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Information on EC 2.4.1.11 - glycogen(starch) synthase
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2.4.1.11 glycogen(starch) synthaseIUBMB Comments
The accepted name varies according to the source of the enzyme and the nature of its synthetic product (cf. EC 2.4.1.1, phosphorylase). Glycogen synthase from animal tissues is a complex of a catalytic subunit and the protein glycogenin. The enzyme requires glucosylated glycogenin as a primer; this is the reaction product of EC 2.4.1.186 (glycogenin glucosyltransferase). A similar enzyme utilizes ADP-glucose (EC 2.4.1.21, starch synthase).
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Word Map
- 2.4.1.11
- kinase-3
- insulin
- phosphorylase
- diabetes
-
insulin-stimulated
- alzheimer
-
clamp
- hepatocytes
-
disposal
- mellitus
- phosphatidylinositol
- 6-phosphate
- lithium
- 3-kinase
- tau
- hexokinase
-
hyperphosphorylation
-
glycogenolysis
- hyperglycemia
- glucose-6-phosphatase
- glucagon
- niddm
- amylose
-
euglycemic
- soleus
-
hyperinsulinemic
- adp-glucose
-
nonoxidative
- lateralis
-
glucose-6-p
-
waxy
-
insulin-induced
-
insulin-mediated
-
amp-dependent
-
non-insulin-dependent
-
glycogenesis
- licl
-
insulin-resistant
-
vastus
- gsk-3beta
- irs-1
-
phosphatase-2a
-
2,6-bisphosphate
- lafora
- nutrition
- axin
- substrate-1
- phosvitin
-
euglycemic-hyperinsulinemic
- kinase-3beta
- amylopectin
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
Synonyms
Cg-GYS, GBSS, glucosyltransferase, uridine diphosphoglucose-glycogen, glycogen synthase, glycogen synthase 2, glycogen synthase-2, glycogen synthetase (starch), granule-bound starch synthase, GSN, GSY2p, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glucosyltransferase, uridine diphosphoglucose-glycogen
-
-
-
-
glycogen synthase
glycogen synthetase (starch)
-
-
-
-
GSY2p
-
-
-
-
GYS1
GYS2
UDP-glucose-glycogen glucosyltransferase
-
-
-
-
UDP-glycogen synthase
-
-
-
-
UDPG-glycogen synthetase
-
-
-
-
UDPG-glycogen transglucosylase
-
-
-
-
uridine diphosphoglucose-glycogen glucosyltransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose + [(1->4)-alpha-D-glucosyl]n = UDP + [(1->4)-alpha-D-glucosyl]n+1
reaction mechanism
-
UDP-alpha-D-glucose + [(1->4)-alpha-D-glucosyl]n = UDP + [(1->4)-alpha-D-glucosyl]n+1
reaction mechanism
-
UDP-alpha-D-glucose + [(1->4)-alpha-D-glucosyl]n = UDP + [(1->4)-alpha-D-glucosyl]n+1
reaction mechanism
-
UDP-alpha-D-glucose + [(1->4)-alpha-D-glucosyl]n = UDP + [(1->4)-alpha-D-glucosyl]n+1
reaction mechanism
-
UDP-alpha-D-glucose + [(1->4)-alpha-D-glucosyl]n = UDP + [(1->4)-alpha-D-glucosyl]n+1
glycogen synthase performs a stepwise SNi-like mechanism, involving the concerted departure of the leaving group and the attack of the incoming nucleophile, via ion-pair intermediate 1,5-anhydro-D-arabino-hex-1-enitol or its tautomeric form, 1,5-anhydro-D-fructose, bound at the catalytic site. Even in the absence of a glucosyl acceptor, glycogen synthase promotes the formation of the cationic intermediate, which, by eliminating the proton of the adjacent C2 carbon atom, yields 1,5-anhydro-D-arabino-hex-1-enitol, overview
-
UDP-alpha-D-glucose + [(1->4)-alpha-D-glucosyl]n = UDP + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:glycogen 4-alpha-D-glucosyltransferase
The accepted name varies according to the source of the enzyme and the nature of its synthetic product (cf. EC 2.4.1.1, phosphorylase). Glycogen synthase from animal tissues is a complex of a catalytic subunit and the protein glycogenin. The enzyme requires glucosylated glycogenin as a primer; this is the reaction product of EC 2.4.1.186 (glycogenin glucosyltransferase). A similar enzyme utilizes ADP-glucose (EC 2.4.1.21, starch synthase).
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CAS REGISTRY NUMBER
COMMENTARY
9014-56-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dTDP-glucose + (1,4-alpha-D-glucosyl)n
dTDP + (1,4-alpha-D-glucosyl)n+1
-
-
-
-
?
GDP-glucose + (1,4-alpha-D-glucosyl)n
GDP + (1,4-alpha-D-glucosyl)n+1
-
-
-
-
?
