Information on EC 2.4.1.11 - glycogen(starch) synthase

New: Word Map on EC 2.4.1.11
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.4.1.11
-
RECOMMENDED NAME
GeneOntology No.
glycogen(starch) synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-glucose + [(1->4)-alpha-D-glucosyl]n = UDP + [(1->4)-alpha-D-glucosyl]n+1
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glycogen biosynthesis
-
-
glycogen biosynthesis II (from UDP-D-Glucose)
-
-
Starch and sucrose metabolism
-
-
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).
CAS REGISTRY NUMBER
COMMENTARY hide
9014-56-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
swine parasite
-
-
Manually annotated by BRENDA team
snail
-
-
Manually annotated by BRENDA team
female
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
; granule-bound starch synthase
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
tapeworm
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
sea mussel
-
-
Manually annotated by BRENDA team
strain FGSC424, eild type
-
-
Manually annotated by BRENDA team
rainbow trout
-
-
Manually annotated by BRENDA team
sheep
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP-glucose + (1,4-alpha-D-glucosyl)n
ADP + (1,4-alpha-D-glucosyl)n+1
show the reaction diagram
ADP-glucose + glycogen
? + ADP
show the reaction diagram
-
-
-
-
?
ADP-glucose + glycogen
ADP + ?
show the reaction diagram
dTDP-glucose + (1,4-alpha-D-glucosyl)n
dTDP + (1,4-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
-
?
GDP-glucose + (1,4-alpha-D-glucosyl)n
GDP + (1,4-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
-
?
UDP-glucose + (1,4-alpha-D-glucosyl)n
UDP + (1,4-alpha-D-glucosyl)n+1
show the reaction diagram
UDP-glucose + amylopectin
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-glucose + amylopectin
UDP + amylose + ?
show the reaction diagram
enzyme polymerizes glucose residues to the outer chains of amylopectin. These chains subsequently are cleaved off amylopectin to generate mature amylose
-
-
?
UDP-glucose + glucose
? + UDP
show the reaction diagram
-
-
-
-
?
UDP-glucose + glycogen
ADP + glycogen
show the reaction diagram
-
increased insulin receptor signaling and glycogen synthase activity contribute to the synergistic effect of exercise on insulin action
-
-
?
UDP-glucose + glycogen
glycogen + UDP
show the reaction diagram
UDP-glucose + glycogen
UDP + ?
show the reaction diagram
UDP-glucose + glycogen
UDP + glycogen
show the reaction diagram
-
glucose starvation results in UDP-glucose deficiency and inactivation of glycogen synthase
-
-
?
UDP-glucose + maltohexaose
? + UDP
show the reaction diagram
-
-
-
-
?
UDP-glucose + maltopentaose
? + UDP
show the reaction diagram
-
-
-
-
?
UDP-glucose + maltotetraose
? + UDP
show the reaction diagram
-
-
-
-
?
UDP-glucose + maltotriose
UDP + amylose
show the reaction diagram
-
-
-
?
UDP-glucose + starch
starch + UDP
show the reaction diagram
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-glucose + (1,4-alpha-D-glucosyl)n
UDP + (1,4-alpha-D-glucosyl)n+1
show the reaction diagram
A8V967
Cyanophora paradoxa synthesizes amylose with a granule-bound starch synthase displaying a preference for UDP-glucose
-
-
?
UDP-glucose + glycogen
ADP + glycogen
show the reaction diagram
-
increased insulin receptor signaling and glycogen synthase activity contribute to the synergistic effect of exercise on insulin action
-
-
?
UDP-glucose + glycogen
glycogen + UDP
show the reaction diagram
UDP-glucose + glycogen
UDP + glycogen
show the reaction diagram
-
glucose starvation results in UDP-glucose deficiency and inactivation of glycogen synthase
-
-
?
