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Information on EC 4.1.1.49 - phosphoenolpyruvate carboxykinase (ATP)
for references in articles please use BRENDA:EC4.1.1.49
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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)
The enzyme appears in viruses and cellular organisms
showSynonyms
pepc kinase, protein p60, phosphoenolpyruvate carboxylase kinase, pepk, atp-dependent phosphoenolpyruvate carboxykinase, pep carboxylase kinase, osppck3, pfpepck, osppck1, pepck (atp), more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADP-linked PEP carboxykinase
ATP-dependent phosphoenolpyruvate carboxykinase
ATP-dependent phosphoenolpyruvate(PEP)carboxykinase
ATP-forming PEP-carboxykinase
ATP-oxaloacetate carboxylase (transphosphorylating)
ATP:oxaloacetate carboxy-lyase
transphosphorylating, interacts also with GTP, EC 4.1.1.32
Carboxykinase, phosphopyruvate (adenosine triphosphate)
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-
-
-
Glycosomal protein P60
-
-
-
-
PCK
PCK1
pckA
PEP carboxykinase
PEP carboxylase
PEPC
PEPCK
PEPCK (ATP)
-
-
-
-
PEPK
-
-
-
-
phosphoenolpyruvate carboxykinase
Phosphoenolpyruvate carboxylase
Phosphoenolpyruvate carboxylase (ATP)
-
-
-
-
phosphoenolpyruvate(PEP)carboxykinase (GTP/ATP:oxaloacetate carboxy-lyase (transphosphorylating)EC 4.1.1.32/49)
phosphoenolpyruvic carboxykinase
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-
-
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Phosphoenolpyruvic carboxylase
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-
-
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phosphopyruvate carboxykinase
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-
-
-
Phosphopyruvate carboxykinase (adenosine triphosphate)
-
-
-
-
PPC
Protein p60
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-
-
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PEP carboxykinase
-
-
-
-
PEP carboxykinase
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-
PEP carboxylase
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-
-
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PEPCK
-
-
-
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phosphoenolpyruvate carboxykinase
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-
-
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phosphoenolpyruvate carboxykinase
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Phosphoenolpyruvate carboxylase
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phosphoenolpyruvate(PEP)carboxykinase (GTP/ATP:oxaloacetate carboxy-lyase (transphosphorylating)EC 4.1.1.32/49)
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phosphoenolpyruvate(PEP)carboxykinase (GTP/ATP:oxaloacetate carboxy-lyase (transphosphorylating)EC 4.1.1.32/49)
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phosphoenolpyruvate(PEP)carboxykinase (GTP/ATP:oxaloacetate carboxy-lyase (transphosphorylating)EC 4.1.1.32/49)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
decarboxylation
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-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
C4 photosynthetic carbon assimilation cycle, PEPCK type, gluconeogenesis I, superpathway of glyoxylate cycle and fatty acid degradation
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SYSTEMATIC NAME
IUBMB Comments
ATP:oxaloacetate carboxy-lyase (transphosphorylating; phosphoenolpyruvate-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9073-94-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CTP + oxaloacetate
CDP + phosphoenolpyruvate + CO2
-
Substrates: 15% of the activity with ATP
Products: -
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?
TTP + oxaloacetate
TDP + phosphoenolpyruvate + CO2
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Substrates: 16% of the activity with ATP
Products: -
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?
UTP + oxaloacetate
UDP + phosphoenolpyruvate + CO2
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Substrates: 20% of the activity with ATP
Products: -
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?
ADP + (E)-3-fluorophosphoenolpyruvate + CO2
ATP + 3-fluorooxaloacetate
Substrates: -
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?
ADP + (E)-3-fluorophosphoenolpyruvate + CO2
ATP + 3-fluorooxaloacetate
Substrates: -
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?
ADP + (Z)-3-fluorophosphoenolpyruvate + CO2
ATP + 3-fluorooxaloacetate
Substrates: -
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?
ADP + (Z)-3-fluorophosphoenolpyruvate + CO2
ATP + 3-fluorooxaloacetate
Substrates: -
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?
ADP + phosphoenolpyruvate + CO2
?
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Substrates: catabolic CO2-fixing enzyme, important role in succinate formation
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?
ADP + phosphoenolpyruvate + CO2
?
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Substrates: the enzyme is responsible for the CO2 fixation
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?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
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?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
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Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
Substrates: -
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?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
Substrates: -
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ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
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Substrates: in contrast to its normal role in gluconeogenesis, PEP carboxykinase can operate in the reverse direction from phosphoenolpyruvate to oxaloacetate, upon knockout of pyruvate kinase in a riboflavin-producing Bacillus subtilis strain and in wild-type 168
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ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
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?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
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Substrates: the enzyme may function in the conversion of carbon skeletons to phosphoenolpyruvate, which, depending on the energy requirements of the phloem, is subsequently utilised by either gluconoeogenesis or the Krebs cycle, which both consume protons
Products: -
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?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
Products: -
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?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
Substrates: -
Products: -
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?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
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Substrates: 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
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
Substrates: -
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?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
Substrates: -
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r
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
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?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: Arg70 is important for catalytic efficiency of the enzyme and for binding of phosphoenolpyruvate
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Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
Substrates: -
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
Substrates: -
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r
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
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r
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
Substrates: -
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r
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
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r
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
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?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
Substrates: -
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r
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
Substrates: -
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ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Substrates: -
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Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate
?
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Substrates: the enzyme is neither regulatory nor inducible, the main function is catalyzing the synthesis of phosphoenopyruvate as a part of the gluconeogenetic pathway
Products: -
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?