UDP-alpha-D-glucose + [(1->4)-alpha-D-glucosyl]n-[glycogenin]
UDP + [(1,4)-alpha-D-glucosyl]n+1 + glycogenin
-
-
-
?
UDP-glucose + amylopectin
UDP + amylose + ?
enzyme polymerizes glucose residues to the outer chains of amylopectin. These chains subsequently are cleaved off amylopectin to generate mature amylose
-
-
?
UDP-glucose + glycogen
ADP + glycogen
-
increased insulin receptor signaling and glycogen synthase activity contribute to the synergistic effect of exercise on insulin action
-
-
?
UDP-glucose + glycogen
UDP + glycogen
-
glucose starvation results in UDP-glucose deficiency and inactivation of glycogen synthase
-
-
?
ADP-glucose + (1,4-alpha-D-glucosyl)n
ADP + (1,4-alpha-D-glucosyl)n+1
Cyanophora paradoxa synthesizes amylose with a granule-bound starch synthase displaying a preference for UDP-glucose
-
-
?
ADP-glucose + (1,4-alpha-D-glucosyl)n
ADP + (1,4-alpha-D-glucosyl)n+1
-
the enzyme can use ADP-glucose or UDP-glucose as donor substrate
-
-
?
ADP-glucose + (1,4-alpha-D-glucosyl)n
ADP + (1,4-alpha-D-glucosyl)n+1
-
-
-
-
?
ADP-glucose + glycogen
ADP + ?
-
-
with granule-bound starch synthase, ADP-glucose is used at less than 2% of the activity with UDP-glucose
-
?
UDP-glucose + (1,4-alpha-D-glucosyl)n
UDP + (1,4-alpha-D-glucosyl)n+1
Cyanophora paradoxa synthesizes amylose with a granule-bound starch synthase displaying a preference for UDP-glucose
-
-
?
UDP-glucose + (1,4-alpha-D-glucosyl)n
UDP + (1,4-alpha-D-glucosyl)n+1
-
the enzyme can use ADP-glucose or UDP-glucose as donor substrate
-
-
?
UDP-glucose + (1,4-alpha-D-glucosyl)n
UDP + (1,4-alpha-D-glucosyl)n+1
-
-
-
-
?
UDP-glucose + (1,4-alpha-D-glucosyl)n
UDP + (1,4-alpha-D-glucosyl)n+1
-
-
-
-
?
UDP-glucose + (1,4-alpha-D-glucosyl)n
UDP + (1,4-alpha-D-glucosyl)n+1
-
conjugated bile acids regulate hepatocyte glycogen synthase activity in vitro and in vivo via Galphai signaling
-
-
?
UDP-glucose + glycogen
glycogen + UDP
-
greater affinity to low molecular mass glycoproteins
-
-
?
UDP-glucose + glycogen
glycogen + UDP
-
important role in initial stages of glycogen biogenesis
-
-
?
UDP-glucose + glycogen
glycogen + UDP
-
transfers glucose to glycogen as well as to its phosphorylase limit dextrin, but not to its beta-amylase dextrin, glucose, maltose and maltotriose are not acceptors
-
-
?
UDP-glucose + glycogen
glycogen + UDP
-
-
-
-
?
UDP-glucose + glycogen
glycogen + UDP
-
-
-
-
?
UDP-glucose + glycogen
glycogen + UDP
-
-
-
-
?
UDP-glucose + glycogen
UDP + ?
-
UDP-glucose is preferred substrate for granule-bound starch synthase and low and high mobility isoforms of starch synthase
-
-
?
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
-
?
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
-
glycogen synthase reacts with its glucosyl donor substrate, uridine 5'-diphosphoglucose to produce the scission of the covalent bond between the terminal phosphate oxygen of UDP and the sugar ring. UDP presence in the active site of the enzyme of a glucose-like derivative that lacks the exocyclic oxygen attached to the anomeric carbon
-
-
?
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
-
?
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
?
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
?
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
?
additional information
?
-
-
a point mutation in the UDP-glucose diphosphorylase gene results in decreases of UDP-glucose. Chronically low UDP-glucose levels in cells result in inactivation of glycogen synthase, owing to loss of the ability of glycogen synthase to bind UDP-glucose - non-substrate-dependent control of glycogen synthase
-
-
-
additional information
?
-
enzyme is able to use both ADP-glucose and UDP-glucose but displays a sixfold higher Vmax with UDP-glucose
-
-
-
additional information
?
-
-
enzyme is able to use both ADP-glucose and UDP-glucose but displays a sixfold higher Vmax with UDP-glucose
-
-
-
additional information
?
-
one mechanism by which peroxisome proliferator-activated receptor-alpha agonist treatment improves whole body insulin sensitivity is by increasing skeletal muscle GS total activity
-
-
-
additional information
?
