Phosphoenolpyruvate carboxykinase (ATP)

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Phosphoenolpyruvate carboxykinase (ATP)
Phosphoenolpyruvate carboxykinase (ATP)
Identifiers
EC no.	4.1.1.49
CAS no.	9073-94-3
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

Phosphoenolpyruvate carboxykinase (ATP) (EC 4.1.1.49, phosphopyruvate carboxylase (ATP), phosphoenolpyruvate carboxylase, phosphoenolpyruvate carboxykinase, phosphopyruvate carboxykinase (adenosine triphosphate), PEP carboxylase, PEP carboxykinase, PEPCK (ATP), PEPK, PEPCK, phosphoenolpyruvic carboxylase, phosphoenolpyruvic carboxykinase, phosphoenolpyruvate carboxylase (ATP), phosphopyruvate carboxykinase, ATP:oxaloacetate carboxy-lyase (transphosphorylating)) is an enzyme with systematic name ATP:oxaloacetate carboxy-lyase (transphosphorylating; phosphoenolpyruvate-forming).^[1]^[2]^[3] This enzyme catalyses the following chemical reaction

ATP + oxaloacetate

\rightleftharpoons

ADP + phosphoenolpyruvate + CO₂

References

^ Cannata, J.J.B. (1970). "Phosphoenolpyruvate carboxykinase from bakers' yeast. Isolation of the enzyme and study of its physical properties". J. Biol. Chem. 245: 792–798. PMID 5416663.
^ Cannata, J.J.B.; Stoppani, A.O.M. (1963). "Phosphopyruvate carboxylase from baker's yeast. I. Isolation, purification, and characterization". J. Biol. Chem. 238: 1196–1207. PMID 14018315.
^ Cannata, J.J.B.; Stoppani, A.O.M. (1963). "Phosphopyruvate carboxylase from baker's yeast. II. Properties of enzyme". J. Biol. Chem. 238: 1208–1212. PMID 14018316.

External links

Phosphoenolpyruvate+carboxykinase+(ATP) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Cannata, J.J.B. (1970). "Phosphoenolpyruvate carboxykinase from bakers' yeast. Isolation of the enzyme and study of its physical properties". J. Biol. Chem. 245: 792–798. PMID 5416663.

[2] Cannata, J.J.B.; Stoppani, A.O.M. (1963). "Phosphopyruvate carboxylase from baker's yeast. I. Isolation, purification, and characterization". J. Biol. Chem. 238: 1196–1207. PMID 14018315.

[3] Cannata, J.J.B.; Stoppani, A.O.M. (1963). "Phosphopyruvate carboxylase from baker's yeast. II. Properties of enzyme". J. Biol. Chem. 238: 1208–1212. PMID 14018316.

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v t e Carbon–carbon lyases (EC 4.1)
4.1.1: Carboxy-lyases	Acetoacetate decarboxylase Adenosylmethionine decarboxylase Arginine decarboxylase Aromatic L-amino acid decarboxylase Glutamate decarboxylase Histidine decarboxylase Lysine decarboxylase Malonyl-CoA decarboxylase Ornithine decarboxylase Oxaloacetate decarboxylase Phosphoenolpyruvate carboxykinase Phosphoenolpyruvate carboxylase Phosphoribosylaminoimidazole carboxylase Pyrophosphomevalonate decarboxylase Pyruvate decarboxylase RuBisCO Uridine monophosphate synthetase/Orotidine 5'-phosphate decarboxylase Uroporphyrinogen III decarboxylase
4.1.2: Aldehyde-lyases	Fructose-bisphosphate aldolase Aldolase A Aldolase B Aldolase C 2-hydroxyphytanoyl-CoA lyase Threonine aldolase
4.1.3: Oxo-acid-lyases	Isocitrate lyase 3-hydroxy-3-methylglutaryl-CoA lyase
4.1.99: Other	Tryptophanase Photolyase CPD lyase Spore photoproduct lyase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

See also

References

External links