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Varda Barash , Hannah Schramm and Alisa Gutman Adipose Tissue Glycogen Synthetase : I

In vitro activation of adipose tissue glycogen synthetase caused a change in kinetic properties of the enzyme. The nonactivated enzyme had a K, for UDP-glucose of 2 m when measured without glucose-6-P. The K, decreased to 0.7 mM in the presence of 2 mM glucose-6-P. The K, for UDP-glucose of the activated enzyme was 0.8 mM. Glucose-6-P affected both the K, for UDP-glucose and the v m&x of the nonactivated enzyme, but had no effect after activation. In the absence of glucose-6-P the nonactivated enzyme was inhibited by F-, SOd2-, Pi, and EDTA, whereas it was activated by Ca2+ and Mg2+. These effects were attenuated in the presence of glucose-6-P or following activation of the enzyme. ATP inhibited the activity of both forms of the enzyme. In the presence of glucose-6-P or after activation the inhibition was competitive with UDP-glucose. Enzyme activity measured with physiological concentrations of UDP-glucose, glucose-6-P, ATP, and Pi increased upon activation from 1 to 10 nmoles per min X mg of protein.