-
-
O-GlcNAc has a role in the regulation of glycogen synthase both in normoglycemia and diabetes
-
-
-
additional information
?
-
-
glycogen synthase 2 is a novel target gene of peroxisome proliferator-activated receptors
-
-
-
additional information
?
-
-
key enzyme in regulation of glycogen synthesis, controlled by multisite phosphorylation, phosphorylation of Ser640 by DYRK family protein kinases causes strong inactivation of glycogen synthase, functionally important site 3a in glycogen synthase by protein kinases from the DYRK family may be involved in a mechanism for the regulation of glycogen synthesis
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + [(1->4)-alpha-D-glucosyl]n-[glycogenin]
UDP + [(1,4)-alpha-D-glucosyl]n+1 + glycogenin
-
-
-
?
UDP-glucose + (1,4-alpha-D-glucosyl)n
UDP + (1,4-alpha-D-glucosyl)n+1
A8V967
Cyanophora paradoxa synthesizes amylose with a granule-bound starch synthase displaying a preference for UDP-glucose
-
-
?
UDP-glucose + glycogen
ADP + glycogen
-
increased insulin receptor signaling and glycogen synthase activity contribute to the synergistic effect of exercise on insulin action
-
-
?
UDP-glucose + glycogen
UDP + glycogen
-
glucose starvation results in UDP-glucose deficiency and inactivation of glycogen synthase
-
-
?
UDP-glucose + glycogen
glycogen + UDP
-
-
-
-
?
UDP-glucose + glycogen
glycogen + UDP
-
important role in initial stages of glycogen biogenesis
-
-
?
UDP-glucose + glycogen
glycogen + UDP
-
-
-
-
?
UDP-glucose + glycogen
glycogen + UDP
-
-
-
-
?
UDP-glucose + glycogen
glycogen + UDP
-
-
-
-
?
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
-
?
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
-
?
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
F2Q6J8
-
-
-
?
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
E0X6R2, E0X6R4
-
-
-
?
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
E0X6R2, E0X6R4
-
-
-
?
additional information
?
-
-
a point mutation in the UDP-glucose diphosphorylase gene results in decreases of UDP-glucose. Chronically low UDP-glucose levels in cells result in inactivation of glycogen synthase, owing to loss of the ability of glycogen synthase to bind UDP-glucose - non-substrate-dependent control of glycogen synthase
-
-
-
additional information
?
-
Q8MJ26
one mechanism by which peroxisome proliferator-activated receptor-alpha agonist treatment improves whole body insulin sensitivity is by increasing skeletal muscle GS total activity
-
-
-
additional information
?
-
-
O-GlcNAc has a role in the regulation of glycogen synthase both in normoglycemia and diabetes
-
-
-
additional information
?
-
-
glycogen synthase 2 is a novel target gene of peroxisome proliferator-activated receptors
-
-
-
additional information
?
-
-
key enzyme in regulation of glycogen synthesis, controlled by multisite phosphorylation, phosphorylation of Ser640 by DYRK family protein kinases causes strong inactivation of glycogen synthase, functionally important site 3a in glycogen synthase by protein kinases from the DYRK family may be involved in a mechanism for the regulation of glycogen synthesis
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Li+
Mg2+
Mn2+
MnSO4
additional information
MnSO4
-
MnSO4-dependent glucose transfer is catalyzed by a non-glucose 6-phosphate dependent form of the enzyme
additional information
-
no divalent cation requirement, no activation by Fe3+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Insulin
-
pre-treatment of cells inhibits, 0.001 mM isoproterenol reverses inhibition
-
p-chloromercuribenzoate
-
90% inactivation at 0.01 mM, dithiothreitol reverses
additional information
-
not inhibitory: EDTA, iodoacetic acid, thioglycolate, trypsin and chymotrypsin decrease activity to 60% within 60 min
-
additional information
-
the eukaryotic enzyme is inhibited by protein kinase mediated phosphorylation, four arginine residues of a regulatory helix regulate the response to phosphorylation. When Thr668 is phosphorylated, Arg580 and Arg581 play a role in stabilizing the inhibited conformation by directly interacting with the phosphate group at or near the N-terminus of the regulatory helix, possibly near one of the sulfate binding sites in our basal state structure
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Bile acids
-
enhance the activity of the insulin receptor and glycogen synthase in primary hepatocytes
bisperoxyvanadium 1,10-phenanthroline
-
phosphatidylinositol 3-kinase inhibitor wortmannin and rapamycin inhibits activation
glucose-6-phosphate
-
D-glucose 6-phosphate binding structure, Arg580 forms an interaction with the 6-phosphate of D-glucose 6-phosphate, overview. The eukaryotic enzyme is activated by protein phosphatases and D-glucose 6-phosphate binding. The enzyme's response to D-glucose 6-phosphate is controlled by Arg583 and Arg587, while four additional arginine residues present within the same regulatory helix regulate the response to phosphorylation
insulin-like growth factor 1
-
stimulation of 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-1increase 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
-
relaxin
-
stimulation of 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
-
