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Glycogen synthase (GS) catalyzes the formation of a(174) glycosidic bonds in glycogen by catalyzing the transfer of UDP-glucose to a glycogen particle where UDP is a byproduct. It is regulated by allosteric modulators and phosphorylation coupled to hormones. Assume GS is a K-system enzyme. Given this information, answer the following questions, a) Do you expect the binding of the substrate UDP-glucose to favor the Ror T state of the enzyme or neither? b) Draw a plot of the rate of GS versus UDP-glucose. Label the axes, define the half-maximal substrate binding (Ko.s) point, and mark the curve with the label UDP-glucose. c) GSK-3 from Question 3 above phosphorylates GS, thus inhibiting the enzyme. When GS is phosphorylated, do you expect the Ror T state of the enzyme or neither to be favored? d) On the same plot that you drew for part (b) now add a second curve indicating the effect of phosphorylation. Define the half-maximal substrate binding (Ko.s) point and mark the curve with the label GS-P