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Information on EC 3.1.3.42 - [glycogen-synthase-D] phosphatase
for references in articles please use BRENDA:EC3.1.3.42
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.3 Phosphoric-monoester hydrolases
3.1.3.42 [glycogen-synthase-D] phosphatase
IUBMB Comments
The product is EC 2.4.1.11 glycogen(starch) synthase.
The enzyme appears in viruses and cellular organisms
- 3.1.3.42
- phosphorylase
-
glycogen-bound
-
adrenalectomized
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glucagon-treated
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g-component
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glucose-6-p
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insulin-mediated
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protein-glycogen
showSynonyms
glycogen synthase phosphatase, glycogen synthetase phosphatase, glycogen synthase d phosphatase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glycogen glucosyltransferase phosphatase
-
-
-
-
glycogen synthase D phosphatase
-
-
-
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glycogen synthase phosphatase
glycogen synthetase phosphatase
-
-
-
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UDP-glycogen glucosyltransferase phosphatase
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-
-
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UDPglucose-glycogen glucosyltransferase phosphatase
-
-
-
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uridine diphosphoglucose-glycogen glucosyltransferase phosphatase
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-
-
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glycogen synthase phosphatase
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[glycogen-synthase D] + H2O = [glycogen-synthase I] + phosphate
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-
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
[UDP-glucose:glycogen 4-alpha-D-glucosyltransferase-D] phosphohydrolase
The product is EC 2.4.1.11 glycogen(starch) synthase.
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CAS REGISTRY NUMBER
COMMENTARY
9043-28-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glycogen phosphorylase + H2O
?
-
Substrates: rabbit muscle glycogen phosphorylase
Products: -
Products: -
?
muscle phosphorylase kinase + H2O
?
-
Substrates: alpha-subunit of rabbit muscle phosphorylase kinase
Products: -
Products: -
?
phosphoprotein phosphatase + H2O
protein + phosphate
-
Substrates: -
Products: -
Products: -
?
glycogen synthase D + H2O
glycogen synthase I + phosphate
-
Substrates: -
Products: -
Products: -
?
glycogen synthase D + H2O
glycogen synthase I + phosphate
-
Substrates: -
Products: -
Products: -
?
glycogen synthase D + H2O
glycogen synthase I + phosphate
-
Substrates: glycogen synthase D from liver, glycogen synthase D1, D2 and D3 from muscle
Products: -
Products: -
?
glycogen synthase D + H2O
glycogen synthase I + phosphate
-
Substrates: inactive glycogen synthase D
Products: active glycogen synthase I, i.e. EC 2.4.1.11
Products: active glycogen synthase I, i.e. EC 2.4.1.11
?
glycogen synthase D + H2O
glycogen synthase I + phosphate
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Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: glycogen does not control enzyme activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: a low basal synthase phosphatase activity and a defect in its response to insulin explains, at least in part, reduced insulin stimulation of skeletal muscle glycogen synthase associated with insulin resistance
Products: -
Products: -
?
additional information
?
-
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Substrates: little activity towards phosphorylase a or phosphohistone
Products: -
Products: -
?
additional information
?
-
-
Substrates: glycogen synthase phosphatase interacts with heat shock factor to activate CUP1 gene transcription
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphoprotein phosphatase + H2O
protein + phosphate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: glycogen does not control enzyme activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: a low basal synthase phosphatase activity and a defect in its response to insulin explains, at least in part, reduced insulin stimulation of skeletal muscle glycogen synthase associated with insulin resistance
Products: -
Products: -
?
additional information
?
-
-
Substrates: glycogen synthase phosphatase interacts with heat shock factor to activate CUP1 gene transcription
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
the inhibition may contribute to the mechanism by which cyclic-AMP-independent hormones inhibit glycogen synthesis in the liver
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glucose 6-phosphate
-
4.9fold activation, without D-glucose 6-phosphate 38.8% remainimng activity and additionally without D-glucose 6-phosphate 23.1% remaining activity
Mg2+
-
5 mM, 3.7fold activation, without Mg2+ 33% remaining activity and additionally without D-glucose 6-phosphate 23.1% remaining activity
additional information
-
no effects of 5 mM K+ and Na+, and 2 mM 6-P-gluconate, D-fructose 1,6-bisphosphate, alpha-glycerol phosphate, creatine phosphate, phosphate, and SO42-
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hyperglycemia
Opposite effects of hyperglycemia and insulin deficiency on liver glycogen synthase phosphatase activity in the diabetic rat.
Insulin Resistance
Impaired insulin-stimulated muscle glycogen synthase activation in vivo in man is related to low fasting glycogen synthase phosphatase activity.
Insulin Resistance
Insulin resistance is associated with reduced fasting and insulin-stimulated glycogen synthase phosphatase activity in human skeletal muscle.
Starvation
Effect of prolonged starvation on glycogen synthase and glycogen synthase phosphatase activity in rat heart.
