EC Number   |
General Information |
Reference |
|---|
    2.4.1.11 | evolution |
glycogen synthase homologues in bacteria and archaea lack regulation, while the eukaryotic enzymes are inhibited by protein kinase mediated phosphorylation and activated by protein phosphatases and D-glucose 6-phosphate binding |
720899 |
| 2.4.1.11 | metabolism |
glycogen synthase intrinsic activity is strongly dependent on glycogen levels. Regulation involves associated dephosphorylation at sites 2 + 2a, 3a, and 3a + 3b. There exist several glycogen metabolism regulatory mechanisms based on glycogen synthase intracellular compartmentalization. After exhausting exercise, epinephrine-induced protein kinase A activation leads to glycogen synthase site 1b phosphorylation targeting the enzyme to intramyofibrillar glycogen particles, which are preferentially used during muscle contraction. When phosphorylated at sites 2 + 2a, glycogen synthase is preferentially associated with subsarcolemmal and intermyofibrillar glycogen particles. After overnight low muscle glycogen level and/or in response to exhausting exercise-induced glycogenolysis, glycogen synthase is associated with spherical structures at the I-band of sarcomeres |
704484 |
| 2.4.1.11 | metabolism |
in healthy subjects, adrenaline infusion increases blood glucose concentration by approximately 50%, but a hyperinsulinemic clamp normalizes blood glucose within 30 minutes. Insulin increases glycogen synthase fractional activity and decreases glycogen synthase Ser641 and Ser645,649,653,657 phosphorylation. In the presence of adrenaline, insulin does neither activate glycogen synthase nor dephosphorylate glycogen synthase Ser641. glycogen synthase Ser7 phosphorylation is not influenced by adrenaline. Adrenaline increases plasma lactate concentration, and muscle glycogen content is reduced in skeletal muscle the day after adrenaline infusion |
705511 |
| 2.4.1.11 | metabolism |
synthesis and degradation of trehalose and glycogen in insects involving glycogen synthase, overview |
718703 |
| 2.4.1.11 | more |
in the basal activity state and D-glucose 6-phosphate activated state, the enzyme is assembled into an unusual tetramer by an insertion unique to the eukaryotic enzymes, and this subunit interface is rearranged by the binding of D-glucose 6-phosphate, which frees the active site cleft and facilitates catalysis. Structure function in enzyme regulation, overview |
720899 |
| 2.4.1.11 | physiological function |
a mutant strain defective in adenylyl cyclase activity accumulates, during vegetative growth, glycogen levels much higher than the wild type strain. The gsn transcript is not increased in this strain but the GSN protein is less phosphorylated in vitro, and therefore more active |
703827 |
| 2.4.1.11 | physiological function |
glycogen synthase catalyzes the key step of glycogen synthesis and plays an important role in glycogen metabolism in liver and muscle, phosphorylation sites regulate the activity of the enzyme |
-, 720446 |
| 2.4.1.11 | physiological function |
glycogen synthase catalyzes the key step of glycogen synthesis and plays an important role in glycogen metabolism in liver and muscle, phosphorylation sites regulate the activity of the enzyme. Transcriptional regulation of GYS1 during myogenic differentiation in porcine satellite cells, overview. Effect of insulin is primarily mediated via posttranscriptional control the porcine glycogen synthase. Insulin promotes dephosphorylation of glycogen synthase in differentiated porcine satellite cells |
-, 720446 |
| 2.4.1.11 | physiological function |
the enzyme is important for maintaining normal physiological functions such as growth and reproduction |
756508 |
