, Propionibacterium freudenreichii subsp. shermanii
brenda
Eden, G.; Fuchs, G.
Autotrophic CO2 fixation in Acetobacterium woodii. II. Demonstration of enzymes involved
Arch. Microbiol.
135
68-73
1983
Acetobacterium woodii
-
brenda
Wood, H.G.; O'Brien, W.E.; Michaels, G.
Properties of carboxytransphosphorylase; pyruvate, phosphate dikinase; pyrophosphate-phosphofructikinase and pyrophosphate-acetate kinase and their roles in the metabolism of inorganic pyrophosphate
Adv. Enzymol. Relat. Areas Mol. Biol.
45
85-155
1977
Propionibacterium freudenreichii subsp. shermanii
brenda
Asanuma, N.; Hino, T.
Molecular characterization, enzyme properties and transcriptional regulation of phosphoenolpyruvate carboxykinase and pyruvate kinase in a ruminal bacterium, Selenomonas ruminantium
Microbiology
147
681-690
2001
Selenomonas ruminantium
brenda
Kim, P.; Laivenieks, M.; Vieille, C.; Zeikus, J.G.
Effect of overexpression of Actinobacillus succinogenes phosphoenolpyruvate carboxykinase on succinate production in Escherichia coli
Appl. Environ. Microbiol.
70
1238-1241
2004
Actinobacillus succinogenes
brenda
Liu, P.; Wood, D.; Nester, E.W.
Phosphoenolpyruvate carboxykinase is an acid-induced chromosomally encoded virulence factor in Agrobacterium tumefaciens
J. Bacteriol.
187
6039-6045
2005
Agrobacterium tumefaciens
brenda
Zhou, J.; Olson, D.G.; Argyros, D.A.; Deng, Y.; van Gulik, W.M.; van Dijken, J.P.; Lynd, L.R.
Atypical glycolysis in Clostridium thermocellum
Appl. Environ. Microbiol.
79
3000-3008
2013
no activity in Clostridium thermocellum
brenda
Chiba, Y.; Kamikawa, R.; Nakada-Tsukui, K.; Saito-Nakano, Y.; Nozaki, T.
Discovery of PPi-type phosphoenolpyruvate carboxykinase genes in eukaryotes and bacteria
J. Biol. Chem.
290
23960-23970
2015
Entamoeba histolytica (C4LWQ8), Entamoeba histolytica (C4LY96), Entamoeba histolytica (C4M1E4)
brenda
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