Information on EC 3.1.3.17 - [phosphorylase] phosphatase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.3.17
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RECOMMENDED NAME
GeneOntology No.
[phosphorylase] phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[phosphorylase a] + 4 H2O = 2 [phosphorylase b] + 4 phosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
SYSTEMATIC NAME
IUBMB Comments
[phosphorylase a] phosphohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9025-74-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the enzyme regulates glycogen metabolism by inhibiting glycogen phosphorylase activity and activating glycogen synthase activity
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glycogen phosphorylase + H2O
?
show the reaction diagram
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?
glycogen phosphorylase a + H2O
glycogen phosphorylase b + phosphate
show the reaction diagram
glycogen synthase + H2O
phosphate + ?
show the reaction diagram
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-
-
-
?
histone II-A + H2O
phosphate + ?
show the reaction diagram
inhibitor 1 + H2O
phosphate + ?
show the reaction diagram
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-
-
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?
lysine-rich histone + H2O
phosphate + ?
show the reaction diagram
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-
-
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?
phosphohistone + H2O
phosphate + ?
show the reaction diagram
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?
phosphorylase a + H2O
phosphorylase b + phosphate
show the reaction diagram
phosphorylase kinase + H2O
phosphate + dephosphorylated phosphorylase kinase
show the reaction diagram
phosphorylated casein + H2O
phosphate + ?
show the reaction diagram
protamine + H2O
phosphate + ?
show the reaction diagram
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-
-
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?
regulatory subunit of cAMP-dependent protein kinase + H2O
phosphate + ?
show the reaction diagram
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-
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?
troponin I + H2O
phosphate + ?
show the reaction diagram
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?
additional information
?
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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
glycogen phosphorylase a + H2O
glycogen phosphorylase b + phosphate
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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oscillation of cytosolic Ca2+, has an important regulatory function in the phosphorylation-dephosphorylation cycle for regulation of glycogen phosphorylase activity, overview
Co2+
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activates
Mg2+
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Km: 0.003 mM, activity is dependent on divalent metal ions, Mg2+ or Mn2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-hydroxyethyl disulfide
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5,5'-dithiobis(2-nitrobenzoic acid)
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D-Pantethine
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Disulfides
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irreversible inactivation
glucose 1-phosphate
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inhibits by binding to one subunit of phosphorylase a
Glycerophosphate
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glycogen
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partially inhibits by binding to one subunit of phosphorylase a
iodoacetamide
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50 mM, 30% inhibition after 1 h at 30C
iodoacetic acid
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50 mM, 30% inhibition after 1 h at 30C
microcystin-LR
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Mn2+
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3 mM, 64% inhibition
NaCl
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0.1-0.3 M, 40-96% inhibition
okadaic acid
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phosphorylase b
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poly(L-lysine)
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0.001 mM, strong
protein
synthetic peptide analog of ribosomal protein S6
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0.2 mM S6229-239, 50% inhibition
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UDP-glucose
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ZnCl2
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10 mM
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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maximal activation at 50 mM, absolute requirement for SH compounds
ascorbic acid
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maximal activation at 1 mM
dithiothreitol
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maximal activation at 1 mM, absolute requirement for SH compounds
ethanol
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80% ethanol, activation of both isoenzymes, conversion of isoenzyme H-1 to a 35500 Da form and isoenzyme H-2 to a 67000 Da form and a 35500 Da form
glucose
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50 mM, activates
glucose 6-phosphate
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0.25 mM, activates
Insulin
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induces the enzyme in diabetic rats
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p-nitrophenyl phosphate
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slight stimulation
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.046
histone
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0.002 - 0.0029
phosphorylase a
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.3
histone
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5.2
phosphorylase a
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
synthetic peptide analog of ribosomal protein S6
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S6229-239
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000053
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liver lysate
0.00422
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glycogen fraction
7.9
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692
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muscle enzyme
2086
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liver enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
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7.5
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.7
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about 50% of maximal activity at pH 6.5 and at pH 8.7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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the enzyme is glycogen-bound via a glycogen-targeting subunit
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
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1 * 31000 regulatory subunit + 1 * 38000 catalytic subunit, SDS-PAGE
33400
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gel filtration
34000
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sucrose density gradient ultracentrifugation
34800
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1 * 34800, SDS-PAGE
35000
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gel filtration
37000
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x * 37000, SDS-PAGE
78000
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gel filtration
160000
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gel filtration
260000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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1 * 31000 regulatory subunit + 1 * 38000 catalytic subunit, SDS-PAGE
monomer
additional information
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subunit interaction, role in controle and regulation, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no modification
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the enzyme is free of bound phosphate, carbohydrate, lipids and nucleic acids
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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30 min, 90% loss of activity
94688
6
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unstable below
94679
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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15 min, 50% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
complete inactivation after treatment with 0.3 M perchloric acid or 10% trichloroacetic acid
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complete inactivation after treatment with 1% dodecyl sulfate or 0.05% cetyltrimethylammonium bromide or 1 M guanidine-HCl after 15 min
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complete inactivation after treatment with 10% w/w pronase at 30C for 3 h
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resistant to trypsin and chymotrypsin and to 8 M urea
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the 31000 Da regulatory subunit is extremely susceptible to proteolysis, rapidly destroyed by incubation with trypsin
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deoxycholate
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stable to 0.5% deoxycholate, 24 h
Ethanol
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stable to 25% ethanol at -5C, 3 h
Triton X-100
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stable to 0.5% Triton X-100, 24 h
Tween
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stable to 0.1% Tween 20, 40 or 80, 24 h
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-28C, 60% glycerol, stable for 10 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli. Expression of the enzyme in the pET3a vector results in the expression of the enzyme as an insoluble aggregate. The vector with the trp-lac hybrid promotor the enzyme is expressed as a soluble protein at levels of 3-4% of the soluble Escherichia coli protein
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