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaSO4
-
to a lesser extent, absence of glucose-6-phosphate
Cl-
-
activation
CoSO4
-
absence of glucose-6-phosphate
FeSO4
-
to a lesser extent, absence of glucose-6-phosphate
KCl
-
activation in presence of glucose 6-phosphate
MgCl2
-
10 mM, NaF inhibits activation
MgSO4
-
to a lesser extent, absence of glucose-6-phosphate
Na+
-
activation
Na2SO4
-
low concentrations
NaCl
-
activation in presence of glucose 6-phosphate
NH4Cl
-
activation in presence of glucose 6-phosphate
NiSO4
-
absence of glucose-6-phosphate
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
-
20% inactivation at 20 mM
1,5-gluconolactone
-
-
2,3-diphosphoglyceric acid
-
high concentrations
2-mercaptoethanol
-
high concentrations
adenine nucleotides
-
-
ADP-glucose
-
competitive with UDPglucose
beta-Glycerophosphate
-
-
Caffeine
-
10-50 mM
calyculin A
-
-
Cl-
-
-
D-glucose
-
-
D-glucose-1-phosphate
-
-
dithiobis-(2-nitrobenzoic acid)
-
77% inactivation at 1 mM
dithiothreitol
-
high concentrations
epinephrine
-
leads to phosphorylation of enzyme
ethanol
-
traces inactivate the enzyme
fructose 1,6-diphosphate
-
high concentrations
glucagon
-
leads to phosphorylation of enzyme
glucosamine
-
high concentrations during cultivation
glucose
Insulin
-
pre-treatment of cells inhibits, 0.001 mM isoproterenol reverses inhibition
-
iodoacetate
Iodobenzoate
-
22% inactivation at 1 mM
-
KCN
-
58% inhibition at 0.1 M
microcystin
-
-
-
N-ethylmaleimide
-
83% inactivation at 3 mM
Na2SO4
-
high concentrations
nucleoside phosphates
-
overview
okadaic acid
-
-
Oxytocin
-
leads to phosphorylation of enzyme
p-chloromercuribenzoate
-
90% inactivation at 0.01 mM, dithiothreitol reverses
phenylmercuric acetate
-
-
phloridzin
-
50% inhibition at 3.3 mM
Phorbol esters
-
-
phosphate
potassium borate
-
80% inhibition at 0.2 M
theophylline
-
10-50 mM
Trehalose phosphate
-
59% inhibition at 10 mM
UDP-galactose
-
-
UDP-glucose
UDP-pyridoxal
uridine 5'-phosphate
-
50% inhibition
Vasopressin
-
leads to phosphorylation of enzyme
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-diphosphoglyceric acid
-
low concentrations
2-deoxyglucose 6-phosphate
-
stimulates interconversion of D to I form
aspartate
-
increased uptake leads to activation
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
D-glucose
dihydroxyacetone
-
increase of activity
fructose
-
increase of activity
fructose 1,6-diphosphate
-
low concentrations
galactose
-
increase of activity
galactose 6-phosphate
glucosamine
-
low concentrations during cultivation
glucosamine 6-phosphate
glucose 6-phosphate
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
glutamate
-
increased uptake leads to activation
glycogen
-
-
Insulin
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
-
mannose
-
increase of activity
phosphate
proline
-
increased uptake leads to activation
Propionate
-
significant activation
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
-
ribose 5-phosphate
-
stimulates interconversion of D to I form
SO42-
-
stimulatory effect increases as the enzyme becomes more phosphorylated
staurosporine
-
-
xylitol
-
increase of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.1 - 46.9
ADP-glucose
2 - 10
amylopectin
4
dTDP-glucose
-
80C, pH 5.0
3.9
GDP-glucose
-
80C, pH 5.0
2.4 - 4.6
glycogen
0.0005 - 21.3
UDP-glucose
additional information
additional information
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
580
adenine
-
80C, pH 5.0
5.4
ADP
-
80C, pH 5.0
22
ADP-glucose
-
-
3.7
AMP
-
80C, pH 5.0
290
D-glucose
-
80C, pH 5.0
120
D-glucose-1-phosphate
-
80C, pH 5.0
20
phosphate
-
-
5.4
UDP
-
80C, pH 5.0
17
UDP-galactose
-
80C, pH 5.0
18
UDP-glucose
-
-
0.043 - 6.5
UMP
90
uridine
-
80C, pH 5.0
0.017
UTP
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
synthase D
4.7
