Reduced nicotinamide adenine dinucleotide activated phosphoenolpyruvate carboxylase in Pseudomonas MA: potential regulation between carbon assimilation and energy production

Comparison of enzyme activities in crude extracts of methylamine grown Pseudomonas MA (ATCC 23319) to those in succinate grown cells indicates the involvement of an acetyl coenzyme A independent phosphoenolpyruvate carboxylase in one carbon metabolism. The purified phosphoenolpyruvate carboxylase is activated specifically by reduced nicotinamide adenine dinucleotide (K(A)=0.2 mM). The regulatory properties of this enzyme suggests that phosphoenolpyruvate serves as a focal point for both carbon assimilation and energy metabolism.