ATP + oxaloacetate
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Substrates: the enzyme is neither regulatory nor inducible, the main function is catalyzing the synthesis of phosphoenopyruvate as a part of the gluconeogenetic pathway
Products: -
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?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
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?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Alternanthera ficoides
-
Substrates: -
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ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
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?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: for the Anaerobiospirillum succiniciproducens enzyme, at physiological concentrations of Mn2+ and Mg2+, the affinity for CO2 increases as the ATP/ADP ratio is increased in the assay medium. The results show that a high ATP/ADP ratio favors CO2 fixation by the PEP carboxykinase from Anaerobiospirillum succiniciproducens
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Anaerobiospirillum succiniproducens
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Substrates: -
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Anaerobiospirillum succiniproducens
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: key enzyme in the regulation of flux through the gluconeogenic pathway, gluconeogenic production of sugars from storage oil
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Substrates: -
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: first commmitted step of gluconeogenesis
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: carbon and nitrogen metabolism
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: critical gluconeogenic enzyme, catalyzes the first committed step in the diversion of tricarboxylic acid cycle intermediates towards gluconeogenesis
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: first commmitted step of gluconeogenesis
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: carbon and nitrogen metabolism
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: responsible for light-independent carbon fixation
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: carbon and nitrogen metabolism
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: carbon and nitrogen metabolism
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: carbon and nitrogen metabolism
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Substrates: -
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: carbon and nitrogen metabolism
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Substrates: -
Products: ADP is the preferred PCK phosphate acceptor
Products: ADP is the preferred PCK phosphate acceptor
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Substrates: -
Products: ADP is the preferred PCK phosphate acceptor
Products: ADP is the preferred PCK phosphate acceptor
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
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ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Substrates: interacts also with GTP, EC 4.1.1.32
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ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
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ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Substrates: -
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Substrates: -
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: acts in the metabolic pathways at the intersection of the glycolysis, the gluconeogenesis and the Krebs cycle, enzyme activity increases when cells are submitted to hypothermic stress
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: responsible for light-independent carbon fixation
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: carbon and nitrogen metabolism
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
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r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: first commmitted step of gluconeogenesis
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: carbon and nitrogen metabolism
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + phosphoenolpyruvate + CO2
ADP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ATP + phosphoenolpyruvate + CO2
ADP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
Substrates: when ADP is replaced by GDP in the PEP-carboxylating reaction, PCK activity decreases approximately 5fold
Products: -
Products: -
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
Substrates: when ADP is replaced by GDP in the PEP-carboxylating reaction, PCK activity decreases approximately 5fold
Products: -
Products: -
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
Substrates: 52% of the activity with ATP
Products: -
Products: -
?
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
Substrates: 52% of the activity with ATP
Products: -
Products: -
?
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
Substrates: 36% of the activity with ATP
Products: -
Products: -
?
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
Substrates: 36% of the activity with ATP
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with IDP, GDP, ITP and GTP
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzes an exchange reaction between C14O2 and the beta-carboxyl group of oxaloacetate
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzes an exchange reaction between C14O2 and the beta-carboxyl group of oxaloacetate
Products: -
Products: -
?
additional information
?
-
-
Substrates: PEP carboxykinase utilizes 2'-dADP and 2'-dATP as substrates with kinetic and equilibrium dissociation constants very similar to those of ADP and ATP, respectively
Products: -
Products: -
?
additional information
?
-
Substrates: GDP and IDP are no substrates
Products: -
Products: -
?
additional information
?
-
Substrates: GDP and IDP are no substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: under physiological conditions the enzyme is bidirectional and is regulated primarily by mass action
Products: -
Products: -
?
additional information
?
-
-
Substrates: CO2-exchange reaction with ATP, GTP, ITP, CTP, UTP and TTP
Products: -
Products: -
?
additional information
?
-
-
Substrates: central role in energy metabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: important regulatory function of the enzyme in the amino-acid catabolism of Trypanosoma cruzi
Products: -
Products: -
?
additional information
?
-
-
Substrates: important regulatory function of the enzyme in the amino-acid catabolism of Trypanosoma cruzi
Products: -
Products: -
?
additional information
?
-
-
Substrates: CO2-exchange reaction with ATP, GTP, ITP, CTP, UTP and TTP
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + phosphoenolpyruvate + CO2
?
-
Substrates: catabolic CO2-fixing enzyme, important role in succinate formation
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
?
-
Substrates: the enzyme is responsible for the CO2 fixation
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: in contrast to its normal role in gluconeogenesis, PEP carboxykinase can operate in the reverse direction from phosphoenolpyruvate to oxaloacetate, upon knockout of pyruvate kinase in a riboflavin-producing Bacillus subtilis strain and in wild-type 168
Products: -
Products: -
r
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: synthesis of oxaloacetate is a key step in the formation of four-carbon compounds, such as malate, fumarate, and succinate
Products: -
Products: -
r
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
Substrates: -
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
Substrates: -
Products: -
Products: -
r
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
?
-
Substrates: the enzyme is neither regulatory nor inducible, the main function is catalyzing the synthesis of phosphoenopyruvate as a part of the gluconeogenetic pathway
Products: -
Products: -
?
ATP + oxaloacetate
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Substrates: the enzyme is neither regulatory nor inducible, the main function is catalyzing the synthesis of phosphoenopyruvate as a part of the gluconeogenetic pathway
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Alternanthera ficoides
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Anaerobiospirillum succiniproducens
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: key enzyme in the regulation of flux through the gluconeogenic pathway, gluconeogenic production of sugars from storage oil
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: first commmitted step of gluconeogenesis
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: carbon and nitrogen metabolism
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: critical gluconeogenic enzyme, catalyzes the first committed step in the diversion of tricarboxylic acid cycle intermediates towards gluconeogenesis
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: first commmitted step of gluconeogenesis
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: carbon and nitrogen metabolism
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: responsible for light-independent carbon fixation
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: carbon and nitrogen metabolism
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: carbon and nitrogen metabolism
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: carbon and nitrogen metabolism
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: carbon and nitrogen metabolism
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: acts in the metabolic pathways at the intersection of the glycolysis, the gluconeogenesis and the Krebs cycle, enzyme activity increases when cells are submitted to hypothermic stress
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: responsible for light-independent carbon fixation
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: carbon and nitrogen metabolism
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: first commmitted step of gluconeogenesis
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: -
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: carbon and nitrogen metabolism
Products: -
Products: -
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
Substrates: gluconeogenesis and anaplerotic reactions
Products: -
Products: -
r
ATP + phosphoenolpyruvate + CO2
ADP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
ATP + phosphoenolpyruvate + CO2
ADP + oxaloacetate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: under physiological conditions the enzyme is bidirectional and is regulated primarily by mass action
Products: -
Products: -
?
additional information
?
