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Information on EC 4.1.1.49 - phosphoenolpyruvate carboxykinase (ATP) and Organism(s) Escherichia coli and UniProt Accession P22259

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.49 phosphoenolpyruvate carboxykinase (ATP)
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This record set is specific for:
Escherichia coli
UNIPROT: P22259 not found.
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
pepc kinase, protein p60, phosphoenolpyruvate carboxylase kinase, pepk, atp-dependent phosphoenolpyruvate carboxykinase, pep carboxylase kinase, osppck3, pfpepck, osppck1, pepck (atp), more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoenolpyruvate carboxykinase
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ATP-dependent phosphoenolpyruvate(PEP)carboxykinase
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ATP-oxaloacetate carboxylase (transphosphorylating)
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Carboxykinase, phosphopyruvate (adenosine triphosphate)
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Glycosomal protein P60
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PEP carboxykinase
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-
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PEP carboxylase
PEPCK
PEPCK (ATP)
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PEPK
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phosphoenolpyruvate carboxykinase
phosphoenolpyruvate carboxykinase [ATP]
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Phosphoenolpyruvate carboxylase
Phosphoenolpyruvate carboxylase (ATP)
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-
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phosphoenolpyruvate(PEP)carboxykinase (GTP/ATP:oxaloacetate carboxy-lyase (transphosphorylating)EC 4.1.1.32/49)
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phosphoenolpyruvic carboxykinase
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Phosphoenolpyruvic carboxylase
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phosphopyruvate carboxykinase
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-
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Phosphopyruvate carboxykinase (adenosine triphosphate)
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Protein p60
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO2
show the reaction diagram
sequential mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:oxaloacetate carboxy-lyase (transphosphorylating; phosphoenolpyruvate-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9073-94-3
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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
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
show the reaction diagram
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
show the reaction diagram
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
show the reaction diagram
additional information
?
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catalyzes an exchange reaction between C14O2 and the beta-carboxyl group of oxaloacetate
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
show the reaction diagram
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-
-
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
show the reaction diagram
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synthesis of oxaloacetate is a key step in the formation of four-carbon compounds, such as malate, fumarate, and succinate
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
the presence of 9.6 mM ATP decreases 3folds the catalytic efficiency of the enzyme
D-fructose 1,6-bisphosphate
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-
D-fructose 6-phosphate
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dihydroxyacetone phosphate
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Glycerate 3-phosphate
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oxalate
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competitive inhibitor
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-fructose 1,6-bisphosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
phosphoenolpyruvate
at pH 7.0 and 37°C
0.05
ADP
-
-
0.06
ATP
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-
13
CO2
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CO2 in form of HCO3-
0.67
oxaloacetate
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-
0.07 - 8
phosphoenolpyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.67
phosphoenolpyruvate
at pH 7.0 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11
phosphoenolpyruvate
at pH 7.0 and 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64000
-
1 * 64000, SDS-PAGE
65000
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equilibrium sedimentation under non-denaturing conditions, non-denaturing PAGE in presence of detergent, sucrose density gradient centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
three-dimensional crystal structure, enzyme possesses a mononucleotide-binding domain unique from other proteins having the P-loop motif
crystals grown by hanging drop vapor diffusion, ADP-ALF3-Mg2+ complex, monoclinic space group C2 with unit cell parameters a : 126.0 A, b : 95.8 A, c : 46.6 A, ADP-ALF3-Mg2+-pyruvate complex, monoclinic space group C2 with unit cell parameters a : 124.7 A, b : 94.2 A, c : 46.3 A
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crystals grown by hanging drop vapor diffusion, monoclinic space group C2, unit cell parameter a = 126.2 A, b = 95.2 A, c = 46.8 A, d = 95.2 A
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space group P2(1)2(1)2(1), a : 77.7 A, b : 89.7 A, c 93.8 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D269E
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site-specific mutagenesis
deltaF409
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site-specific mutagenesis, deletion of Phe409
E508Q/E511Q
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site-specific mutagenesis
F409A
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site-specific mutagenesis
F413A
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site-specific mutagenesis
R2S
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site-specific mutagenesis
R396S
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site-specific mutagenesis
R396TAA
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site-specific mutagenesis, termination codon at position 396
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 66
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in presence of phosphoenolpyruvate and MnCl2, 50% loss of enzyme activity at 66°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni+ affinity column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli ER2566 cells
overexpressed
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Krebs, A.; Bridger, W.A.
