Multiple Glycogen-binding Sites in Eukaryotic Glycogen Synthase are Required for High Catalytic Efficiency toward Glycogen

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Glycogen synthase is a charge-limiting enzyme in the biosynthesis of glycogen and has a necessary position in glucose homeostasis. The three-dimensional constructions of yeast glycogen synthase (Gsy2p) complexed with maltooctaose identified 4 conserved maltodextrin-binding websites distributed across the surface of the enzyme. Site-1 is positioned on the N-terminal area, site-2 and site-three are present on the C-terminal domain, and site-4 is located in an interdomain cleft adjacent to the lively site. Mutation of these surface websites decreased glycogen binding and catalytic efficiency toward glycogen. 40- and 70-fold, respectively. 1-gsy2) transformed with the site-1, site-2, combined site-1/site-2, or site-4 mutant form of Gsy2p was decreased by as much as 40-fold. In contrast to the glycogen results, the power to make the most of maltooctaose as an in vitro substrate was unaffected in the positioning-2 mutant, moderately affected in the location-1 mutant, and nearly fully abolished in the positioning-four mutant. These data show that the flexibility to utilize maltooctaose as a substrate can be unbiased of the flexibility to utilize glycogen. Our data assist the speculation that site-1 and site-2 provide a 'toehold mechanism,' conserving glycogen synthase tightly related to the glycogen particle, whereas site-four is more intently associated with positioning of the nonreducing finish during catalysis.<br>
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