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Multiple Glycogen-binding Sites In Eukaryotic Glycogen Synthase Are Required For Prime Catalytic Efficiency Towards Glycogen

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Revision as of 17:33, 4 August 2025 by Lynell3340 (talk | contribs) (Created page with "<br>Glycogen synthase is a rate-limiting enzyme in the biosynthesis of glycogen and has an essential function in glucose homeostasis. The three-dimensional buildings 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 area, site-2 and site-3 are present on the C-terminal domain, and site-4 is positioned in an interdom...")
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Glycogen synthase is a rate-limiting enzyme in the biosynthesis of glycogen and has an essential function in glucose homeostasis. The three-dimensional buildings 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 area, site-2 and site-3 are present on the C-terminal domain, and site-4 is positioned in an interdomain cleft adjoining to the lively site. Mutation of these floor websites decreased glycogen binding and catalytic efficiency toward glycogen. 40- and 70-fold, respectively. 1-gsy2) transformed with the site-1, site-2, mixed site-1/site-2, or site-four mutant type of Gsy2p was decreased by as much as 40-fold. In distinction to the glycogen results, the power to make the most of maltooctaose as an in vitro substrate was unaffected in the location-2 mutant, reasonably affected in the location-1 mutant, and nearly fully abolished in the positioning-4 mutant. These data present that the flexibility to utilize maltooctaose as a substrate will be impartial of the power to utilize glycogen. Our data help the hypothesis that site-1 and site-2 provide a 'toehold mechanism,' conserving glycogen synthase tightly associated with the glycogen particle, whereas site-4 is extra intently associated with positioning of the nonreducing finish during catalysis.

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