Enzymes concerned with beta-carboxylation in marine phytoplankter. Purification and properties of phosphoenolpyruvate carboxykinase.

The enzyme resonsible for β-carboxylation, with eventual incorporation of CO₂ into amino acids, has been studied in three diatoms and a dinoflagellate. The enzyme from Phaeodactylum tricornutum has been purified to homogeneity and has an absolute requirement for ADP and Mn²⁺. This enzyme is best described as phosphoenolpyruvate carboxykinase (carboxylating), but it differs considerably from enzymes with the same name, isolated from mammalian and bacterial sources, in that the reaction of phosphoenolpyruvate with bicarbonate lies strongly in the direction of formation of oxaloacetate and ATP. This conservation of the high-energy phosphate groups of phosphoenolpyruvate in ATP would be advantageous to diatoms living at low levels of light intensity in seawater.