Phosphoenolpyruvate carboxylase (also known as PEP carboxylase, PEPCase, or PEPC; EC4.1.1.31, PDB ID: 3ZGE) is an enzyme in the family of carboxy-lyases found in plants and some bacteria that catalyzes the addition of bicarbonate (HCO3−) to phosphoenolpyruvate (PEP) to form the four-carbon compound oxaloacetate and inorganic phosphate:[1]
PEP + HCO3− → oxaloacetate + Pi
This reaction is used for carbon fixation in CAM (crassulacean acid metabolism) and C4 organisms, as well as to regulate flux through the citric acid cycle (also known as Krebs or TCA cycle) in bacteria and plants. The enzyme structure and its two step catalytic, irreversible mechanism have been well studied. PEP carboxylase is highly regulated, both by phosphorylation and allostery.
^Kai Y, Matsumura H, Izui K (June 2003). "Phosphoenolpyruvate carboxylase: three-dimensional structure and molecular mechanisms". Archives of Biochemistry and Biophysics. 414 (2): 170–9. doi:10.1016/S0003-9861(03)00170-X. PMID12781768.