D-glucose
-
phosphatidylinositol 3-kinase inhibitor wortmannin inhibits activation
glucose 6-phosphate
-
synthase D, i.e. phosphorylated form, is glucose 6-phosphate dependent, synthase I, i.e. dephosphorylated form, is glucose 6-phosphate independent, interconversion of D and I forms and vice versa
glucose 6-phosphate
-
synthase D, i.e. phosphorylated form, is glucose 6-phosphate dependent, synthase I, i.e. dephosphorylated form, is glucose 6-phosphate independent, interconversion of D and I forms and vice versa
glucose 6-phosphate
-
synthase D, i.e. phosphorylated form, is glucose 6-phosphate dependent, synthase I, i.e. dephosphorylated form, is glucose 6-phosphate independent, interconversion of D and I forms and vice versa
glucose 6-phosphate
-
glucose-6-phosphate dependent form is inactive in vivo
glucose 6-phosphate
-
synthase D, i.e. phosphorylated form, is glucose 6-phosphate dependent, synthase I, i.e. dephosphorylated form, is glucose 6-phosphate independent, interconversion of D and I forms and vice versa
glucose 6-phosphate
-
enzyme from cells cultivated in low glucose concentrations is more sensitive to glucose 6-phosphate
glucose 6-phosphate
-
synthase D, i.e. phosphorylated form, is glucose 6-phosphate dependent, synthase I, i.e. dephosphorylated form, is glucose 6-phosphate independent, interconversion of D and I forms and vice versa
glucose 6-phosphate
-
stimulates at UDP-glucose concentration of 0.4 mM; synthase D, i.e. phosphorylated form, is glucose 6-phosphate dependent, synthase I, i.e. dephosphorylated form, is glucose 6-phosphate independent, interconversion of D and I forms and vice versa
glucose 6-phosphate
-
2fold activation in vivo and 10fold activation in vitro
glucose 6-phosphate
-
synthase D, i.e. phosphorylated form, is glucose 6-phosphate dependent, synthase I, i.e. dephosphorylated form, is glucose 6-phosphate independent, interconversion of D and I forms and vice versa
glucose 6-phosphate
-
synthase D, i.e. phosphorylated form, is glucose 6-phosphate dependent, synthase I, i.e. dephosphorylated form, is glucose 6-phosphate independent, interconversion of D and I forms and vice versa
Insulin
-
stimulation of 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-1increase 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
-
Insulin
-
phosphatidylinositol 3-kinase inhibitor wortmannin inhibits activation
-
phosphate
-
e.g. sugar phosphates, inorganic phosphate, nucleoside phosphates, activation of synthase I
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.31 - 0.32
UDP-glucose
-
value independent of glucose 6-phosphate concentration
0.415 - 0.416
UDP-glucose
-
synthase D, value independent of presence of glucose 6-phosphate
0.57 - 1.25
UDP-glucose
-
value dependent on the presence of glucose 6-phosphate
additional information
additional information
-
dependence on glucose 6-phosphate concentration
-
additional information
additional information
-
dependence on glucose 6-phosphate concentration
-
additional information
additional information
-
glycogen: 3.5 mg/ml
-
additional information
additional information
-
values for phosphorylated enzyme forms
-
additional information
additional information
-
regulation by phosphorylation
-
additional information
additional information
-
regulation by phosphorylation
-
additional information
additional information
-
regulation by phosphorylation
-
additional information
additional information
-
dependence on glucose 6-phosphate concentration
-
additional information
additional information
-
dependence on glucose 6-phosphate concentration
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21
40
additional information
additional information
-
measurement of glycogen synthase activity in crude extracts by capillary electrophoresis
additional information
-
assay based on ESI-mass spectrometry enables detection of submicromolar quantities of substrate, thus requiring even lower concentrations of protein and is amenable to high throughput screening methods
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
8.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
30 - 40
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
human enzyme has no activity above 50°C, rat enzyme is active up to at least 60°C
additional information
-
human enzyme has no activity above 50°C, rat enzyme is active up to at least 60°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
488404, 488405, 488412, 488414, 488417, 488426, 488427, 488434, 488447, 488450, 659348, 671614, 671622
-
-
brenda
-
488406, 488420, 488421, 488424, 488428, 488435, 488439, 488442, 659002, 675727, 685034, 686586, 687921, 702190, 704484, 705511
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
synthetic peroxisome proliferator-activated receptor beta/delta, and gamma agonists markedly up-regulate Gys-2 mRNA and protein expression in mouse 3T3-L1 adipocytes
brenda
-
hypoxia activates glycogen synthase in fed rat myocardium through a combination of rapid glycogenolysis, elevated local glucose 6-phosphate content, and increased protein phosphatase 1 activity, and fasting attenuates this action independent of local glucose 6-phosphate content. Activation of glycogen synthase in myocardium induced by intermittent hypoxia is much lower in fasted than in fed rats