-
-
Substrates: central role in energy metabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: important regulatory function of the enzyme in the amino-acid catabolism of Trypanosoma cruzi
Products: -
Products: -
?
additional information
?
-
-
Substrates: important regulatory function of the enzyme in the amino-acid catabolism of Trypanosoma cruzi
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
Co2+
Mg2+
Mn2+
additional information
Co2+
-
exchange reaction: Mn2+ is the most effective divalent cation activator followed by Cd2+ and Mg2+
Mg2+
-
dual cation requirement. Mn2+ is necessary to activate, and Mn2+ or Mg2+ forms the cation-nucleotide complex as the active form of the substrate
Mg2+
-
exchange reaction: MnCl2 is the most effective divalent cation activator followed by Cd2+ and Mg2+
Mg2+
-
Mg2+ does not substitute for Mn2+, but stimulates aspartate decarboxylation in presence of Mn2+
Mn2+
-
KM: 0.048 mM for wild-type enzyme, 0.038 mM for mutant enzyme H225E, 0.16 mM for mutant enzyme D263E
Mn2+
required. Highest activity is obtained at 1 mM Mn2+ in the absence of Mg2+, the presence of 0.5 mM Mg2+ decreases the activity by a factor 2
Mn2+
-
the enzyme possesses one binding site for Mn2+ per enzyme monomer
Mn2+
-
dual cation requirement. Mn2+ is necessary to activate, and Mn2+ or Mg2+ forms the cation-nucleotide complex as the active form of the substrate
Mn2+
-
exchange reaction: Mn2+ is the most effective divalent cation activator followed by Cd2+ and Mg2+
additional information
absolute requirement for divalent cations, the most effective activator is Mn2+. Cation preference in decreasing order is Mn2+ = Co2+ >> Zn2+ > Ni2+ > Mg2+. Ca2+ and Cu2+ are completely ineffective
additional information
-
enzyme contains at least two binding sites, related to cation requirement. One binding a cation-nucleotide complex, the true substrate, and the latter site greatly enhances the affinity of the former for the cation nucleotide substrate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-Butanedione
-
phosphoenolpyruvate, ADP and Mn2+, alone or in combination protect against inactivation
Phenylglyoxal
-
phosphoenolpyruvate, ADP and Mn2+, alone or in combination protect against inactivation. Modification of only two of the three to four reactive arginine residues per enzyme subunit is responsible for inactivation
ATP
the presence of 9.6 mM ATP decreases 3folds the catalytic efficiency of the enzyme
additional information
presence of inorganic phosphate strongly reduces expression of PPCK1 and PPCK2 transcripts
-
additional information
-
presence of inorganic phosphate strongly reduces expression of PPCK1 and PPCK2 transcripts
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
malate
50% activation at 2.6 mM, Hill coeficient 1.2. In presence of Mg2+, 50% activation at 2.1 mM, Hill coeficient 14.1
additional information
NH4+, NO3- and K+ do not affect PPCK transcript abundance. Sucrose is required for the induction of PPCK2, but not PPCK1, by inorganic phosphate starvation
-
additional information
-
NH4+, NO3- and K+ do not affect PPCK transcript abundance. Sucrose is required for the induction of PPCK2, but not PPCK1, by inorganic phosphate starvation
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acidosis
The regulation of phosphoenolpyruvate carboxykinase (GTP) synthesis in rat kidney cortex. The role of acid-base balance and glucocorticoids.
Acidosis, Lactic
Cytosolic Phosphoenolpyruvate Carboxykinase Deficiency: Cause of Hypoglycemia-Induced Seizure and Death.
Adenoviridae Infections
Adenovirus E1A represses the cyclic AMP-induced transcription of the gene for phosphoenolpyruvate carboxykinase (GTP) in hepatoma cells.
Carcinoma, Hepatocellular
Adenovirus E1A represses the cyclic AMP-induced transcription of the gene for phosphoenolpyruvate carboxykinase (GTP) in hepatoma cells.
Carcinoma, Hepatocellular
Effects of amino acid analogues on protein synthesis and degradation in isolated cells.
Carcinoma, Hepatocellular
Regulation of gene expression in rat hepatocytes and hepatoma cells by insulin: quantitation of messenger ribonucleic acid's coding for tyrosine aminotransferase, tryptophan oxygenase, and phosphoenolpyruvate carboxykinase.
Carcinoma, Hepatocellular
Regulation of phosphoenolpyruvate carboxykinase gene transcription by insulin and cAMP: reciprocal actions on initiation and elongation.
Carcinoma, Hepatocellular
The role of protein synthesis in the decay of phosphoenolpyruvate carboxykinase messenger RNA.
Carcinoma, Hepatocellular
Vanadate inhibits expression of the gene for phosphoenolpyruvate carboxykinase (GTP) in rat hepatoma cells.
Chagas Disease
Crystal structure of the dimeric phosphoenolpyruvate carboxykinase (PEPCK) from Trypanosoma cruzi at 2 A resolution.