-
-
9.83
-
synthase I
11.3
-
synthase I
14.13
-
-
21 - 25
-
synthase I
22
-
presence of 20 mM glucose 6-phosphate
30 - 35
-
synthase D
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9.2
-
synthase D, presence of glucose 6-phosphate
6.7
-
synthase I, enzyme form 1, absence of Na2SO4
6.8 - 9.2
-
synthase I, presence of glucose 6-phosphate
7 - 8.5
-
synthase D, absence of glucose 6-phosphate
7 - 9
-
synthase I
7 - 9
-
synthase I
7
-
synthase I, broad pH optimum
7.1
-
synthase I, enzyme form 2, absence of Na2SO4
7.2
-
synthase D, MOPS buffer
7.2 - 8
-
synthase I, absence of glucose 6-phosphate
7.4
-
glucose 6-phosphate independent form
7.5
-
absence of glucose 6-phosphate
7.7
-
synthase I, enzyme form 1, presence of Na2SO4
8.3
-
glucose 6-phosphate dependent form
8.4
-
muscle enzyme
8.5
-
synthase I, narrow pH optimum
9.5
-
low-mobility isoform
10
-
high-mobility isoform
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
25
-
both low-mobility isoform and high-mobility isoform
30 - 40
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.78
GYS1, sequence calculation
5.84
sequence calculation
6.46
GYS2, sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
strong expression, relative levels of Cg-GYS transcripts appear highest in October corresponding to glycogen storage and resting period
Manually annotated by BRENDA team
-
strong expression, relative levels of Cg-GYS transcripts appear highest in October corresponding to glycogen storage and resting period
Manually annotated by BRENDA team
-
glycolytic glioma cells with active glycogen synthase are sensitive to phosphatase and tensin homolog (PTEN) and inhibitors of phosphatidylinositol-3 kinase and gluconeogenesis
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
glycolytic glioma cells with active glycogensynthase are sensitive to phosphatase and tensin homolog (PTEN) and inhibitors of phosphatidylinositol-3 kinase and gluconeogenesis
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
longitudinal sarcoplasmic reticulum membrane membrane
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
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 FostersO)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
87000
-
calculated from amino acids residues
100000
-
gel filtration
170000
-
synthase I, sucrose density gradient centrifugation
183000
-
synthase D, sucrose density gradient centrifugation
270000
-
sucrose density gradient centrifugation
274000 - 312000
-
sucrose density gradient centrifugation
280000
-
gel filtration
300000 - 310000
300000 - 400000
-
gel filtration
340000
-
native enzyme
377000
-
high speed sedimentation equilibrium centrifugation
390000
410000
420000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
trimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
the enzyme has two potential N-glycosylation sites at residues 520 and 577
phosphoprotein
additional information
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 20C. 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, 20C, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement
-
sitting drop vapor diffusion method
-
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 7.6
-
-
488424
7.4 - 8.4
-
sensitive to small changes in pH in the presence of Mg2+
488424
7.4 - 8.2
-
-
488423
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
stable in imidazole or beta-glycerophosphate buffer, instable in Tris or glycylglycine buffer
42
-
inactivation after 30 min, sulfate protects
50
-
inactivation above
60
-
inactivation above
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
albumin is essential during lyophilization, lyophilized enzyme is stable for years
-
dithiothreitol stabilizes
-
freezing leads to loss of activity
-
glucose 6-phosphate stabilizes
-
glycogen stabilizes
