2.4.1.11: glycogen(starch) synthase
This is an abbreviated version!
For detailed information about glycogen(starch) synthase, go to the full flat file.
Word Map on EC 2.4.1.11
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2.4.1.11
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kinase-3
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phosphorylase
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insulin-stimulated
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hepatocytes
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alzheimer
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3-kinase
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clamp
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mellitus
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tau
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hexokinase
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neuroprotective
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hyperglycemia
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6-phosphate
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lithium
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phosphatidylinositol
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glucose-6-phosphatase
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glycogenolysis
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amylose
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disposal
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hyperphosphorylation
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insulin-resistant
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insulin-mediated
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hyperinsulinemic
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irs-1
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waxy
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glycogenesis
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amylopectin
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licl
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adp-glucose
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niddm
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glucokinase
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soleus
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glucose-6-p
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non-insulin-dependent
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insulin-induced
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amp-dependent
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vastus
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euglycemic
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phosphatase-1
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gsk-3beta
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agpase
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debranching
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p-gsk-3
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medicine
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substrate-1
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2,6-bisphosphate
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euglycemic-hyperinsulinemic
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nonoxidative
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phosvitin
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kinase-3beta
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nutrition
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lafora
- 2.4.1.11
- kinase-3
- phosphorylase
-
insulin-stimulated
- hepatocytes
- alzheimer
- 3-kinase
-
clamp
- mellitus
- tau
- hexokinase
-
neuroprotective
- hyperglycemia
- 6-phosphate
- lithium
- phosphatidylinositol
- glucose-6-phosphatase
-
glycogenolysis
- amylose
-
disposal
-
hyperphosphorylation
-
insulin-resistant
-
insulin-mediated
-
hyperinsulinemic
- irs-1
-
waxy
-
glycogenesis
- amylopectin
- licl
- adp-glucose
- niddm
- glucokinase
- soleus
-
glucose-6-p
-
non-insulin-dependent
-
insulin-induced
-
amp-dependent
-
vastus
-
euglycemic
- phosphatase-1
- gsk-3beta
- agpase
-
debranching
-
p-gsk-3
- medicine
- substrate-1
-
2,6-bisphosphate
-
euglycemic-hyperinsulinemic
-
nonoxidative
- phosvitin
- kinase-3beta
- nutrition
- lafora
Reaction
Synonyms
Cg-GYS, GBSS, GBSSI, glucosyltransferase, uridine diphosphoglucose-glycogen, glycogen synthase, glycogen synthase 2, glycogen synthase-2, glycogen synthetase (starch), granule bound starch synthase, granule-bound starch synthase, GS-I, GSN, GSY2p, Gys-2, GYS1, GYS2, Gys2p, starch synthase I, starch/glycogen synthase, TVAG_258220, UDP-glucose-glycogen glucosyltransferase, UDP-glycogen synthase, UDPG-glycogen synthetase, UDPG-glycogen transglucosylase, uridine diphosphoglucose-glycogen glucosyltransferase
ECTree
2.4.1.11 glycogen(starch) synthaseAdvanced search results
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General Information on EC 2.4.1.11 - glycogen(starch) synthase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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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
metabolism
physiological function
additional information
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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
metabolism
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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
metabolism
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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
metabolism
synthesis and degradation of trehalose and glycogen in insects involving glycogen synthase, overview
physiological function
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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
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
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
physiological function
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the enzyme is important for maintaining normal physiological functions such as growth and reproduction
physiological function
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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
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physiological function
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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
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