BRENDA - Enzyme Database
show all sequences of 3.1.3.47

Phosphorylation-dephosphorylation of rat liver 3-hydroxy 3-methylglutaryl coenzyme A reductase associated with changes in activity

Gil, G.; Sitges, M.; Bove, J.; Hegardt, G.; FEBS Lett. 110, 195-199 (1980)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
fluoride
-
Rattus norvegicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate + H2O
Rattus norvegicus
-
?
-
-
-
Organic Solvent Stability
Organic Solvent
Commentary
Organism
Ethanol
after treatment with this solvent a catalytic subunit of 32000-35000 Da is obtained, activity increased
Rattus norvegicus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rattus norvegicus
-
-
-
Purification (Commentary)
Commentary
Organism
liver
Rattus norvegicus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
Storage Stability
Storage Stability
Organism
-40°C, several months, no measurable loss of activity
Rattus norvegicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate + H2O
-
94963
Rattus norvegicus
[hydroxymethylglutaryl-CoA reductase (NADPH)] + phosphate
-
94963
Rattus norvegicus
?
[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate + H2O
-
94963
Rattus norvegicus
?
-
-
-
-
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
for the catalytic subunit of 32000-35000 Da retrieved after ethanol treatment
Rattus norvegicus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
fluoride
-
Rattus norvegicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate + H2O
Rattus norvegicus
-
?
-
-
-
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
Ethanol
after treatment with this solvent a catalytic subunit of 32000-35000 Da is obtained, activity increased
Rattus norvegicus
Purification (Commentary) (protein specific)
Commentary
Organism
liver
Rattus norvegicus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
Storage Stability (protein specific)
Storage Stability
Organism
-40°C, several months, no measurable loss of activity
Rattus norvegicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate + H2O
-
94963
Rattus norvegicus
[hydroxymethylglutaryl-CoA reductase (NADPH)] + phosphate
-
94963
Rattus norvegicus
?
[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate + H2O
-
94963
Rattus norvegicus
?
-
-
-
-
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
for the catalytic subunit of 32000-35000 Da retrieved after ethanol treatment
Rattus norvegicus
Other publictions for EC 3.1.3.47
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
94956
Sitges M.; Gil G.; Hegardt G.
Partial purification from rat ...
Rattus norvegicus
J. Lipid Res.
25
497-506
1984
-
-
-
-
-
-
4
-
2
-
3
1
-
2
-
-
1
-
-
1
3
1
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
2
-
3
1
-
-
-
1
-
1
3
1
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
94957
Hegardt G.; Gil G.; Calvet E.
Inactivation of rat liver HMG- ...
Rattus norvegicus
J. Lipid Res.
24
821-830
1983
-
-
-
-
-
-
7
-
-
2
2
1
-
2
-
-
1
-
-
1
3
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
7
-
-
-
2
2
1
-
-
-
1
-
1
3
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
94958
Brown W.E.; Rodwell V.W.
Purification and properties of ...
Rattus norvegicus
Biochim. Biophys. Acta
751
218-229
1983
-
-
-
-
-
-
2
-
1
-
2
1
2
1
-
-
1
-
-
2
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
2
1
2
-
-
1
-
2
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
94959
Feingold K.R.; Wiley M.H.; Moser A.H.; Lear S.R.; Siperstein M.D.
Activation of HMG-CoA reductas ...
Rattus norvegicus
J. Lipid Res.
24
290-296
1983
-
-
-
-
-
-
2
-
4
-
-
1
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
4
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
94960
Feingold K.R.; Wiley M.H.; Moser A.H.; Lear S.R.; Siperstein M.D.
Inhibition of HMG-CoA reductas ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
107
1376-1383
1982
-
-
-
-
-
-
2
-
1
-
-
1
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
94961
Gil G.; Hegardt F.
Some properties of purified 3- ...
Rattus norvegicus
Arch. Biochem. Biophys.
214
192-198
1982
-
-
-
-
-
-
6
-
2
-
-
1
-
1
-
-
1
-
-
3
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
2
-
-
1
-
-
-
1
-
3
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
94962
Gil G.; Sitges M.; Hegardt F.G.
Purification and properties of ...
Rattus norvegicus
Biochim. Biophys. Acta
663
211-221
1981
-
-
-
-
-
-
1
3
-
-
2
1
1
1
-
-
1
-
-
1
3
1
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
2
1
1
-
-
1
-
1
3
1
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
94963
Gil
Phosphorylation-dephosphorylat ...
Rattus norvegicus
FEBS Lett.
110
195-199
1980
-
-
-
-
-
-
1
-
-
-
-
1
1
1
-
-
1
-
-
1
-
1
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
1
-
1
-
1
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-