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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results (Engineering
Engineering on EC 2.4.1.11 - glycogen(starch) synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
R243X
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mutation 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
S10A
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phosphorylation mutant. Mutation does not cause singnificant changes in the activation state
S648A
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phosphorylation mutant. Mutation does not cause singnificant changes in the activation state
S652A
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phosphorylation mutant. Mutation does not cause singnificant changes in the activation state
S656A
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phosphorylation mutant. Mutation does not cause singnificant changes in the activation state
S7A
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phosphorylation mutant, large increase in the activity ratio both in soluble and insoluble fraction. Enzyme is almost fully active and able to induce glycogen deposition in primary hepatocytes incubated in the absence of glucose and in FTO2B cells, a cell line that does not normallysynthesize glycogen. Mutation is also sufficient to trigger the aggregation and translocation of liver glycogen synthase from the cytoplasm to the hepatocyte cell cortex in the absence of glucose
S7A/E509A
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phosphorylation and active site mutant. Translocation of liver glycogen synthase from the cytoplasm to the hepatocyte cell cortex in the absence of glucose is not observed
S7A/S10A
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phosphorylation double mutant, large increase in the activity ratio both in soluble and insoluble fraction
S7A/S640A
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phosphorylation double mutant, large increase in the activity ratio both in soluble and insoluble fraction
S7A/S644A
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phosphorylation double mutant, large increase in the activity ratio both in soluble and insoluble fraction
S7A/S648A
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phosphorylation double mutant, large increase in the activity ratio both in soluble and insoluble fraction
S7A/S652A
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phosphorylation double mutant, large increase in the activity ratio both in soluble and insoluble fraction
S7A/S656A
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phosphorylation double mutant, large increase in the activity ratio both in soluble and insoluble fraction
R580A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R580A/R581A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R580A/R581A/R583A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme. The triple mutant enzyme is resistant to inhibition by Pho85p/Pcl10p phosphorylation
R587A/R589A/R592A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R589A/R592A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
additional information
identification of homozygous two base pair deletion in exon 2, c.162-163delAG resulting in muscle-specific glycogen synthase deficiency. 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
additional information
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identification of homozygous two base pair deletion in exon 2, c.162-163delAG resulting in muscle-specific glycogen synthase deficiency. 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
additional information
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generation of a wild-type 640 truncation mutant with increased activity compared to the wild-type, and of point mutation variants with nonphospho- and phospho-peptides ligated, which alters the mutant activities, overview