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
-
more than 70% of the activity is recovered in the postmicrosomal supernatant
-
brenda
additional information
-
the enzyme is largely recovered in the glycogen fraction and to a minor extent in the cytosol
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
additional information
-
partially purified enzyme is resolved in three fractions by gel filtration, 115000 Da, 340000 Da, and 500000 Da
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
5 min, 20 mM Tris-HCl, pH 7.4, 0.2% bovine serum albumin, enzyme species of 49000 Da, more than 65% loss of activity towards synthase D and phosphocasein
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol, 1.7 mM, and bovine serum albumin, 0.07%, stabilize the enzyme during assay
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enzyme dialyzed against EDTA is stable to freezing and thawing in absence of Mn2+
-
trypsin treatment of the subcellular fractions results in complete loss of activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, storage overnight, complete loss of activity, activity can be restored after addition of 20% v/v glycerol
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bollen, M.; Vandenheede, J.R.; Goris, J.; Stalmans, W.
Characterization of glycogen-synthase phosphatase and phosphorylase phosphatase in subcellular liver fractions
Biochim. Biophys. Acta
969
66-77
1988
Rattus norvegicus
brenda
Tsuiki, S.; Hiraga, A.; Kikuchi, K.; Tamura, S.
Purification of an Mg2+-dependent protein phosphatase
Methods Enzymol.
159
437-446
1988
Rattus norvegicus
brenda
Tsuiki, S.; Kikuchi, K.; Tamura, S.; Hiraga, A.; Shineha, R.
Glycogen synthase phosphatase and phosphorylase phosphatase of rat liver
Adv. Protein Phosphatases
1
193-214
1985
Rattus norvegicus
-
brenda
Hiraga, A.; Kikuchi, K.; Tamura, S.; Tsuiki, S.
Purification and characterization of Mg2+-dependent glycogen synthase phosphatase (phosphoprotein phosphatase Ia) from rat liver
Eur. J. Biochem.
119
503-510
1981
Rattus norvegicus
brenda
Feigenbaum Binstock, J.; Li, H.C.
A novel glycogen synthase phosphatase
Biochem. Biophys. Res. Commun.
87
1226-1234
1979
Oryctolagus cuniculus
brenda
Mackenzie, C.W.; Bulbulian, G.J.; Bishop, J.S.
Use of fluoride to inactivate phosphorylase a phosphatases from rat liver cytosol. Presence of fluoride-insensitive glycogen synthase-specific phosphatase
Biochim. Biophys. Acta
614
413-424
1980
Rattus norvegicus
brenda
Kikuchi, K.; Tamura, S.; Hiraga, A.; Tsuiki, S.
Glycogen synthase phosphatase of rat liver. Its separation from phosphorylase phosphatase on DE-52 columns
Biochem. Biophys. Res. Commun.
75
29-37
1977
Rattus norvegicus
brenda
Kato, K.; Bishop, J.S.
Glycogen synthetase-D phosphatase. I. Some new properties of the partially purified enzyme from rabbit skeletal muscle
J. Biol. Chem.
247
7420-7429
1972
Oryctolagus cuniculus
brenda
Abe, N.; Tsuiki, S.
Studies on glycogen synthase D phosphatase of rat liver multiple nature
Biochim. Biophys. Acta
350
383-391
1974
Rattus norvegicus
brenda
Mishra, C.
Evidence for the occurence of glycogen synthase phosphatases and kinases in yeast
FEMS Microbiol. Lett.
18
25-29
1983
Saccharomyces cerevisiae
-
brenda
Peng, Z.Y.; Wang, W.; Wilson, S.E.; Schlender, K.K.; Trumbly, R.J.; Reimann, E.M.
Identification of a glycogen synthase phosphatase from yeast Saccharomyces cerevisiae as protein phosphatase 2A
J. Biol. Chem.
266
10925-10932
1991
Saccharomyces cerevisiae
brenda
Cadefau, J.; Bollen, M.; Stalmans, W.
Glucose-induced glycogenesis in the liver involves the glucose-6-phosphate-dependent dephosphorylation of glycogen synthase
Biochem. J.
322
745-750
1997
Rattus norvegicus
brenda
Kida, Y.; Esposito-Del Puente, A.; Bogardus, C.; Mott, D.M.
Insulin resistance is associated with reduced fasting and insulin-stimulated glycogen synthase phosphatase activity in human skeletal muscle
J. Clin. Invest.
85
476-481
1990
Homo sapiens
brenda
Stalmans, W.; Mvumbi, L.
Inhibition of glycogen synthase phosphatase by Ca2+
Biochem. Soc. Trans.
13
890
1985
Rattus norvegicus
-
brenda
Lin, J.T.; Lis, J.T.
Glycogen synthase phosphatase interacts with heat shock factor to activate CUP1 gene transcription in Saccharomyces cerevisiae
Mol. Cell. Biol.
19
3237-3245
1999
Saccharomyces cerevisiae
brenda
Vardanis, A.
Regulation of glycogen synthesis in human skeletal muscle: does cellular glycogen control glycogen synthase phosphatase activity?
Biochem. Int.
25
289-298
1991
Homo sapiens
brenda
Thomas, J.A.; Nakai, C.
Control of glycogen synthase phosphatase from rat heart
J. Biol. Chem.
248
2208-2213
1973
Rattus norvegicus
brenda
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