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
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medicine
nutrition
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calorie restriciton does not alter glycogen synthase or glycogen phosphatase activity/protein levels in young rats. Calorie restriction hinders age-related decreases in glycogen synthase activity/protein, unrelated to glycogen synthase mRNA levels, and glycogen synthase inactivation-phosphorylation
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glycogen synthase activity correlates inversely with phosphorylation of glycogen synthase sites 2 + 2a and 3a. Insulin significantly decreases 2 + 2a phosphorylation in lean subjects only and induces a larger dephosphorylation at site 3 in lean compared with obese subjects. The exaggerated insulin resistance in type 2 diabetes mellitus compared with obese subjects is not reflected by differences in site 3 phosphorylation but is accompanied by a significantly higher site 1b phosphorylation during insulin stimulation. Hyperphosphorylation of another Ca2/calmodulin-dependent kinase-II target, phospholamban-Thr17, is also evident in type 2 diabetes mellitus. Dephosphorylation of glycogen synthase by phosphatase treatment fully restores glycogen synthase activity in all groups
medicine
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in patients with polycystic ovary syndrome, reduced insulin-mediated glucose disposal is associated with a lower insulin-stimulated glycogen synthase activity, explained by absent insulin-mediated dephosphorylation of glycogen synthase at the NH2-terminal sites 2 + 2a, whereas dephosphorylation at the COOH-terminal sites 3a + 3b is intact in polycystic ovary syndrome subjects. Insulin activation of glycogen synthase is dependent on dephosphorylation of sites 3a + 3b in women with polycystic ovary syndrome. No significant abnormalities in glycogen synthaseK-3 or -3 are found. Pioglitazone treatment improves insulin-stimulated glucose metabolism and glycogen synthase activity in polycystic ovary syndrome and restores the ability of insulin to dephosphorylate glycogen synthase at sites 2 and 2a
medicine
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insulin, insiulin-like growth factor 1 and relaxin stimulate the enzymatic activity. In patients with type 1 diabetes glycogen synthase activity remains unchanged versus control, and insulin does not stimulate the enzyme activity. In patients with type 2 diabetes a significant decrease in glycogen synthase activity is accompanied by the decrease in the effect of peptides, giving the following order of their efficiency: insulin = IGF-1 > relaxin. In myometrium of pregnant women with gestational treated and untreated diabetes, glycogen synthase activity decreases, the effect of insulin is weaker, whereas the effects of relaxin and IGF-1 increase thus giving the following order of their efficiency: relaxin > IGF-1 > insulin. Insulin therapy of type 1 diabetes incompletely restores sensitivity of the enzymes to the peptide actions
medicine
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mutation R243X has been identified in a patient with glycogen storage disease type 0, together with frameshift mutation 966_967delGA/insC introducing a stop codon 21 amino acids downstream from the site of the mutation and leading to loss of 51% of the C-terminal portion of the protein. Patient is heterozygous for the mutations and presents with fasting hypoglycemia and postprandial hyperglycemia
medicine
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old compared to young rats maintained ad libitum on a standard diet have reduced glycogen synthase activity, lower muscle glycogen synthase protein levels, increased phosphorylation of glycogen synthase at site 3a with less activation in soleus muscle. Age-associated impairments in glycogen synthase protein and activation-phosphorylation are also shown in tibialis anterior muscle. There is an age-associated reduction in glycogen phosphorylase activity level in soleus, while brain/muscle isoforms of glycogen phosphorylase protein levels are higher. Calorie restriciton does not alter glycogen synthase or glycogen phosphatase activity/protein levels in young rats. Calorie restriction hinders age-related decreases in glycogen synthase activity/protein, unrelated to glycogen synthase mRNA levels, and glycogen synthase inactivation-phosphorylation
medicine
patient with muscle-specific glycogen synthase deficiency due to homozygous two base pair deletion in exon 2, c.162-163delAG. Mutation is predicted to result in a protein frameshift that alters the amino acid sequence after the mutation and terminates prematurely. Patient presents with abnormal mitochondrial ultrastructure and pre-ragged red fibres, predominance of type I oxidative fibres in the muscle and depletion of glycogen stores