Control by Phosphorylation, Part B (Specific Enzymes), 3rd by Paul D. Boyer

By Paul D. Boyer

Content material: v. 17. normal gains -- particular enzymes (I). -- v. 18. particular enzymes (II) -- organic procedures

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

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B. YEAST There is a growing amount of evidence that implicates phosphorylation-dephosphorylation in the regulation of fructose- 1,6-bisphosphatase from Saccharomyces cerevisiae. This enzyme has been purified to homogeneity from Baker's yeast and consists of a dimer with a subunit molecular weight of 57,000 (190). The specific activity of the yeast enzyme is 46 units/mg which is similar to that of the rat liver enzyme, and it is inhibited by AMP, Fru-2,6-P,, and its substrate Fru-1,6-P,. The inhibition by AMP is noncompetitive and does not exhibit cooperative behavior (176).

6-Phosphofructo-1-Kinase: Possible Role of Phosphorylation in the Control of Enzyme Activity A. LIVER 6-Phosphofructo- 1-kinase has been purified from livers of a number of species (86-98). The rat liver enzyme consists of four apparently identical subunits with a molecular weight of 82,000 (90-92). Like that of heart (99) and muscle (ZOO), it tends to form aggregates with molecular weights of the order of several million (90-92, 101). This aggregation is an equilibrium process influenced by enzyme concentration, the presence of allosteric effectors, the oxidation-reduction state of sulfhydryl groups, and temperature (8, 9, 91, 92, 102).

Inorganic phosphate and a-glycerol-P are competitive inhibitors at low Fru-2,6-P2 concentrations (26), but both effectors are activators at higher Fru-2,6-P2 concentrations where substrate inhibition is seen (5, 6, 14, 25, 26, 49). 4. It has been reported that GTP, and to a lesser extent ATP, activate partially purified fructose-2,6-bisphosphatase(47, 49), but this observation is not confirmed with a homogeneous preparation of the enzyme (M. R. ElMaghrabi and S. J. Pilkis, unpublished results).

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