Dehydration
[Activity of NADP-dependent glyceraldehyde-phosphate dehydrogenase and phosphoenolpyruvate carboxylase in wheat leaves under water stress]
Herpes Simplex
A novel cellular protein, p60, interacting with both herpes simplex virus 1 regulatory proteins ICP22 and ICP0 is modified in a cell-type-specific manner and Is recruited to the nucleus after infection.
Hyperglycemia
SirT1 knockdown in liver decreases basal hepatic glucose production and increases hepatic insulin responsiveness in diabetic rats.
Hyperthyroidism
3,5,3'-Triiodothyronine-induced synthesis of rat liver phosphoenolpyruvate carboxykinase.
Hyperthyroidism
Renal phosphoenolpyruvate carboxykinase turnover in hypo- and hyperthyroid rat in vivo.
Hypoglycemia
Cytosolic Phosphoenolpyruvate Carboxykinase Deficiency: Cause of Hypoglycemia-Induced Seizure and Death.
Infections
A novel cellular protein, p60, interacting with both herpes simplex virus 1 regulatory proteins ICP22 and ICP0 is modified in a cell-type-specific manner and Is recruited to the nucleus after infection.
Infections
Cell-surface location of Listeria-specific protein p60--detection of Listeria cells by indirect immunofluorescence.
Insulinoma
Identification of a calcium-regulated insulinoma cell phosphoprotein as an islet cell keratin.
Neoplasms
Autoimmune expression of a cytoplasmic protein p60 in mice bearing metastasizing SV40-transformed tumors.
Neoplasms
Identification of transformation-specific proteins synthesized in cryptovirogenic mammalian cells.
Sarcoma, Avian
Staurosporine inhibits tyrosine-specific protein kinase activity of Rous sarcoma virus transforming protein p60.
Starvation
3,5,3'-Triiodothyronine-induced synthesis of rat liver phosphoenolpyruvate carboxykinase.
Starvation
cAMP stimulates transcription of the gene for cytosolic phosphoenolpyruvate carboxykinase in rat liver nuclei.
Starvation
Characterization and functional analysis of phosphoenolpyruvate carboxylase kinase genes in rice.
Starvation
Induction of rat liver phosphoenolpyruvate carbonxykinase (GTP) by cyclic AMP during starvation. The permissive action of glucocorticoids.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
MnATP2- as substrate, for S252A mutant Km above 3000 microM
-
0.01
ADP
-
mutant enzyme E299A, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.013
ADP
-
mutant enzyme Y207L, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.016
ADP
-
wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.034
ADP
-
wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.077
ADP
for the pyruvate kinase-like activity of S252A mutant
0.099
ADP
-
mutant enzyme L460A, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.17
ADP
-
F216Y: kinetic parameter in the PEP carboxylation direction
0.026
ATP
-
mutant enzyme E299A, in 100 mM MOPS buffer (pH 7.0), at 30°C
0.03
ATP
-
wild type enzyme, in 100 mM MOPS buffer (pH 7.0), at 30°C
0.204
ATP
-
mutant enzyme L460A, in 100 mM MOPS buffer (pH 7.0), at 30°C
0.024
CO2
-
F216Y: kinetic parameter in the PEP carboxylation direction
0.36
CO2
-
condition: 0.1 mM Mn2+, 5 mM Mg2 /Vmax: 16 micromol/min/mg
1.9
CO2
-
condition: 0.1 mM Mn2+, 5 mM Mg2 /Vmax: 37 micromol/min/mg
2 - 3
CO2
-
mutant enzyme K212M, in 100 mM MOPS buffer (pH 6.6), at 30°C
8.4
CO2
-
condition: 4 mM Mn2+ /Vmax: 47 micromol/min/mg
9
CO2
-
mutant enzyme E272Q, in 100 mM MOPS buffer (pH 6.6), at 30°C
11
CO2
-
mutant enzyme K213Q, in 100 mM MOPS buffer (pH 6.6), at 30°C
14
CO2
-
mutant enzyme E284Q, in 100 mM MOPS buffer (pH 6.6), at 30°C
14
CO2
-
mutant enzyme L460A, in 100 mM MOPS buffer (pH 6.6), at 30°C
29
CO2
-
mutant enzyme Y207L, in 100 mM MOPS buffer (pH 6.6), at 30°C
47
CO2
-
mutant enzyme E299A, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.012
Mn2+
-
pH high (pH range:6-8.4), pH:12, PEP carboxylation direction
0.056
Mn2+
-
F216Y: kinetic parameter in the PEP carboxylation direction
0.345
Mn2+
-
F216Y: kinetic parameter in the PEP formation direction
0.066
oxalacetate
-
kinetic parameter in the PEP formation direction
0.122
oxalacetate
for the oxaloacetate decarboxylase activity of wild-type
1.079
oxalacetate
-
F216Y: kinetic parameter in the PEP formation direction
5.2
oxalacetate
for the oxaloacetate decarboxylase activity of S252A mutant
0.014
oxaloacetate
-
condition: + 2 mM ADP /Vmax: 0.32 micromol/min/mg
0.024
oxaloacetate
-
mutant enzyme K213Q, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.051
oxaloacetate
-
mutant enzyme L460A, in 100 mM MOPS buffer (pH 7.0), at 30°C
0.066
oxaloacetate
-
wild type enzyme, in 100 mM MOPS buffer (pH 7.0), at 30°C
0.068
oxaloacetate
-
mutant enzyme K212M, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.079
oxaloacetate
-
condition: no ADP /Vmax: 3.27 micromol/min/mg
0.13
oxaloacetate
-
wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.13
oxaloacetate
-
mutant enzyme E299A, in 100 mM MOPS buffer (pH 7.0), at 30°C
0.2
oxaloacetate
-
mutant enzyme K212R, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.238
oxaloacetate
-
mutant enzyme E272Q, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.99
oxaloacetate
-
condition: + 2 mM ADP /Vmax: 3.36 micromol/min/mg
2
oxaloacetate
-
Km above 2.0 mM, mutant enzyme E284Q, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.037
phosphoenolpyruvate
for the pyruvate kinase-like activity of S252A mutant
0.085
phosphoenolpyruvate
-
pH 6.5, 30°C, mutant enzyme H225E
0.104
phosphoenolpyruvate
-
mutant enzyme L460A, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.108
phosphoenolpyruvate
-
mutant enzyme E299A, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.135
