Biology:Phosphoenolpyruvate carboxykinase (ATP)

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Phosphoenolpyruvate carboxykinase (ATP)
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Phosphoenolpyruvate carboxykinase (ATP) monomer, E.Coli
Identifiers
EC number4.1.1.49
CAS number9073-94-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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 [math]\displaystyle{ \rightleftharpoons }[/math] ADP + phosphoenolpyruvate + CO2

See also

References

  1. "Phosphoenolpyruvate carboxykinase from bakers' yeast. Isolation of the enzyme and study of its physical properties". The Journal of Biological Chemistry 245 (4): 792–8. February 1970. PMID 5416663. 
  2. "Phosphopyruvate carboxylase from baker's yeast. I. Isolation, purification, and characterization". The Journal of Biological Chemistry 238: 1196–207. April 1963. PMID 14018315. 
  3. "Phosphopyruvate carboxylase from baker's yeast. II. Properties of enzyme". The Journal of Biological Chemistry 238: 1208–12. April 1963. PMID 14018316. 

External links