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Glycogen synthase is a charge-limiting enzyme within the biosynthesis of glycogen and has a necessary function in glucose homeostasis.
The three-dimensional buildings of yeast glycogen synthase (Gsy2p) complexed with maltooctaose recognized four conserved maltodextrin-binding sites distributed throughout the floor 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 positioned in an interdomain cleft adjacent to the active site.
Mutation of these surface sites decreased glycogen binding and catalytic effectivity towards glycogen. 40- and 70-fold respectively. 1-gsy2) transformed with the site-1 site-2 combined site-1/site-2 or site-4 mutant type of Gsy2p was decreased by as much as 40-fold.
In contrast to the glycogen results the flexibility to make the most of maltooctaose as an in vitro substrate was unaffected in the site-2 mutant moderately affected in the location-1 mutant and almost fully abolished in the positioning
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