brenda
-
strong expression, relative levels of Cg-GYS transcripts appear highest in October corresponding to glycogen storage and resting period
brenda
-
strong expression, relative levels of Cg-GYS transcripts appear highest in October corresponding to glycogen storage and resting period
brenda
-
glycolytic glioma cells with active glycogen synthase are sensitive to phosphatase and tensin homolog (PTEN) and inhibitors of phosphatidylinositol-3 kinase and gluconeogenesis
brenda
-
in distal tubular cells, adiponectin through luminal ADIPOR1 activates AMPK, leading to the inhibition of glycogen synthase. During hyperglycemia, this regulation is altered, which may explain, at least in part, the accumulation of large glycogen deposits
brenda
-
glycolytic glioma cells with active glycogensynthase are sensitive to phosphatase and tensin homolog (PTEN) and inhibitors of phosphatidylinositol-3 kinase and gluconeogenesis
brenda
additional information
-
expression of Gys-2 is significantly reduced in adipose tissue of peroxisome proliferator-activated receptor alpha-/-, peroxisome proliferator-activated receptor beta/delta-/- and peroxisome proliferator-activated receptor gamma+/- mice
brenda
subcutaneous, expression of GYS2; subcutaneous, GYS1
brenda
high expression level of GYS1; high expression level of GYS1
brenda
-
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside positively regulates glycogen synthase activity and LDL receptor expression through Raf-1/MEK/p42/44MAPK/p90RSK/GSK-3 signaling cascade
brenda
-
upon rapamycin treatment, the overexpression of constitutively active Akt-1 in Hep-G2 cells leads to an increase in the phosphorylation of Akt (Ser 473) and, an increase in the GS and PP-1 activities, in contrast to a decrease in Akt phosphorylation and GS and PP-1 activities in parental HepG2 cells
brenda
-
insulin receptor substrate (IRS) protein 1 knockdown reduces the glycogen synthase activity in parental HepG2 cells. It is upregulated in HepG2-CA-Akt/PKB cells
brenda
-
reduction in glucose production in primary hepatocytes by the overexpression of the mutant GYS2. The elevation of liver glycogen synthase activity in primary hepatocytes reduces glucose production by shunting gluconeogenic precursors into glycogen rather than by stimulating direct glucose incorporation into glycogen
brenda
-
basal glycogen synthase activity in muscle lacking rictor is increased to that of insulin-stimulated controls. A decrease in basal levels of phosphorylated glycogen synthase at a GSK-3/protein phosphatase 1 (glycogen-associated protein phosphatase 1)-regulated site in rictor knockout muscle is observed. This change in glycogen synthase phosphorylation is associated with an increase in the catalytic activity of glycogen-associated glycogen-associated protein phosphatase 1 but not increased GSK-3 inactivation
brenda
-
contraction activates glycogen synthase in muscles from dexamethasone-treated rats
brenda
-
in low glycogen, basal and insulin-stimulated glycogen synthesis and glycogen synthase activation is higher and glycogen synthase phosphorylation (Ser645, Ser649, Ser653, Ser657) lower than in normal glycogen. Muscles with high glycogen show lower insulin-stimulated glycogen synthesis and glycogen synthase activation than normal glycogen despite similar dephosphorylation
brenda
-
of insulin-resistant, fat-fed rats and chow-fed controls, either maintained in the basal state or after a euglycaemichyperinsulinaemic clamp
brenda
-
elevated glycogen synthase activity in Polysaccharide Storage Myopathy horses. A gain of function mutation in GYS1 results in a glycogenosis
brenda
-
slowtwitch (soleus) and fast-twitch (epitrochlearis) muscle. Improved insulin-stimulated glucose uptake and glycogen synthase activation after adrenaline infusion
brenda
-
sucrose feeding does not alter muscle glycogen concentration but provokes a small reduction in the glycogen synthase activity ratio (-/+ glucose-6-phosphate) in red but not in white gastrocnemius. Dexamethasone administration augments glycogen concentration and reduces glycogen synthase activity ratio in both muscle fiber types
brenda
longissimus dorsi muscle, high expression level of GYS1
brenda
-
longissimus dorsi muscle, high expression level of GYS1
-
brenda
additional information
tissue distribution in tissues from the developmental stages from the first-instar larvae to fifth-instar to pupae and expression pattern, overview
brenda
additional information
-
tissue distribution in tissues from the developmental stages from the first-instar larvae to fifth-instar to pupae and expression pattern, overview
brenda
additional information
tissue expression pattern of GYS1, GYS1 is upregulated during porcine myogenic cell differentiation; tissue expression pattern of GYS2
brenda
additional information
tissue expression pattern of GYS1, GYS1 is upregulated during porcine myogenic cell differentiation; tissue expression pattern of GYS2
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
longitudinal sarcoplasmic reticulum membrane membrane
brenda
additional information
additional information
-
