Information on EC 3.1.3.42 - [glycogen-synthase-D] phosphatase

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The expected taxonomic range for this enzyme is: Opisthokonta

EC NUMBER
COMMENTARY
3.1.3.42
-
RECOMMENDED NAME
GeneOntology No.
[glycogen-synthase-D] phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
[glycogen-synthase D] + H2O = [glycogen-synthase I] + phosphate
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
[UDP-glucose:glycogen 4-alpha-D-glucosyltransferase-D] phosphohydrolase
The product is EC 2.4.1.11 glycogen(starch) synthase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycogen glucosyltransferase phosphatase
-
-
-
-
glycogen synthase D phosphatase
-
-
-
-
glycogen synthase phosphatase
-
-
-
-
glycogen synthase phosphatase
-
-
glycogen synthetase phosphatase
-
-
-
-
UDP-glycogen glucosyltransferase phosphatase
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-
-
-
UDPglucose-glycogen glucosyltransferase phosphatase
-
-
-
-
uridine diphosphoglucose-glycogen glucosyltransferase phosphatase
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9043-28-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
S. carlsbergensis, ATCC 9080
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
casein + H2O
?
show the reaction diagram
-
-
-
-
?
glycogen phosphorylase + H2O
?
show the reaction diagram
-
rabbit muscle glycogen phosphorylase
-
-
?
glycogen synthase + H2O
?
show the reaction diagram
-
-
-
-
-
glycogen synthase D + H2O
glycogen synthase I + phosphate
show the reaction diagram
-
-
-
?
glycogen synthase D + H2O
glycogen synthase I + phosphate
show the reaction diagram
-
-
-
?
glycogen synthase D + H2O
glycogen synthase I + phosphate
show the reaction diagram
-
-
-
?
glycogen synthase D + H2O
glycogen synthase I + phosphate
show the reaction diagram
-
-
-
?
glycogen synthase D + H2O
glycogen synthase I + phosphate
show the reaction diagram
-
-
-
?
glycogen synthase D + H2O
glycogen synthase I + phosphate
show the reaction diagram
-
-
-
?
glycogen synthase D + H2O
glycogen synthase I + phosphate
show the reaction diagram
-
glycogen synthase D from liver, glycogen synthase D1, D2 and D3 from muscle
-
?
glycogen synthase D + H2O
glycogen synthase I + phosphate
show the reaction diagram
-
inactive glycogen synthase D
active glycogen synthase I, i.e. EC 2.4.1.11
?
glycogen synthase D + H2O
glycogen synthase I
show the reaction diagram
-
-
-
-
?
muscle phosphorylase kinase + H2O
?
show the reaction diagram
-
alpha-subunit of rabbit muscle phosphorylase kinase
-
-
?
phosphocasein + H2O
?
show the reaction diagram
-
-
-
-
?
phosphoprotein phosphatase + H2O
protein + phosphate
show the reaction diagram
-
-
-
-
?
histone phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
little activity towards phosphorylase a or phosphohistone
-
-
-
additional information
?
-
-
glycogen synthase phosphatase interacts with heat shock factor to activate CUP1 gene transcription
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-
-
additional information
?
-
-
glycogen does not control enzyme activity
-
-
-
additional information
?
-
-
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
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphoprotein phosphatase + H2O
protein + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
glycogen synthase phosphatase interacts with heat shock factor to activate CUP1 gene transcription
-
-
-
additional information
?
-
-
glycogen does not control enzyme activity
-
-
-
additional information
?
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
Mg2+, Mn2+ or Co2+ required
Mg2+
-
required, maximal activity at 5 mM Mg2+
Mg2+
-
Mg2+, Mn2+ or Co2+ required
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
required
Mn2+
-
can partially replace Mg2+, 75% of the activity with Mg2+
Mn2+
-
Mg2+, Mn2+ or Co2+ required
Mn2+
-
Mn2+ or Mg2+ required
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
the inhibition may contribute to the mechanism by which cyclic-AMP-independent hormones inhibit glycogen synthesis in the liver
diphosphate
-
0.2 mM
glycogen
-
competitive inhibition with glycogen synthase D as substrate
KF
-
50 mM, 30C, pH 7.8, complete inhibition
Na2SO3
-
1 mM, 27% inhibition
phosphate
-
0.2 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
5 mM, 2.4fold activation
D-Glucosamine 6-phosphate
-
2 mM, 30C, pH 7.8, 3.2fold activation
D-glucose 1-phosphate
-
2 mM, 30C, pH 7.8, 3.8fold activation
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
galactose 6-phosphate
-
0.1 mM, stimulates activity
glucosamine 6-phosphate
-
0.1 mM, stimulates activity
glucose 6-phosphate
-
0.1 mM, about 2fold increase in activity
glucose 6-phosphate
-
stimulates
Mg2+
-
5 mM, 3.7fold activation, without Mg2+ 33% remaining activity and additionally without D-glucose 6-phosphate 23.1% remaining activity
Mn2+
-
5 mM, 4.4fold activation
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-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.3
-
-
at 30C
7.4
-
-
glycylglycine buffer
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
more than 70% of the activity is recovered in the postmicrosomal supernatant; the enzyme is largely recovered in the glycogen fraction and to a minor extent in the cytosol
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
26000
-
-
minor peak, gel filtration
40000
-
-
gel filtration
40000
-
-
-
49000
-
-
major peak, gel filtration
50000
-
-
gel filtration
160000
-
-
gel filtration
additional information
-
-
partially purified enzyme is resolved in three fractions by gel filtration, 115000 Da, 340000 Da, and 500000 Da
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
-
1 * 48000, SDS-PAGE
trimer
-
1 * 37000 + 1 * 53000 + 1 * 60000, SDS-PAGE
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
57
-
-
4 min, 80% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
dithiothreitol, 1.7 mM, and bovine serum albumin, 0.07%, stabilize the enzyme during assay
-
enzyme dialyzed against EDTA is stable to freezing and thawing in absence of Mn2+
-
Mn2+, 5 mM, stabilizes
-
ethanol, 80%, 21C, inactivation is totally prevented by 2 mM MgCl2
-
trypsin treatment of the subcellular fractions results in complete loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, storage overnight, complete loss of activity, activity can be restored after addition of 20% v/v glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE