PMID: 6411505Jan 1, 1983Paper

Some regulatory properties of a glucose-6-phosphate-dependent form of glycogen synthase purified from rabbit renal medulla

The International Journal of Biochemistry
K K Schlender, C M Doster

Abstract

Glycogen synthase D was purified greater than 1000-fold from rabbit renal medulla. The enzyme was almost completely dependent upon glucose-6-P for activity (activity ratio approximately equal to 0.01). The A0.5 for glucose-6-P activation was 420 microM when UDPGlc was present at 4.4 mM and the A0.5 was 2.23 mM when UDPGlc was present at physiological concentration (100 microM). The S0.5 for UDPGlc of glycogen synthase D was dependent on glucose-6-P. The S0.5 ranged from 250 to 70 microM when glucose-6-P was varied from 0.2 to 10 mM. The Vmax increased 3-fold. Inhibition of glycogen synthase D by ATP was competitive with respect to UDPGlc. The Ki for ATP inhibition was 340 microM. At physiological concentration of UDPGlc, the enzyme was inhibited 50% by 500 microM ATP. ATP inhibition was not reversed by glucose-6-P. These results suggest that renal medullary glycogen synthase D would be inactive at normal cellular concentrations of the substrate UDPGlc, the activator glucose-6-P, and the inhibitor ATP.

References

May 3, 1977·Molecular and Cellular Biochemistry·R J Roach, J Larner
Feb 28, 1973·Biochimica Et Biophysica Acta·K K Schlender
May 1, 1969·Biochemistry·R Piras, R Staneloni
Jan 1, 1981·Current Topics in Cellular Regulation·P J Roach
Jan 1, 1982·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·K K Schlender, C M Doster
Jul 1, 1962·The American Journal of Physiology·J B LEEG F CAHILL

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