existence of 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, GS 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
-
brenda
additional information
neither glycogen synthase activity nor glycogen synthase protein are present in the cytosolic fraction of subfractionated skeletal muscle obtained after an overnight fast or after 90 min of insulin infusion during a hyperinsulinemic euglycemic clamp in healthy or in insulin-resistant monkeys. Glycogen synthase activity, glycogen synthase protein, and glycogen are present in all other fractions. In vivo insulin regulation of skeletal muscle glycogen synthase activity does not involve changes in the subcellular localization of glycogen synthase. One mechanism by which peroxisome proliferator-activated receptor-alpha agonist treatment improves whole body insulin sensitivity is by increasing skeletal muscle GS total activity
-
brenda
additional information
-
initial localization of glycogen synthase in a soluble pool plays an important role in glycogen synthesis, and that its sequestration in an insulin-resistant insoluble pool may explain in part the reduced glycogen synthesis caused by lipid oversupply
-
brenda
additional information
the enzyme contains no signal peptide, putative cleavage sites, and transmembrane domain
-
brenda
additional information
-
the enzyme contains no signal peptide, putative cleavage sites, and transmembrane domain
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
metabolism
physiological function
additional information
-
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
-
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
-
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
-
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; 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
-
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; 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
-
Show AA Sequence and Transmembrane Helices (3764 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85000
300000 - 310000
390000
410000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
trimer
?
x * 80600, about, GYS2, sequence calculation; x * 83700, about, GYS1, sequence calculation
?
-
x * 80600, about, GYS2, sequence calculation; x * 83700, about, GYS1, sequence calculation
-
trimer
-
homotrimeric protein. The contacts between subunits, which only involve the N-terminal domains, do not restrict the movements of the corresponding C-domains, likely required for catalysis
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
the enzyme has two potential N-glycosylation sites at residues 520 and 577
phosphoprotein
additional information
phosphoprotein
-
incorporation of 1.3 pmol phosphate per mol enzyme; phosphorylation leads to loss of activity; phosphorylation of glucose-6-phosphate independent enzyme, i.e. I enzyme, results in glucose-6-phosphate dependent enzyme, i.e. D enzyme
phosphoprotein
-
incorporation of 1-3 phosphates per subunit; phosphorylation leads to loss of activity; phosphorylation of glucose-6-phosphate independent enzyme, i.e. I enzyme, results in glucose-6-phosphate dependent enzyme, i.e. D enzyme
phosphoprotein
-
phosphorylation fails to convert between D and I form
phosphoprotein
-
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
phosphoprotein
-
multiple phosphorylations on serine residues leads to inactivation; phosphorylation leads to loss of activity; phosphorylation of glucose-6-phosphate independent enzyme, i.e. I enzyme, results in glucose-6-phosphate dependent enzyme, i.e. D enzyme
phosphoprotein
-
phosphorylation of glucose-6-phosphate independent enzyme, i.e. I enzyme, results in glucose-6-phosphate dependent enzyme, i.e. D enzyme
phosphoprotein
-
incorporation of 1.13 mol phosphate per subunit; phosphorylation leads to loss of activity
phosphoprotein
-
phosphorylation at more than 10 sites; phosphorylation leads to loss of activity; phosphorylation of glucose-6-phosphate independent enzyme, i.e. I enzyme, results in glucose-6-phosphate dependent enzyme, i.e. D enzyme
phosphoprotein
-
phosphorylated by Ca2+-calmodulin dependent protein kinase in fast-twitch skeletal muscle. Phosphorylation does not affect glycogen synthase activity by itself, but it might be necessary for the modulation of glycogen synthase by other protein kinases
phosphoprotein
-
phosphorylation of enzyme a into b leads to an altered enzyme activity in adult rats, newborn rat enzyme does not show b into a transformation
phosphoprotein
-
in the absence of insulin, glycogen synthase Ser645, Ser649, Ser653, and Ser657 phosphorylation is similar in soleus muscles from control and dexamethasone-treated rats. In epitrochlearis, glycogen synthase phosphorylation is slightly elevated in muscles from dexamethasone-treated rats. Contraction decreases glycogen synthase Ser645, Ser649, Ser653, and Ser657 phosphorylation in soleus to a similar low level in muscles from control and dexamethasone-treated rats. In epitrochlearis muscles, contraction also decreases glycogen synthase phosphorylation to a low level in muscles from control and dexamethasone-treated rats. In soleus and epitrochlearis muscles, the combination of contraction and insulin does not decrease glycogen synthase phosphorylation more than contraction alone
