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Glycogen synthase is a fee-limiting enzyme in the biosynthesis of glycogen and has an important function in glucose homeostasis. The three-dimensional structures of yeast glycogen synthase (Gsy2p) complexed with maltooctaose recognized four conserved maltodextrin-binding websites distributed throughout the surface of the enzyme. Site-1 is positioned on the N-terminal domain, site-2 and [site-three](https://www.blogher.com/?s=site-three) are present on the C-terminal area, and site-4 is positioned in an interdomain cleft adjoining to the active site. Mutation of these surface sites decreased glycogen binding and catalytic efficiency toward glycogen. 40- and 70-fold, respectively. 1-gsy2) remodeled with the positioning-1, site-2, mixed site-1/site-2, or site-four mutant type of Gsy2p was decreased by up to 40-fold. In distinction to the glycogen outcomes, the ability to utilize maltooctaose as an in vitro substrate was unaffected in the location-2 mutant, reasonably affected in the location-1 mutant, and almost completely abolished in the positioning-4 mutant. These data show that the power to utilize maltooctaose as a substrate could be unbiased of the power to utilize 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 extra intently related to positioning of the nonreducing finish during catalysis.
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