commit 7947a97fc953751e49dc34641e5d20d31a8bcfe8 Author: oplrenate61327 Date: Mon Sep 22 08:51:02 2025 +0000 Update 'Multiple Glycogen-binding Sites in Eukaryotic Glycogen Synthase are Required for Prime Catalytic Efficiency toward Glycogen' diff --git a/Multiple-Glycogen-binding-Sites-in-Eukaryotic-Glycogen-Synthase-are-Required-for-Prime-Catalytic-Efficiency-toward-Glycogen.md b/Multiple-Glycogen-binding-Sites-in-Eukaryotic-Glycogen-Synthase-are-Required-for-Prime-Catalytic-Efficiency-toward-Glycogen.md new file mode 100644 index 0000000..3f7fba3 --- /dev/null +++ b/Multiple-Glycogen-binding-Sites-in-Eukaryotic-Glycogen-Synthase-are-Required-for-Prime-Catalytic-Efficiency-toward-Glycogen.md @@ -0,0 +1 @@ +
Glycogen synthase is a fee-limiting enzyme within the biosynthesis of glycogen and has a vital role in glucose homeostasis. The three-dimensional constructions of yeast glycogen synthase (Gsy2p) complexed with maltooctaose identified 4 conserved maltodextrin-binding websites distributed throughout the floor of the enzyme. Site-1 is positioned on the N-terminal area, site-2 and site-three are present on the C-terminal area, and site-four is positioned in an interdomain cleft adjacent to the lively site. Mutation of those surface websites decreased glycogen binding and catalytic effectivity toward glycogen. 40- and 70-fold, respectively. 1-gsy2) reworked with the positioning-1, site-2, [Healthy Flow Blood](https://botdb.win/wiki/User:MalorieBou) mixed site-1/site-2, or site-4 mutant type of Gsy2p was decreased by up to 40-fold. In contrast to the glycogen outcomes, the flexibility to make the most of maltooctaose as an in vitro substrate was unaffected in the location-2 mutant, moderately affected in the site-1 mutant, and almost fully abolished in the site-four mutant. These data present that the power to utilize maltooctaose as a substrate might be unbiased of the ability to make the most of glycogen. Our data assist the hypothesis that site-1 and site-2 present a 'toehold mechanism,' protecting glycogen synthase tightly related to the glycogen particle, whereas site-four is more carefully related to positioning of the nonreducing finish during catalysis.

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