Li+ increases hepatic glycogen synthase stability though a proteasome-related mechanism
-
phosphate stabilizes
-
spontaneous, temperature-dependent inactivation caused by irreversible conformational changes
-
sulfate stabilizes
UDP stabilizes
-
UDP-glucose stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, stable for 1 month in 5 mg/ml glycogen and 33% glycerol
-
-20C, 1% w/v bovine serum albumin, 2 weeks
-
-20C, 3 weeks, 55-100% loss of activity
-
-20C, 45 mM Tris/HCl buffer, pH 7.5, 1 mM 2-mercaptoethanol, 10% glycerol, several months
-
-20C, 45 mM Tris/HCl buffer, pH 7.5, 1 mM DTT, 10% glycerol, several months
-
-20C, glycogen-free or glycogen-containing enzyme, lyophilized, more than 3 years, solubilized enzyme several weeks
-
-20C, stable for several months
-
-60C, stable for 2 months
-
-70C, 50 mM Tris/HCl buffer, pH 7.8, 25% v/v glycerol, 5 mM EDTA, 2 mM EGTA, 1 mM DTT, 6 months
-
-70C, at least 6 months
-
-70C, beta-glycerophosphate buffer, 1 year
-
-70C, stable for at least 3 months
-
-70C, stable up to 6 months
-
-80C, 50 mM glycerophosphate buffer, pH 7.0, 2 mM EDTA, 40 mM 2-mercaptoethanol, 10% sucrose
-
-80C, with 5 mM glucose-6-phosphate, stable for at least 4 to 6 months
-
-85C, stable for several months
-
4C, 24 h stable
-
4C, stable for 1 week in 5 mg/ml glycogen
-
4C, stable for several days
-
liquid N2, 50 mM Tris/HCl buffer, pH 7.0, 1 mM DTT, 50% glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His6-tagged recombinant proteins
-
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
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA and amino acid sequence determination and analysis, phylogenetic analysis and tree
expression in Escherichia coli
-
expression in Escherichia coli strain BL21(DE3)/pG-Tf2
-
expression of His-tagged wild-type and mutant Gsy2 proteins in Escherichia coli strain BL21(DE3)
-
fusion with green fluorescence protein
-
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
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E510A
-
no enzyme activity
E518A
-
6% enzyme activity
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
S640A
-
phosphorylation mutant, moderate increase in the activity ratio
S644A
-
phosphorylation mutant, moderate increase in the activity ratio
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
H167A
-
1.1% of wild-type activity
K118A
-
1.5% of wild-type activity
K274A
-
0.2% of wild-type activity
K289A/K291A/R297A
-
46.4% of wild-type activity
K30A
-
100.6% of wild-type activity
K359A
-
122.3% of wild-type activity
K369A/R375A
-
46.8% of wild-type activity
K390A/R391A
-
109.7% of wild-type activity
K425A/R426A/R433A
-
1.2% of wild-type activity
K599A
-
47.7% of wild-type activity
R179A/R181A/R182A
-
39.1% of wild-type activity
R198A
-
0.4% of wild-type activity
R19A
-
161% of wild-type activity
R229A/R234A
-
7.2% of wild-type activity
R319A/K325A
-
0.2% of wild-type activity
R336A/K342A
-
55.9% of wild-type activity
R459A
-
30.1% of wild-type activity
R470A/K472A
-
0.6% of wild-type activity
R496A
-
145% of wild-type activity
R555A/R556A/K558A
-
0.3% of wild-type activity
R579A/R580A/R582A
-
36.2% of wild-type activity
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
R586A/R558A/R591A
-
71.1% of wild-type activity
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
R609A/R615A
-
125.8% of wild-type activity
S650D
-
97.8% of wild type activity
S650D/S654D
-
140.3% of wild type activity
S650D/S654D/S667D
-
110.8% of wild type activity
S650D/T667D
-
91.4% of wild type activity
S654D
-
96.2% of wild type activity
S654D/T667D
-
116.5% of wild type activity
T667D
-
68.6% of wild type activity
W510A
-
1.7% of wild-type activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
Show AA Sequence (444 entries)
Please use the Sequence Search for a certain query.