Kinetic studies on muscle glycogen synthase.
نویسندگان
چکیده
منابع مشابه
Structural Studies on Rabbit Muscle Glycogen Synthase
Limited tryptic digestion of either synthase I or D forms resulted in the appearance of a new glucose 6-phosphate-dependent form which was composed of 75,000 molecular weight subunits. Early in tryptic digestion, an intermediate 78,000 subunit was also observed with both forms of the enzyme. The NH,terminal dipeptide sequence of the 75,000 subunit of both forms was the same as that of the origi...
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Glycogen synthase (GS), a key enzyme in glycogen synthesis, is activated by the allosteric stimulator glucose-6-phosphate (G6P) and by dephosphorylation through inactivation of GS kinase-3 with insulin. The relative importance of these two regulatory mechanisms in controlling GS is not established, mainly due to the complex interplay between multiple phosphorylation sites and allosteric effecto...
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catalyzed by glycogen synthase D (UDP-glucose:glycogen o-4-glucosyltransferase, EC 2.4.1.11) was studied, using r4C isotope transfer rates. The reaction rates were determined at varying concentrations of either substrate at constant amounts of the other substrate. The inhibition patterns of UDP as well as the activation patterns of the activator glucose 6-phosphate toward either substrate were ...
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Isotope-exchange rates at chemical equilibrium were determined for the glycogen-a-D-glucopyranose l-phosphatePi system in the presence of phosphorylase a. Exchange of 32P from a-n-glucopyranose l-phosphate (glucose-l-P) into Pi and exchange of 14C from glucose-l-P into glycogen were followed simultaneously by the use of glucose-l-P containing both isotopes. Concentrations of glucose-l-P and Pi ...
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Glycogen is an important component of whole-body glucose metabolism. MGSKO mice lack skeletal muscle glycogen due to disruption of the GYS1 gene, which encodes muscle glycogen synthase. MGSKO mice were 5-10% smaller than wild-type littermates with less body fat. They have more oxidative muscle fibers and, based on the activation state of AMP-activated protein kinase, more capacity to oxidize fa...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1975
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)41539-1