The reduced nicotinamide adenine dinucleotide-activated phosphoenolpyruvate carboxylase from Pseudomonas MA. Correlation of allosteric properties with changes in the sedimentation behavior.

@article{Millay1976TheRN,
  title={The reduced nicotinamide adenine dinucleotide-activated phosphoenolpyruvate carboxylase from Pseudomonas MA. Correlation of allosteric properties with changes in the sedimentation behavior.},
  author={R H Millay and Louis B. Hersh},
  journal={The Journal of biological chemistry},
  year={1976},
  volume={251 9},
  pages={2754-60}
}
Phosphoenolpyruvate carboxylase from Pseudomonas MA, grown on methylamine as a sole carbon source, has been studied with respect to some of its regulatory properties. The enzyme shows both negative and positive cooperativity with respect to the substrate phosphoenolpyruvate (Hill coefficients of 0.5 and 1.75). The enzyme requires a divalent cation for… CONTINUE READING