Enrique Rozengurt

TL;DR: It is concluded that small variations in the intracellular pH could be important in the regulation of pyruvate kinase activity by metabolites in vivo.

TL;DR: It is concluded that this amino acid is an allosteric inhibitor of skeletal muscle pyruvate kinase, independent of pH and it is not reversed by the amino acids.

TL;DR: The physiological role of the Cu++-fructose 1,6-diphosphate interrelation in the balance between glycolysis and gluconeogenesis is discussed and the activation of the enzyme with NH4+ has been found to be more efficient than with K+.

TL;DR: A kinetic study of the early changes in uridine and phosphate-transport rates and 3':5'-cyclic AMP levels induced by the addition of serum to quiescent 3T3 cells revealed that the increase in phosphate uptake and the decrease in the intracellular concentration of 3'5'cyclic amp immediately follow the addition by serum and was clearly preceded by other changes as mentioned in this paper.

TL;DR: At least two forms of pyruvate kinase Type M can be distinguished in rat tissues on the basis of kinetic properties, and the inhibition by phenylalanine and alanine of the liver pyruviate kinases Type M is of the mixed type with respect to phosphoenol pyruVate and is only slightly dependent on pH.