BRENDA - Enzyme Database show
show all sequences of 1.1.1.32

Stereochemistry of the reaction catalyzed by mevaldate reductase

Ngan, H.L.; Popjak, G.; Bioorg. Chem. 4, 166-180 (1975)
No PubMed abstract available

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-3-hydroxy-3-methyl-5-oxovaleric acid + NADH
Sus scrofa
-
(R)-3-hydroxy-3-methyl-5-hydroxyvaleric acid + NAD+
-
Sus scrofa
-
(S)-3-hydroxy-3-methyl-5-oxovaleric acid + NADH
Sus scrofa
-
(S)-3-hydroxy-3-methyl-5-hydroxyvaleric acid + NAD+
-
Sus scrofa
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sus scrofa
-
-
-
Reaction
Reaction
Commentary
Organism
(R)-mevalonate + NAD+ = mevaldate + NADH + H+
stereospecific insertion of hydride into C-5, hydride is added from the re-face of carbonyl group in 3R and 3S-isomers
Sus scrofa
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Sus scrofa
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.2
-
partially purified liver enzyme
Sus scrofa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-3-hydroxy-3-methyl-5-oxovaleric acid + NADH
-
286553
Sus scrofa
(R)-3-hydroxy-3-methyl-5-hydroxyvaleric acid + NAD+
-
286553
Sus scrofa
-
(R)-3-hydroxy-3-methyl-5-oxovaleric acid + NADPH
-
286553
Sus scrofa
(R)-3-hydroxy-3-methyl-5-hydroxyvaleric acid + NADP+
-
286553
Sus scrofa
-
(S)-3-hydroxy-3-methyl-5-oxovaleric acid + NADH
-
286553
Sus scrofa
(S)-3-hydroxy-3-methyl-5-hydroxyvaleric acid + NAD+
-
286553
Sus scrofa
-
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
-
Sus scrofa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Sus scrofa
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-3-hydroxy-3-methyl-5-oxovaleric acid + NADH
Sus scrofa
-
(R)-3-hydroxy-3-methyl-5-hydroxyvaleric acid + NAD+
-
Sus scrofa
-
(S)-3-hydroxy-3-methyl-5-oxovaleric acid + NADH
Sus scrofa
-
(S)-3-hydroxy-3-methyl-5-hydroxyvaleric acid + NAD+
-
Sus scrofa
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Sus scrofa
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.2
-
partially purified liver enzyme
Sus scrofa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-3-hydroxy-3-methyl-5-oxovaleric acid + NADH
-
286553
Sus scrofa
(R)-3-hydroxy-3-methyl-5-hydroxyvaleric acid + NAD+
-
286553
Sus scrofa
-
(R)-3-hydroxy-3-methyl-5-oxovaleric acid + NADPH
-
286553
Sus scrofa
(R)-3-hydroxy-3-methyl-5-hydroxyvaleric acid + NADP+
-
286553
Sus scrofa
-
(S)-3-hydroxy-3-methyl-5-oxovaleric acid + NADH
-
286553
Sus scrofa
(S)-3-hydroxy-3-methyl-5-hydroxyvaleric acid + NAD+
-
286553
Sus scrofa
-
Other publictions for EC 1.1.1.32
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)
286553
Ngan
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Stereochemistry of the reactio ...
Sus scrofa
Bioorg. Chem.
4
166-180
1975
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286554
Schlesinger
Reduction of mevaldic acid to ...
Rattus norvegicus, Sus scrofa
J. Biol. Chem.
236
2421-2424
1961
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286555
Coon
-
The enzymic synthesis of branc ...
Sus scrofa
CIBA Symposium on the biosynthesis of terpenes and sterols (Wolstenholme, G. E. W. ; O. Conner, M. , eds)
62-72
1954
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