Glycogen synthase is a fee-limiting enzyme in the biosynthesis of glycogen and has an important position in glucose homeostasis. The three-dimensional constructions of yeast glycogen synthase (Gsy2p) complexed with maltooctaose identified four conserved maltodextrin-binding sites distributed throughout the surface of the enzyme. Site-1 is positioned on the N-terminal domain, site-2 and site-3 are present on the C-terminal domain, and site-4 is situated in an interdomain cleft adjacent to the lively site. Mutation of these floor websites decreased glycogen binding and catalytic effectivity toward glycogen. 40- and 70-fold, respectively. 1-gsy2) remodeled with the site-1, site-2, mixed site-1/site-2, or site-four mutant form of Gsy2p was decreased by up to 40-fold. In distinction to the glycogen results, the ability to utilize maltooctaose as an in vitro substrate was unaffected in the site-2 mutant, reasonably affected in the positioning-1 mutant, and virtually utterly abolished in the positioning-four mutant. These data show that the ability to utilize maltooctaose as a substrate may be independent of the ability to make the most of glycogen. Our data help the hypothesis that site-1 and site-2 provide a 'toehold mechanism,' preserving glycogen synthase tightly associated with the glycogen particle, whereas site-four is more carefully associated with positioning of the nonreducing end throughout catalysis.
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Multiple Glycogen binding Sites in Eukaryotic Glycogen Synthase are Required for Prime Catalytic Efficiency toward Glycogen
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