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.
|Number of pages||9|
|Journal||Journal of Bacteriology|
|State||Published - 1975|
ASJC Scopus subject areas
- Molecular Biology