phosphoenolpyruvate
for the pyruvate kinase-like activity of wild-type
0.17
phosphoenolpyruvate
-
mutant enzyme E284Q, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.185
phosphoenolpyruvate
-
mutant enzyme E272Q, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.216
phosphoenolpyruvate
-
mutant enzyme K212M, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.219
phosphoenolpyruvate
-
pH 6.5, 30°C, wild-type enzyme
0.289
phosphoenolpyruvate
-
pH 6.5, 30°C, mutant enzyme D263E
0.307
phosphoenolpyruvate
-
kinetic parameter in the PEP carboxylation direction
0.307
phosphoenolpyruvate
-
wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.32
phosphoenolpyruvate
-
mutant enzyme K213Q, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.5
phosphoenolpyruvate
-
mutant enzyme Y207L, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.651
phosphoenolpyruvate
-
mutant enzyme K212R, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.917
phosphoenolpyruvate
-
F216Y: kinetic parameter in the PEP carboxylation direction
3
phosphoenolpyruvate
-
wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kcat for oxalacetate as a substrate is above 19 1/s for S252A mutant in the phosphoenolpyruvate formation direction
-
13
ADP
-
mutant enzyme L460A, in 100 mM MOPS buffer (pH 6.6), at 30°C
18
ADP
-
mutant enzyme E299A, in 100 mM MOPS buffer (pH 6.6), at 30°C
3 - 6
ATP
-
mutant enzyme L460A, in 100 mM MOPS buffer (pH 7.0), at 30°C
32
ATP
-
mutant enzyme E299A, in 100 mM MOPS buffer (pH 7.0), at 30°C
0.32
oxalacetate
for the oxaloacetate decarboxylase activity of wild-type
1
oxalacetate
for the oxaloacetate decarboxylase activity of S252A mutant
65
oxalacetate
wild-type, apparent kinetic parameters for wild-type in the phosphoenolpyruvate formation direction
0.08
oxaloacetate
-
mutant enzyme E272Q, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.08
oxaloacetate
-
Km above 2.0 mM, mutant enzyme E284Q, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.11
oxaloacetate
-
mutant enzyme K212R, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.28
oxaloacetate
-
wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.58
oxaloacetate
-
mutant enzyme K213Q, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.85
oxaloacetate
-
mutant enzyme K212M, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.014
phosphoenolpyruvate
-
mutant enzyme K212R, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.07
phosphoenolpyruvate
-
mutant enzyme E284Q, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.13
phosphoenolpyruvate
-
mutant enzyme K212M, in 100 mM MOPS buffer (pH 6.6), at 30°C
0.2
phosphoenolpyruvate
for the pyruvate kinase-like activity of S252A mutant
0.5
phosphoenolpyruvate
S252A mutant, apparent kinetic parameters for S252A mutant in the phosphoenolpyruvate carboxylation direction
0.8
phosphoenolpyruvate
for the pyruvate kinase-like activity of wild-type
5.1
phosphoenolpyruvate
-
mutant enzyme K213Q, in 100 mM MOPS buffer (pH 6.6), at 30°C
19
phosphoenolpyruvate
-
mutant enzyme E272Q, in 100 mM MOPS buffer (pH 6.6), at 30°C
62
phosphoenolpyruvate
wild-type, apparent kinetic parameters for wild-type in the phosphoenolpyruvate carboxylation direction
63
phosphoenolpyruvate
-
wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
130
ADP
-
mutant enzyme L460A, in 100 mM MOPS buffer (pH 6.6), at 30°C
1800
ADP
-
wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C
1800
ADP
-
mutant enzyme E299A, in 100 mM MOPS buffer (pH 6.6), at 30°C
180
ATP
-
mutant enzyme L460A, in 100 mM MOPS buffer (pH 7.0), at 30°C
1200
ATP
-
mutant enzyme E299A, in 100 mM MOPS buffer (pH 7.0), at 30°C
1300
ATP
-
wild type enzyme, in 100 mM MOPS buffer (pH 7.0), at 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
27
D-fructose 6-phosphate
Arabidopsis thaliana
Hill coefficient 0.9, pH 7, 30°C
8.1
D-glucose 6-phosphate
Arabidopsis thaliana
Hill coefficient 1.5, pH 7, 30°C
19
2-oxoglutarate
Arabidopsis thaliana
presence of Mg2+, Hill coefficient 1.1, pH 7, 30°C
10.3
citrate
Arabidopsis thaliana
presence of Mg2+, Hill coefficient 1.5, pH 7, 30°C
11
citrate
Arabidopsis thaliana
presence of Mg2+, Hill coefficient 2.3, pH 7, 30°C
16
D-fructose 1,6-bisphosphate
Arabidopsis thaliana
Hill coefficient 1.2, pH 7, 30°C
43
D-fructose 1,6-bisphosphate
Arabidopsis thaliana
Hill coefficient 0.8, pH 7, 30°C
9.6
fumarate
Arabidopsis thaliana
presence of Mg2+, Hill coefficient 1.9, pH 7, 30°C
6.1
N-phosphomethylglycine
Arabidopsis thaliana
Hill coefficient 0.8, pH 7, 30°C
21
N-phosphomethylglycine
Arabidopsis thaliana
Hill coefficient 0.9, pH 7, 30°C
14.5
succinate
Arabidopsis thaliana
presence of Mg2+, Hill coefficient 3.5, pH 7, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.1
-
exchange reaction between 14CO2 and the beta-carboxyl group of oxaloacetate
6.5
6.9
additional information
additional information
expression of the two PPCK genes and the phosphorylation state of PEPC are increased in response to increasing intracellular pH
additional information
-
expression of the two PPCK genes and the phosphorylation state of PEPC are increased in response to increasing intracellular pH
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
ratio of the two values is pH-dependent and a calibration curve is constructed measuring the fluorescence of free BCECF over the pH range 4-8
5.3 - 7.5
-
pH 5.3: about 30% of maximal activity, pH 7.5: about 25% of maximal activity, oxaloacetate formation
6 - 8.5
6.3 - 9.3
-
pH 6.3: about 35% of maximal activity, pH 9.3: about 30% of maximal activity, phosphoenolpyruvate formation