phosphoprotein
-
in low glycogen, basal and insulin-stimulated glycogen synthesis and glycogen synthase activation is higher and glycogen synthase phosphorylation (Ser645, Ser649, Ser653, Ser657) lower than in normal glycogen. Muscles with high glycogen show lower insulin-stimulated glycogen synthesis and glycogen synthase activation than normal glycogen despite similar dephosphorylation
phosphoprotein
-
incorporation of 3 phosphates per subunit; phosphorylation leads to loss of activity; phosphorylation of glucose-6-phosphate independent enzyme, i.e. I enzyme, results in glucose-6-phosphate dependent enzyme, i.e. D enzyme
phosphoprotein
-
0.7-0.9 mol phosphate per mol protein; phosphorylation leads to loss of activity
phosphoprotein
-
the eukaryotic enzymes are inhibited by protein kinase mediated phosphorylation and activated by protein phosphatases and glucose-6-phosphate binding, regulation, overview
phosphoprotein
the enzyme harbors a C-terminal cluster of phosphorylation sites, but no N-terminal phosphorylation sites
phosphoprotein
regulatory sites of GYS1 that undergo reversible phosphorylation are identified: two of them, sites 2 and 2a, are located near the N-terminus, while the remaining seven sites, 3a, 3b, 3c, 4, 5, 1a, and 1b, are found within the C-terminus. Insulin promotes dephosphorylation of glycogen synthase in differentiated porcine satellite cells; regulatory sites of GYS2 that undergo reversible phosphorylation are identified: two of them, sites 2 and 2a, are located near the N-terminus, while the remaining seven sites, 3a, 3b, 3c, 4, and 5 are found within the C-terminus, GYS2 does not contain sites 1a and 1b
phosphoprotein
-
regulatory sites of GYS1 that undergo reversible phosphorylation are identified: two of them, sites 2 and 2a, are located near the N-terminus, while the remaining seven sites, 3a, 3b, 3c, 4, 5, 1a, and 1b, are found within the C-terminus. Insulin promotes dephosphorylation of glycogen synthase in differentiated porcine satellite cells; regulatory sites of GYS2 that undergo reversible phosphorylation are identified: two of them, sites 2 and 2a, are located near the N-terminus, while the remaining seven sites, 3a, 3b, 3c, 4, and 5 are found within the C-terminus, GYS2 does not contain sites 1a and 1b
-
additional information
-
no covalently attached amino sugars, 2% carbohydrate
additional information
the enzyme contains no signal peptide, putative cleavage sites, and transmembrane domain
additional information
-
the enzyme contains no signal peptide, putative cleavage sites, and transmembrane domain
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
crystals from the protein and from its selenomethionyl variant are grown in 100 mM sodium citrate pH 5.6 containing 20% PEG and 20% dioxane by hanging drop vapour-diffusion method at 20°C. Crystals grow in thin needles, diffract to 3.5 A resolution and belong to space group C2, with unit-cell parameters a = 202 A, b = 73 A, c = 149 A, beta = 131°
-
purified recombinant enzyme in complex with UDP-Glc, sitting drop vapor diffusion method, 0.002 ml of 5 mg/ml protein in 50-mM Tris-HCl, pH 7.4, with 10 mM UDP-Glc is mixed with 0.002 ml reservoir solution containing 0.1-M sodium citrate, pH 4.0, and 20-28% 2-methyl-2,4-pentanediol, 2 months, 20°C, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement
-
purified recombinant His-tagged enzyme, basal state and glucose-6-phosphate activated state Gsy2p, X-ray diffraction structure determination and analysis at 3.0 A and 2.4 A, respectively, modeling
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R243X
-
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
-
phosphorylation mutant. Mutation does not cause singnificant changes in the activation state
S648A
-
phosphorylation mutant. Mutation does not cause singnificant changes in the activation state
S652A
-
phosphorylation mutant. Mutation does not cause singnificant changes in the activation state
S656A
-
phosphorylation mutant. Mutation does not cause singnificant changes in the activation state
S7A
-
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
-
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
-
phosphorylation double mutant, large increase in the activity ratio both in soluble and insoluble fraction
S7A/S640A
-
phosphorylation double mutant, large increase in the activity ratio both in soluble and insoluble fraction
S7A/S644A
-
phosphorylation double mutant, large increase in the activity ratio both in soluble and insoluble fraction
S7A/S648A
-
phosphorylation double mutant, large increase in the activity ratio both in soluble and insoluble fraction
S7A/S652A
-
phosphorylation double mutant, large increase in the activity ratio both in soluble and insoluble fraction
S7A/S656A
-
phosphorylation double mutant, large increase in the activity ratio both in soluble and insoluble fraction
R580A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R580A/R581A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R580A/R581A/R583A
-
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
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R589A/R592A
-
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
