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Information on EC 4.1.1.49 - phosphoenolpyruvate carboxykinase (ATP)
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4.1.1.49 phosphoenolpyruvate carboxykinase (ATP)Specify your search results
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- 4.1.1.49
-
pepcs
- monocytogenes
-
crassulacean
-
anti-p60
- fedtschenkoi
- grayi
- sanguinalis
-
6.4.1.1
-
digitaria
- medicine
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
ADP-linked PEP carboxykinase, ATP, oxaloacetate carboxy-lyase (transphosphorylating), ATP-dependent phosphoenolpyruvate carboxykinase, ATP-dependent phosphoenolpyruvate(PEP)carboxykinase, ATP-forming PEP-carboxykinase, ATP-oxaloacetate carboxylase (transphosporylating), ATP: oxaloacetate carboxy-lyase, ATP:oxaloacetate carboxy-lyase, ATP:oxaloacetate carboxylyase (transphosphorylating), Carboxykinase, phosphopyruvate (adenosine triphosphate), 
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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 (transphosporylating)
ATP:oxaloacetate carboxy-lyase
transphosphorylating, interacts also with GTP, EC 4.1.1.32
Carboxykinase, phosphopyruvate (adenosine triphosphate)
-
-
-
-
Glycosomal protein P60
-
-
-
-
PCK
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
-
-
-
-
Phosphoenolpyruvic carboxylase
-
-
-
-
phosphopyruvate carboxykinase
-
-
-
-
Phosphopyruvate carboxykinase (adenosine triphosphate)
-
-
-
-
PPC
Protein p60
-
-
-
-
PEP carboxykinase
-
-
-
-
PEP carboxykinase
-
-
PEP carboxylase
-
-
-
-
PEPCK
-
-
-
-
phosphoenolpyruvate carboxykinase
-
-
-
-
phosphoenolpyruvate carboxykinase
-
-
Phosphoenolpyruvate carboxylase
-
-
-
-
phosphoenolpyruvate(PEP)carboxykinase (GTP/ATP:oxaloacetate carboxy-lyase (transphosphorylating)EC 4.1.1.32/49)
-
-
phosphoenolpyruvate(PEP)carboxykinase (GTP/ATP:oxaloacetate carboxy-lyase (transphosphorylating)EC 4.1.1.32/49)
-
-
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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PATHWAY SOURCE
PATHWAYS
KEGG
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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
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
CTP + oxaloacetate
CDP + phosphoenolpyruvate + CO2
-
15% of the activity with ATP
-
-
-
TTP + oxaloacetate
TDP + phosphoenolpyruvate + CO2
-
16% of the activity with ATP
-
-
-
UTP + oxaloacetate
UDP + phosphoenolpyruvate + CO2
-
20% of the activity with ATP
-
-
-
ADP + (E)-3-fluorophosphoenolpyruvate + CO2
ATP + 3-fluorooxaloacetate
-
-
-
-
?
ADP + (E)-3-fluorophosphoenolpyruvate + CO2
ATP + 3-fluorooxaloacetate
-
-
-
?
ADP + (Z)-3-fluorophosphoenolpyruvate + CO2
ATP + 3-fluorooxaloacetate
-
-
-
-
?
ADP + (Z)-3-fluorophosphoenolpyruvate + CO2
ATP + 3-fluorooxaloacetate
-
-
-
?
ADP + phosphoenolpyruvate + CO2
?
-
catabolic CO2-fixing enzyme, important role in succinate formation
-
-
-
ADP + phosphoenolpyruvate + CO2
?
-
the enzyme is responsible for the CO2 fixation
-
-
-
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
-
-
-
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
-
-
-
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
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
-
-
r
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
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
-
-
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
synthesis of oxaloacetate is a key step in the formation of four-carbon compounds, such as malate, fumarate, and succinate
-
r
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
-
-
-
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
-
-
-
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
Arg70 is important for catalytic efficiency of the enzyme and for binding of phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
-
r
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
ATP + oxaloacetate
?
-
the enzyme is neither regulatory nor inducible, the main function is catalyzing the synthesis of phosphoenopyruvate as a part of the gluconeogenetic pathway
-
-
-
ATP + oxaloacetate
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
the enzyme is neither regulatory nor inducible, the main function is catalyzing the synthesis of phosphoenopyruvate as a part of the gluconeogenetic pathway
-
-
-
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
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
-
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Anaerobiospirillum succiniproducens
-
-
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Anaerobiospirillum succiniproducens
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
key enzyme in the regulation of flux through the gluconeogenic pathway, gluconeogenic production of sugars from storage oil
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
first commmitted step of gluconeogenesis
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
carbon and nitrogen metabolism
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
critical gluconeogenic enzyme, catalyzes the first committed step in the diversion of tricarboxylic acid cycle intermediates towards gluconeogenesis
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
first commmitted step of gluconeogenesis
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
carbon and nitrogen metabolism
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
responsible for light-independent carbon fixation
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
carbon and nitrogen metabolism
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
carbon and nitrogen metabolism
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
carbon and nitrogen metabolism
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
-
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
carbon and nitrogen metabolism
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
ADP is the preferred PCK phosphate acceptor
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
ADP is the preferred PCK phosphate acceptor
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
-
-
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
interacts also with GTP, EC 4.1.1.32
-
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
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
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
responsible for light-independent carbon fixation
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
carbon and nitrogen metabolism
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
first commmitted step of gluconeogenesis
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
carbon and nitrogen metabolism
-
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
when ADP is replaced by GDP in the PEP-carboxylating reaction, PCK activity decreases approximately 5fold
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
when ADP is replaced by GDP in the PEP-carboxylating reaction, PCK activity decreases approximately 5fold
-
-
r
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
52% of the activity with ATP
-
-
-
GTP + oxaloacetate
GDP + phosphoenolpyruvate + CO2
-
52% of the activity with ATP
-
-
-
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
36% of the activity with ATP
-
-
-
ITP + oxaloacetate
IDP + phosphoenolpyruvate + CO2
-
36% of the activity with ATP
-
-
-
additional information
?