additional information
-
it is shown that Mn2+ affinity increases as the pH increases
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 53
-
in presence of phosphoenolpyruvate and MnCl2, 50% loss of enzyme activity at 52.5°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
PPCK2 gene; ecotype Col0 and Landsberg erecta ecotype
UniProt
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the enzyme is present in the companion cells of the adaxial phloem of minor veins, the internal and external phloem of vascular bundles in petioles and stems, the phloem in roots and the eextra-fascicular phloem in leaves, cotyledons, petioles and stems
brenda
-
the enzyme is present in the companion cells of the adaxial phloem of minor veins, the internal and external phloem of vascular bundles in petioles and stems, the phloem in roots and the eextra-fascicular phloem in leaves, cotyledons, petioles and stems
brenda
additional information
-
abundance of the enzyme is greatly increased by watering plants with a solution of ammonium chloride at low, but not at high pH
brenda
-
abundance of the enzyme is greatly increased by watering plants with a solution of ammonium chloride at low, but not at high pH
brenda
additional information
-
OsPPCK1 are highly expressed in roots and at low levels in other organs
brenda
additional information
-
OsPPCK3 is highly expressed in roots and at low levels in other organs
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
lack of phosphoenolpyruvate carboxykinase leads to activation of AMP-activated protein kinase, which inhibits cAMP-induced steroidogenic gene promoter activity and gene expression
malfunction
-
Brucella suis 513 attenuation occurrs only in the double phosphoenolpyruvate carboxykinase (PckA) / pyruvate phosphate dikinase (PpdK) mutant
metabolism
-
Brucella suis 513 used pyruvate phosphate dikinase (PpdK) and phosphoenolpyruvate carboxykinase (PckA) for phosphoenolpyruvate synthesis in vitro
metabolism
glutamate dehydrogenase GDH2- and PEPCK-catalyzed reactions are essential for ATP generation and gluconeogenesis respectively during carbon starvation and glutamate catabolism. GDH2 and PEPCK reciprocally regulate each other's protein levels during glutamate catabolism such that GDH2 is downregulated in PEPCK mutants and PEPCK is downregulated in GDH2 mutant strains. Sequential conversion of glutamate to 2-oxoglutarate and oxaloacetate by GDH2 and AAT2, respectively, is essential for PEPCK synthesis in cells metabolizing glutamate. Translation of GDH2 mRNA is induced by glutamate while oxaloacetate derived from glutamate is likely to be the inducer of PEPCK mRNA translation during glutamate catabolism
metabolism
-
glutamate dehydrogenase GDH2- and PEPCK-catalyzed reactions are essential for ATP generation and gluconeogenesis respectively during carbon starvation and glutamate catabolism. GDH2 and PEPCK reciprocally regulate each other's protein levels during glutamate catabolism such that GDH2 is downregulated in PEPCK mutants and PEPCK is downregulated in GDH2 mutant strains. Sequential conversion of glutamate to 2-oxoglutarate and oxaloacetate by GDH2 and AAT2, respectively, is essential for PEPCK synthesis in cells metabolizing glutamate. Translation of GDH2 mRNA is induced by glutamate while oxaloacetate derived from glutamate is likely to be the inducer of PEPCK mRNA translation during glutamate catabolism
-
metabolism
Brucella suis 513
-
Brucella suis 513 used pyruvate phosphate dikinase (PpdK) and phosphoenolpyruvate carboxykinase (PckA) for phosphoenolpyruvate synthesis in vitro
-
physiological function
-
the enzyme is required for steroidogenesis in testicular Leydig cells
physiological function
-
Danio rerio larvae show increased V-ATPase-mediated acid secretion and transient expression of Pck1, in response to acid stress. Pck1 gene knockdown decreases the H+ secretion via V-ATPase, the effect is rescued by supplementation of glucose into the yolk. Pck1 knockdown does not affect glutamine/glutamate catalysis
physiological function
-
both phosphoenolpyruvate carboxykinase and diphosphate-dependent pyruvate phosphate dikinase colocalize with glycolytic enzymes within the glycosomes of Trypanosoma evansi. Both enzymes can make use of PEP for contributing to the production of ATP within the organelles
physiological function
-
Brucella suis biovar 5 depends on phosphoenolpyruvate carboxykinase and pyruvate phosphate dikinase for full virulence in laboratory models
physiological function
-
both phosphoenolpyruvate carboxykinase and diphosphate-dependent pyruvate phosphate dikinase colocalize with glycolytic enzymes within the glycosomes of Trypanosoma evansi. Both enzymes can make use of PEP for contributing to the production of ATP within the organelles
-
physiological function
Brucella suis 513
-
Brucella suis biovar 5 depends on phosphoenolpyruvate carboxykinase and pyruvate phosphate dikinase for full virulence in laboratory models
-
Show AA Sequence and Transmembrane Helices (14361 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
251000
252000
-
gel filtration, calculation from sedimentation and diffusion data
400000
-
the 12 000 Da N-terminal extension is likely to project from the molecule and increase its Stokes radius, gel filtration
56000
60000
61000
65000
-
equilibrium sedimentation under non-denaturing conditions, non-denaturing PAGE in presence of detergent, sucrose density gradient centrifugation
74000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
homotetramer
monomer
