Phosphoenolpyruvate carboxykinase (ATP)

Last updated
Phosphoenolpyruvate carboxykinase (ATP)
6w2m.jpg
Phosphoenolpyruvate carboxykinase (ATP) monomer, E.Coli
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
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

Contents

ATP + oxaloacetate ADP + phosphoenolpyruvate + CO2

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. doi: 10.1016/S0021-9258(18)63334-4 . 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 (4): 1196–207. doi: 10.1016/S0021-9258(18)81164-4 . 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 (4): 1208–12. doi: 10.1016/S0021-9258(18)81165-6 . PMID   14018316.