-
-
no activity with IDP, GDP, ITP and GTP
-
-
-
additional information
?
-
-
catalyzes an exchange reaction between C14O2 and the beta-carboxyl group of oxaloacetate
-
-
-
additional information
?
-
-
catalyzes an exchange reaction between C14O2 and the beta-carboxyl group of oxaloacetate
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
GDP and IDP are no substrates
-
?
additional information
?
-
-
under physiological conditions the enzyme is bidirectional and is regulated primarily by mass action
-
-
-
additional information
?
-
-
CO2-exchange reaction with ATP, GTP, ITP, CTP, UTP and TTP
-
-
-
additional information
?
-
-
important regulatory function of the enzyme in the amino-acid catabolism of Trypanosoma cruzi
-
-
-
additional information
?
-
-
important regulatory function of the enzyme in the amino-acid catabolism of Trypanosoma cruzi
-
-
-
additional information
?
-
-
CO2-exchange reaction with ATP, GTP, ITP, CTP, UTP and TTP
-
-
-
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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
ADP + phosphoenolpyruvate + CO2
?
-
catabolic CO2-fixing enzyme, important role in succinate formation
-
-
-
ADP + phosphoenolpyruvate + CO2
?
-
the enzyme is responsible for the CO2 fixation
-
-
-
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
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
-
-
r
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
synthesis of oxaloacetate is a key step in the formation of four-carbon compounds, such as malate, fumarate, and succinate
-
r
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
-
-
-
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
-
-
-
?
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
-
r
ATP + oxaloacetate
?
-
the enzyme is neither regulatory nor inducible, the main function is catalyzing the synthesis of phosphoenopyruvate as a part of the gluconeogenetic pathway
-
-
-
ATP + oxaloacetate
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
the enzyme is neither regulatory nor inducible, the main function is catalyzing the synthesis of phosphoenopyruvate as a part of the gluconeogenetic pathway
-
-
-
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
Anaerobiospirillum succiniproducens
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
key enzyme in the regulation of flux through the gluconeogenic pathway, gluconeogenic production of sugars from storage oil
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
first commmitted step of gluconeogenesis
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
carbon and nitrogen metabolism
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
critical gluconeogenic enzyme, catalyzes the first committed step in the diversion of tricarboxylic acid cycle intermediates towards gluconeogenesis
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
first commmitted step of gluconeogenesis
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
carbon and nitrogen metabolism
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
responsible for light-independent carbon fixation
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
carbon and nitrogen metabolism
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
carbon and nitrogen metabolism
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
carbon and nitrogen metabolism
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
carbon and nitrogen metabolism
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
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
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
responsible for light-independent carbon fixation
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
carbon and nitrogen metabolism
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
first commmitted step of gluconeogenesis
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
carbon and nitrogen metabolism
-
?
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
ATP + oxaloacetate
ADP + phosphoenolpyruvate + CO2
-
gluconeogenesis and anaplerotic reactions
-
r
additional information
?
-
-
under physiological conditions the enzyme is bidirectional and is regulated primarily by mass action
-
-
-
additional information
?
-
-
important regulatory function of the enzyme in the amino-acid catabolism of Trypanosoma cruzi
-
-
-
additional information
?
-
-
important regulatory function of the enzyme in the amino-acid catabolism of Trypanosoma cruzi
-
-
-
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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+
-
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; Km: 0.97 mM
Mn2+
-
one Mn2+ is required for the activation of each 42000 Da subunit; strictly dependent on
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
additional information
presence of inorganic phosphate strongly reduces expression of PPCK1 and PPCK2 transcripts
-
ATP
-
the presence of 9.6 mM ATP decreases 3folds the catalytic efficiency of the enzyme
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.099
ADP
-
mutant enzyme L460A, in 100 mM MOPS buffer (pH 6.6), at 30°C
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
0.36
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
0.024
HCO3-
-
F216Y: kinetic parameter in the PEP carboxylation direction
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
0.077
MnADP-
-
for the pyruvate kinase-like activity of S252A mutant
0.17
MnADP-
-
F216Y: kinetic parameter in the PEP carboxylation direction
0.016
MnATP2-
-
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
-
Km above 2.0 mM, mutant enzyme E284Q, in 100 mM MOPS buffer (pH 6.6), at 30°C; mutant enzyme E272Q, 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
-
mutant enzyme E299A, in 100 mM MOPS buffer (pH 6.6), at 30°C; wild type enzyme, 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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.31
-
in 50 mM Tris-HCl (pH 8.0) and 5 mM dithiothreitol, at 55°C
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
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
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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
-
OsPPCK1 are highly expressed in roots and at low levels in other organs; OsPPCK3 is highly expressed in roots and at low levels in other organs
brenda