tetramer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
the enzyme is reversibly phosphorylated and the phosphorylation process is regulated in vivo by light
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.85 A and 1.7 A resolution structures of the native and pyruvate/Mn2+/phosphate complex, space group of native enzyme is P4(3), space group for enzyme complex is P2(1), unit-cell parameters for native enzyme: a = b = 102.09 A, c = 72.12 A, beta = 90°. Unit-cell parameters for the enzyme complex: a = 56.74 A, b = 55.09 A, c = 90.08 A, beta = 106.17°
hanging drop vapor diffusion method. 2.2 A resolution crystal structure of the enzyme complexed with ATP, Mg2+, Mn2+ and the transition state analogue oxalate. 2.4 A resolution structure of the native enzyme. Unit cell dimensions of the enzyme complex: a = 194.87 A, b = 123.22 A, c = 48.46 A, alpha = beta = gamma = 90°C. Unit cell dimensions of the native enzyme: a = 129.66 A, b = 55.73 A, c = 139.4 A, alpha = 90°, beta = 93.77°, gamma = 90°
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
-
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
-
structures of mutants K254S, D269N, S250A, to 1.65, 1.66 and 1.70 A resolution, respectively
three-dimensional crystal structure, enzyme possesses a mononucleotide-binding domain unique from other proteins having the P-loop motif
oil-microbatch method, the unliganded form crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 64.7, b = 129.91 A, c = 173.39 A. The ATP-liganded crystals are nearly isomorphous to the unliganded crystals. They belong to space group P2(1)2(1)2(1), with unit cell parameters a = 64.07 A, b = 130.55 A, c = 174.2 A
sitting drop vapour diffusion, primitive orthorhombic crystals, space group P2(1)2(1)2(1), a : 65.97 A, b : 107.61 A, c : 179.08 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D263E
-
16800fold reduction in maximal velocity compared to wild-type enzyme, KM-value for ADP is 1.8fold lower than wild-type value, KM-value for phosphoenolpyruvate is 1.3fold higher than wild-type value, KM-value for HCO3- is 1.1fold lower than wild-type value
H225E
-
600fold reduction in maximal velocity compared to wild-type enzyme, KM-value for ADP is 2.4fold lower than wild-type value, KM-value for phosphoenolpyruvate is 2.6fold lower than wild-type value, KM-value for HCO3- is 1.1fold higher than wild-type value
D269N
residue is part of the coordination sphere of Mn2+, mutation reduces kcat by 14fold, and significantly increases the Km values for Mn2+ and oxaloacetate
H232Q
residue is part of the coordination sphere of Mn2+, mutation reduces kcat by 14fold, and significantly increases the Km values for Mn2+ and oxaloacetate
K213S
no detectable activity in the presence of Mn2+. When assayed with MgATP and oxaloacetate alone, K213S displays a 7.8fold reduction in kcat
K254S
muutation in a key residue in the P-loop motif that interacts with MgATP, significantly elevates the Km value for MgATP and reduces kcat
R333Q
key residue that interacts with oxaloacetate. The mutation significantly reduces kcat
R65Q
key residue that interacts with oxaloacetate. The mutation significantly increases the Km value for oxaloacetate
S250A
3-fold increased Km value oxaloacetate, 10fold increased Km value for MgATP and 1.4fold reduced kcat
D269N
-
residue is part of the coordination sphere of Mn2+, mutation reduces kcat by 14fold, and significantly increases the Km values for Mn2+ and oxaloacetate
-
H232Q
-
residue is part of the coordination sphere of Mn2+, mutation reduces kcat by 14fold, and significantly increases the Km values for Mn2+ and oxaloacetate
-
K254S
-
muutation in a key residue in the P-loop motif that interacts with MgATP, significantly elevates the Km value for MgATP and reduces kcat
-
R333Q
-
key residue that interacts with oxaloacetate. The mutation significantly reduces kcat
-
R65Q
-
key residue that interacts with oxaloacetate. The mutation significantly increases the Km value for oxaloacetate
-
H205Q
mutation remarkably diminishes the activity, Km value for Mn2+ is 250fold increased
Y180F
2- and 8fold decrease in specific acitvity for the oxaloacetate- and phosphoenolpyruvate-forming reactions, respectively
E272Q
-
the mutation increases the activation constant for Mn2+ in the main reaction of the enzyme 11fold
E284Q
-
the mutation increases the activation constant for Mn2+ in the main reaction of the enzyme 69fold, the mutation changes the nucleotide-independent oxalacetate decarboxylase activity of PEP carboxykinase into an ADP-requiring activity
F216Y
H233Q
-
mutation leads to less polar environment for the phosphoryridoxyl group, decreased binding affinity of phosphoenolpyruvate
K212M
-
the mutation increases the activation constant for Mn2+ in the main reaction of the enzyme 17fold, the mutation changes the nucleotide-independent oxalacetate decarboxylase activity of PEP carboxykinase into an ADP-requiring activity
K212R
-
the mutation does not affect the Mn2+ affinity of the enzyme
K213Q
-
the mutation increases the activation constant for Mn2+ in the main reaction of the enzyme 107fold, the mutation changes the nucleotide-independent oxalacetate decarboxylase activity of PEP carboxykinase into an ADP-requiring activity
K214R
-
mutation leads to less polar environment for the phosphoryridoxyl group, decreased binding affinity of phosphoenolpyruvate
L460A
-
the mutation decreases the catalytic efficiency to about 14% of the wild type value as a consequence of the 7fold increase in the Km (ATP-Mn2-). The mutation decreases the catalytic efficiency to about 7% of the wild type value as a consequence of the 3fold increase in Km (ADP-Mn-) and the reduction in kcat
