Phosphoenolpyruvate carboxykinase (ATP)

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 ADP + phosphoenolpyruvate + CO2
Phosphoenolpyruvate carboxykinase (ATP)
Phosphoenolpyruvate carboxykinase (ATP) monomer, E.Coli
Identifiers
EC no.4.1.1.49
CAS no.9073-94-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

See also

References

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