From 74fdd4dbe5000e0b2f4ca0d9628450e373480f4a Mon Sep 17 00:00:00 2001 From: Suzanne Freeling Date: Mon, 4 Aug 2025 23:55:08 +0000 Subject: [PATCH] Add Multiple Glycogen-binding Sites in Eukaryotic Glycogen Synthase are Required for Prime Catalytic Efficiency toward Glycogen --- ... Required for Prime Catalytic Efficiency toward Glycogen.-.md | 1 + 1 file changed, 1 insertion(+) create mode 100644 Multiple Glycogen-binding Sites in Eukaryotic Glycogen Synthase are Required for Prime Catalytic Efficiency toward Glycogen.-.md 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..74b1b4d --- /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 price-limiting enzyme in the biosynthesis of glycogen and has a vital role in glucose homeostasis. The three-dimensional constructions 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 area, site-2 and site-three are current on the C-terminal area, and site-4 is located in an interdomain cleft adjoining to the lively site. Mutation of those surface sites decreased glycogen binding and catalytic effectivity towards glycogen. 40- and 70-fold, respectively. 1-gsy2) remodeled with the positioning-1, site-2, mixed site-1/site-2, or site-4 mutant form of Gsy2p was decreased by up to 40-fold. In contrast to the glycogen results, [Glyco Forte supplement](http://wooriwebs.com/bbs/board.php?bo_table=faq) the power to make the most of maltooctaose as an in vitro substrate was unaffected in the positioning-2 mutant, moderately affected in the positioning-1 mutant, and nearly utterly abolished in the site-four mutant. These data present that the ability to make the most of maltooctaose as a substrate might be unbiased of the flexibility to utilize glycogen. Our information support the speculation that site-1 and site-2 present a 'toehold mechanism,' holding glycogen synthase tightly associated with the glycogen particle, whereas site-four is extra intently associated with positioning of the nonreducing end throughout catalysis.

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