Kinetic properties of glycogen synthase from skeletal muscle after phosphorylation by glycogen synthase kinase 4

Biochemical and Biophysical Research Communications
D F BrownE M Reimann

Abstract

Glycogen synthase I (EC 2.4.1.11) from rat and from rabbit skeletal muscle was phosphorylated in vitro by glycogen synthase kinase 4 (EC 2.7.1.37) to the extent of 0.8 phosphates/subunit. For both phosphorylated enzymes, the activity ratio (activity without glucose 6-P divided by activity with 8 mM glucose 6-P) was 0.8 when determined with low concentrations of glycogen synthase and/or short incubation times. However, the activity ratio was 0.5 with high enzyme concentrations and longer incubation times. It was found that the lower activity ratios result largely from UDP inhibition of activity measured in the absence of glucose 6-P. Inhibition by UDP was much less pronounced for glycogen synthase I, indicating that a major consequence of phosphorylation by glycogen synthase kinase 4 is an increased sensitivity to UDP inhibition.

References

Jan 1, 1989·The International Journal of Biochemistry·I Farkas, P Gergely
Aug 1, 1993·The International Journal of Biochemistry·M al-Habori
Jun 27, 2002·Biochemical and Biophysical Research Communications·Ronit IlouzHagit Eldar-Finkelman

Citations

May 1, 1969·Biochemistry·R Piras, R J Staneloni

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