By Paul D. Boyer

Content material: v. 17. basic good points -- particular enzymes (I). -- v. 18. particular enzymes (II) -- organic procedures

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Extra resources for Control by Phosphorylation, Part B (Specific Enzymes), 3rd Edition

Sample text

The decrease in 6-phosphofructo- I-kinase activity and the activation of fructose-1,6-bisphoshatase cause a reduction in the level of Fru-1,6-P, which is a potent allosteric activator of pyruvate kinase. Inhibition of this enzyme occurs not only by a decrease in Fru-l,6-P2 levels but also by CAMP-dependent phosphorylation of a specific seryl residue (see L. Engstrom et al. Chapter 2, this volume). Inhibition of pyruvate kinase plays a major role in the stimulation of gluconeogenesis and the inhibition of glycolysis by hormones that elevate cyclic AMP levels.

A summary of these effects is shown in Fig. 5A. Hormones that stimulate cyclic AMP production cause phosphorylation of the bifunctional enzyme. This results in a decrease in Fru-2,6-P2 levels due to inhibition of the kinase reaction and activation of the bisphosphatase reaction. The decrease in Fru-2,6-P2 in turn leads to decreased allosteric activation of 6phosphofructo-1-kinase and decreased inhibition of fructose- 1,6-bisphosphatase. These changes in enzyme activity may be further amplified by concomitant phosphorylation of 6-phosphofructo- 1-kinase and fructose- 1,6-bisphosphatase.

Such modification may alter an enzyme’s affinity for substrate or cofactor or it may affect maximal velocity, or both. In the case of fructose-2,6-bisphosphatase,a phosphoenzyme intermediate and the kinetic competence of this phosphoenzyme have been demonstrated (26). The rate of breakdown of the phosphoenzyme intermediate was shown to be the rate-limiting step in phosphoenzyme turnover (26). These discoveries have made it possible to identify what step or steps in the reaction pathway are influenced by phosphorylation.

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