Phosphoenolpyruvate carboxykinase (ATP)
Phosphoenolpyruvate carboxykinase (ATP) is an enzyme that helps make phosphoenolpyruvate (PEP) from oxaloacetate, using ATP in the process. The reaction is oxaloacetate plus ATP → phosphoenolpyruvate plus ADP plus CO2. This decarboxylation–phosphorylation step is important for gluconeogenesis, the production of glucose from non-carbohydrate sources. The enzyme is found in bacteria such as Escherichia coli and has several synonyms, including phosphopyruvate carboxylase (ATP) and PEP carboxykinase (ATP). Its systematic name is ATP:oxaloacetate carboxy-lyase (transphosphorylating; phosphoenolpyruvate-forming). It belongs to the carboxy-lyase family (EC 4.1.1.49) and typically functions as a monomer.
This page was last edited on 2 February 2026, at 08:40 (CET).