Abstract

The human placental glucose-6-P-dependent form of glycogen synthase, in the absence of glucose-6-P, can be activated by MnSO4. Separately, Mn2+ and SO4(2-) have no significant effect. In the presence of glucose-6-P, Mn2+ activates the enzyme, but SO4(2-) inhibits; MnSO4 synergetically increases the enzyme activity. Mn2+ reduces the Ka for glucose-6-P to one-tenth of the control value; SO4(2-) increases the Ka 5-fold; however, MnSO4 has no effect on Ka. MnSO4, like glucose-6-P, increases the Vmax of the enzyme in the presence of its substrate, UDP-glucose; it slightly increases the Km for UDP-glucose. In the presence of glucose-6-P, Mn2+ increases and SO4(2-) decreases the Vmax of the enzyme, but neither has an effect on the Km for UDP-glucose. At physiological concentrations of UDP-glucose and glucose-6-P, either Mn2+ or MnSO4 at concentrations less than 1 mM increases the enzyme activity as much as 8 mM glucose-6-P does. At physiological concentrations of UDP-glucose and glucose-6-P, Mn2+ or MnSO4 reverses the inhibition of the enzyme by ATP.

Highlights

  • From the Section on Developmental Enzymology, Laboratory ofBiomedical of Child Health and Human Development, National Institutes of Health, Sciences, National Bethesda, Maryland

  • In the presence of glucose-6-P, Mn’+ increases and SO,‘- decreases the V, of the enzyme, but neither has an effect on the K, for UDP-glucose

  • In the presence of glucose-6-P, the enzyme activity is increased by the addition of MnSO, (Fig. lA)

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Summary

Introduction

From the Section on Developmental Enzymology, Laboratory ofBiomedical of Child Health and Human Development, National Institutes of Health, Sciences, National Bethesda, Maryland. The human placental glucose-6-P-dependent form of glycogen synthase, in the absence of glucose-&P, can be activated by MnSO,. MnSO,, like glucose-&P, increases the Y,;,, of the enzyme in the presence of its substrate, the K,,, for UDP-glucose.

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