-
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
stable in imidazole or beta-glycerophosphate buffer, instable in Tris or glycylglycine buffer
30
37
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
albumin is essential during lyophilization, lyophilized enzyme is stable for years
-
glycogen stabilizes
Li+ increases hepatic glycogen synthase stability though a proteasome-related mechanism
-
spontaneous, temperature-dependent inactivation caused by irreversible conformational changes
-
sulfate stabilizes
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 45 mM Tris/HCl buffer, pH 7.5, 1 mM 2-mercaptoethanol, 10% glycerol, several months
-
-20°C, glycogen-free or glycogen-containing enzyme, lyophilized, more than 3 years, solubilized enzyme several weeks
-
-70°C, 50 mM Tris/HCl buffer, pH 7.8, 25% v/v glycerol, 5 mM EDTA, 2 mM EGTA, 1 mM DTT, 6 months
-
-80°C, 50 mM glycerophosphate buffer, pH 7.0, 2 mM EDTA, 40 mM 2-mercaptoethanol, 10% sucrose
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant Gsy2 proteins from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
-
the COOH-terminal fragment of glycogenin can be used as an effective high affinity reagent for the purification of glycogen synthase from skeletal muscle and liver
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
cDNA and amino acid sequence determination and analysis, phylogenetic analysis and tree
expression of His-tagged wild-type and mutant Gsy2 proteins in Escherichia coli strain BL21(DE3)
-
gene GYS1, in silico cloning, DNA and amino acid sequence determination and analysis, promoter determination and analysis, quantitative real-time RT-PCR tissue expression analysis; gene GYS2, in silico cloning, DNA and amino acid sequence determination and analysis, promoter determination and analysis, quantitative real-time RT-PCR tissue expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression level of GYS1 is upregulated from proliferation to differentiation in the porcine satellite cells
heat-shock down-regulates gsn gene transcription in wild-type as well as in mutants deficient in adenylyl cyclase activity and a temperature-sensitive mutant defective in the regulatory subunit of protein kinase A
-
insulin does not significantly affect the transcription of GYS1
under starvation conditions, glycogen synthase transcript expression rapidly decreases with increasing starvation time
expression level of GYS1 is upregulated from proliferation to differentiation in the porcine satellite cells
expression level of GYS1 is upregulated from proliferation to differentiation in the porcine satellite cells
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
nutrition
-
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
-
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
-
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
-
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
-
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
-
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
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pitcher, J.; Smythe, C.; Cohen, P.
Glycogenin is the priming glucosyltransferase required for the initiation of glycogen biogenesis in rabbit skeletal muscle
Eur. J. Biochem.
176
391-395
1988
Oryctolagus cuniculus
brenda
Leloir, L.F.; Cardini, C.E.
UDPG-glycogen transglucosylase
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbäck, K. , eds. )
6
317-326
1962
Oryctolagus cuniculus, Rattus norvegicus, Saccharomyces cerevisiae
-
brenda
Westphal, S.A.; Nuttall, F.Q.
Comparative characterization of human and rat liver glycogen synthase
Arch. Biochem. Biophys.
292
479-486
1992
Homo sapiens, Rattus norvegicus
brenda
Sangan, P.; Gunasekaran, M.
Purification and properties of glycogen synthase from Phymatotrichum omnivorum
Mycologia
83
669-673
1991
Phymatotrichopsis omnivora
-
brenda
Peng, Z.Y.; Trumbly, R.J.; Reimann, E.M.
Purification and characterization of glycogen synthase from a glycogen-deficient strain of Saccharomyces cerevisiae
J. Biol. Chem.
265
13871-13877
1990
Saccharomyces cerevisiae
brenda
Carabaza, A.; Arino, J.; Fox, J.W.; Villar-Palasi, C.; Guinovart, J.J.
Purification, characterization and partial amino acid sequence of glycogen synthase from Saccharomyces cerevisiae
Biochem. J.
268
401-407
1990
Saccharomyces cerevisiae
brenda
Hannigan, L.L.; Donahue, M.J.; Masaracchia, R.A.
Comparative purification and characterization of invertebrate muscle glycogen synthase from the porcine parasite Ascaris suum
J. Biol. Chem.
260
16099-16105
1985
Ascaris suum
brenda
Dickey-Dunkirk, S.; Killilea, S.D.
Purification of bovine heart glycogen synthase
Anal. Biochem.
146
199-205
1985
Bos taurus
brenda
Camici, M.; DePaoli-Roach, A.A.; Roach, P.J.
Rabbit liver glycogen synthase. Purification and comparison of the properties of glucose-6-P-dependent and glucose-6-P-independent forms of the enzyme
J. Biol. Chem.
259
3429-3434
1984
Oryctolagus cuniculus
brenda
Mitchell, J.W.; Thomas, J.A.
Phosphorylation of bovine heart glycogen synthase by two protein kinases. Kinetic properties of phosphorylated forms of the enzyme
J. Biol. Chem.
256
6160-6169
1981
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