On the monomeric structure and proposed regulatory properties of phosphoenolpyruvate carboxykinase of Escherichia coli
Can. J. Biochem.
54
22-26
1976
Escherichia coli
Manually annotated by BRENDA team
Krebs, A.; Bridger, W.A.
The kinetic properties of phosphoenolpyruvate carboxykinase of Escherichia coli
Can. J. Biochem.
58
309-318
1980
Escherichia coli
Manually annotated by BRENDA team
Matte, A.; Goldie, H.; Sweet, R.M.; Delbaere, L.T.J.
Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold
J. Mol. Biol.
256
126-143
1996
Escherichia coli (P22259), Escherichia coli
Manually annotated by BRENDA team
Lea, P.J.; Chen, Z.H.; Leegood, R.C.; Walker, R.P.
Does phosphoenolpyruvate carboxykinase have a role in both amino acid and carbohydrate metabolism?
Amino Acids
20
225-241
2001
Anaerobiospirillum succiniproducens, Ananas comosus, Clusia aripoensis, Clusia minor, Coleus scutellarioides, Corynebacterium glutamicum, Cucumis sativus, Cupriavidus necator, Digitaria sanguinalis, Escherichia coli, Megathyrsus maximus, no activity in Saccharum officinarum, no activity in Sorghum bicolor, Rhodopseudomonas palustris, Ruminococcus flavefaciens, Saccharomyces cerevisiae, Sinorhizobium meliloti, Staphylococcus aureus, Tillandsia fasciculata, Udotea flabellum, Urochloa panicoides, Vitis vinifera, Zea mays
Manually annotated by BRENDA team
Gokarn, R.R.; Eiteman, M.A.; Altman, E.
Metabolic analysis of Escherichia coli in the presence and absence of the carboxylating enzymes phosphoenolpyruvate carboxylase and pyruvate carboxylase
Appl. Environ. Microbiol.
66
1844-1850
2000
Escherichia coli
Manually annotated by BRENDA team
Delbaere, L.T.J.; Sudom, A.M.; Prasad, L.; Leduc, Y.; Goldie, H.
Structure/function studies of phosphoryl transfer by phosphoenolpyruvate carboxykinase
Biochim. Biophys. Acta
1697
271-278
2004
Corynebacterium glutamicum, Escherichia coli, Trypanosoma cruzi
Manually annotated by BRENDA team
Sudom, A.; Walters, R.; Pastushok, L.; Goldie, D.; Prasad, L.; Delbaere, L.T.J.; Goldie, H.
Mechanisms of activation of phosphoenolpyruvate carboxykinase from Escherichia coli by Ca2+ and of desensitization by trypsin
J. Bacteriol.
185
4233-4242
2003
Escherichia coli
Manually annotated by BRENDA team
Sudom, A.M.; Prasad, L.; Goldie, H.; Delbaere, L.T.
The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate carboxykinase from the use of AlF(3)
J. Mol. Biol.
314
83-92
2001
Escherichia coli
Manually annotated by BRENDA team
Ravanal, M.C.; Goldie, H.; Cardemil, E.
Thermal stability of phosphoenolpyruvate carboxykinases from Escherichia coli, Trypanosoma brucei, and Saccharomyces cerevisiae
J. Protein Chem.
22
311-315
2003
Saccharomyces cerevisiae, Escherichia coli, Trypanosoma brucei
Manually annotated by BRENDA team
Kwon, Y.D.; Lee, S.Y.; Kim, P.
A physiology study of Escherichia coli overexpressing phosphoenolpyruvate carboxykinase
Biosci. Biotechnol. Biochem.
72
1138-1141
2008
Escherichia coli (P22259)
Manually annotated by BRENDA team
Lee, H.J.; Kim, H.J.; Seo, J.; Na, Y.A.; Lee, J.; Lee, J.Y.; Kim, P.
Estimation of phosphoenolpyruvate carboxylation mediated by phosphoenolpyruvate carboxykinase (PCK) in engineered Escherichia coli having high ATP
Enzyme Microb. Technol.
53
13-17
2013
Escherichia coli (P22259)
Manually annotated by BRENDA team