R70K
-
1.7fold increase in KM-value for ADP, 1.3fold increase in KM-value for phosphoenolpyruvate, 1.4fold increase in KM-value for HCO3-
R70M
-
2.5fold increase in KM-value for ADP, 2.4fold increase in KM-value for phosphoenolpyruvate, 1.8fold decrease in KM-value for HCO3-
R70Q
-
1.9fold increase in KM-value for ADP, 2.3fold increase in KM-value for phosphoenolpyruvate, 1.1fold increase in KM-value for HCO3-
additional information
-
metabolic control of liver gluconeogenesis is quantified in groups of knock-out mice with varying PEPCK protein content. Livers with a 90% reduction in PEPCK content show only a 40% reduction in gluconeogenic flux, indicating a lower than expected capacity for PEPCK protein content to control gluconeogenesis. PEPCK flux correlates tightly with TCA cycle activity, suggesting that under some conditions in mice, PEPCK expression must coordinate with hepatic energy metabolism to control gluconeogenesis
F216Y
-
Km: 0.075 (MnADP-), 0.323 (phosphoenolpyruvate), 17 (HCO3-), 0.063 (Mn2+). Mutation Phe216Tyr shows that the introduction of a hydroxyl group in the lateral chain of the residue produces a substantial loss in the enzyme affinity for Mn2+, suggesting an increase of the pKa of Lys213
F216Y
-
kinetic parameter in the PEP formation direction: Km: 0.016 mM (MnATP2-), 1.079 mM (oxalacetate), 0.345 mM (Mn2+)
F216Y
-
kinetic parameter in the PEP carboxylation direction: Km: 0.170 mM (MnADP-), 0.917 mM (phosphoenolpyruvate), 0.056 mM (Mn2+), 0.024 mM (HCO3-)
F216Y
-
mutation Phe216Tyr shows that the introduction of a hydroxyl group in the lateral chain of the residue produces a substantial loss in the enzyme affinity for Mn2+, suggesting an increase of the pKa of Lys213
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 56
-
in presence of phosphoenolpyruvate and MnCl2, 50% loss of enzyme activity at 55.5°C
20 - 66
-
in presence of phosphoenolpyruvate and MnCl2, 50% loss of enzyme activity at 66°C
30
-
remaining activity after 214 h: 57% in presence of 20% v/v glycerol, 37% in presence of 1 mM NaCl, 31% in presence of 1 mM KCl, 28% in absence of salts
90
-
about 50% loss of activity after 20 min, about 90% loss of activity after 45 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-196°C, stored in 50% glycerol in liquid nitrogen, stable for more than 3 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap chelating affinity column chromatography and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned in Escherichia coli and in in the PEP carboxykinase-deficient Saccharomyces cerevisiae-strain PUK-3B
-
expressed in pyruvate carboxylase-negative Saccharomyces cerevisiae strain IMK157, IMW001, and IMW002
-
expressed in the PEP carboxykinase-deficient Saccharomyces cerevisiae strain PUK-3B
-
expression in Escherichia coli K-12. PEPCK overexpression has no effect on succinate fermentation. In contrast, in the phosphoenolpyruvate carboxylase mutant Escherichia coli strain K-12 ppc::kan, PEPCL overexpression increases succinate production 6.5fold
-
increasing the acetyl-CoA pool in the presence of overexpressed phosphoenolpyruvate carboxylase enhances succinate production in Escherichia coli
-
mutant enzyme Y207L is expressed in the PEP carboxykinase-deficient Saccharomyces cerevisiae strain PUK-3B
-
mutant plasmid is transformed into the phosphoenolpyruvate carboxykinase-deficient yeast strain PUK-3B (MATalpha pck ura3)
transformed into the PEP carboxykinase-deficient yeast strain PUK-3B (MATalpha pck ura3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
pubertal mouse (8-week-old) testes and human chorionic gonadotropin-induced prepubertal mouse testes show increased enzyme expression
-
the effects of ischemic stroke on the PCK expression are seen predominately in astrocytes
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
analysis
direct assay using liquid chromatography-tandem mass spectrometry to quantify PEP, in coelution with oxaloacete
medicine
Trypanosoma cruzi is the causative agent of Chagas' disease, enzyme is a good target for the development of new anti-chagasic drugs
medicine
-
cellular PEP levels parallel extracellular glucose in colon carcinoma cell lines, HCT-116 and SW480. PEP correlates with cytosolic calcium and NFAT activity, together with transcriptional up-regulation of canonical targets PTGS2 and IL6. Inhibition of PEPCK activity shows the regulation of PEP and calcium levels and consequential downstream modulation of NFAT and c-Myc activities
medicine
reactive oxygen species, lactate, phosphoenolpyruvate, mRNA, and protein of total PCK, PCK-1, and PCK-2 increase after intraluminal middle cerebral artery occlusion andoxygen-glucose deprivation. Oxaloacetate level decreases, while PEP and glucose are increased. These changes are attenuated by phenothiazine, 3-mercaptopicolinic acid, or PCK shRNA
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brenda
Geng, X.; Shen, J.; Li, F.; Yip, J.; Guan, L.; Rajah, G.; Peng, C.; DeGracia, D.; Ding, Y.
Phosphoenolpyruvate carboxykinase (PCK) in the brain gluconeogenic pathway contributes to oxidative and lactic injury after stroke
Mol. Neurobiol.
58
2309-2321
2021
Rattus norvegicus (P07379)
brenda
Dey, T.; Rangarajan, P.N.
Posttranscriptional regulation of glutamate dehydrogenase 2 and phosphoenolpyruvate carboxykinase in Komagataella phaffii
Yeast
39
337-347
2022
Komagataella phaffii (C4QZB8), Komagataella phaffii GS115 (C4QZB8)
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