Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli or yeast | Saccharomyces cerevisiae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | - |
Saccharomyces cerevisiae | |
Ni2+ | - |
Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | the Km-value for NAD+ ranges from 0.054 mM to 0.15 mM when enzyme concentration varies from 0.008 mg/ml to 0.16 mg/ml, the Km-value for 3-isopropylmalate ranges from 0.023 mM to 0.042 mM when enzyme concentration varies from 0.008 mg/ml to 0.16 mg/ml | Saccharomyces cerevisiae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cd2+ | divalent cation required, Mn2+ and Cd2+ are about equally effective at 0.5 mM | Saccharomyces cerevisiae | |
Co2+ | divalent cations required 0.5 mM, Co2+ is 73% as effective as Mn2+ or Co2+ | Saccharomyces cerevisiae | |
Mg2+ | divalent cations required 0.5 mM Mg2+ is 62% as effective as Mn2+ or Co2+ | Saccharomyces cerevisiae | |
Mn2+ | divalent cation required, Mn2+ and Cd2+ are about equally effective at 0.5 mM | Saccharomyces cerevisiae |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
39085 | - |
1 * 39085, enzyme exists in a dynamic monomer-dimer equilibrium, calculation from nucleotide sequence | Saccharomyces cerevisiae |
39085 | - |
2 * 39085, enzyme exists in a dynamic monomer-dimer equilibrium, calculation from nucleotide sequence | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2R,3S)-3-isopropylmalate + NAD+ | Saccharomyces cerevisiae | the enzyme catalyzes the third pathway-specific reaction in the biosynthesis of leucine | 2-oxoisocaproate + NADH + H+ + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Saccharomyces cerevisiae |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
18.4 | - |
- |
Saccharomyces cerevisiae |
Storage Stability | Organism |
---|---|
20-23°C, 0.1 M potassium phosphate buffer, pH 6.9, 1.5 mM ammonium sulfate, 20% v/v glycerol, 0.03% NaN3, stable for 2 weeks, thereafter gradual loss of activity | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2R,3S)-3-isopropylmalate + NAD+ | - |
Saccharomyces cerevisiae | 2-oxoisocaproate + NADH + H+ + CO2 | - |
? | |
(2R,3S)-3-isopropylmalate + NAD+ | the enzyme catalyzes the third pathway-specific reaction in the biosynthesis of leucine | Saccharomyces cerevisiae | 2-oxoisocaproate + NADH + H+ + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 43000-45000, enzyme exists in a dynamic monomer-dimer equilibrium, SDS-PAGE | Saccharomyces cerevisiae |
dimer | 2 * 39085, enzyme exists in a dynamic monomer-dimer equilibrium, calculation from nucleotide sequence | Saccharomyces cerevisiae |
monomer | 1 * 39085, enzyme exists in a dynamic monomer-dimer equilibrium, calculation from nucleotide sequence | Saccharomyces cerevisiae |
monomer | 1 * 43000-45000, enzyme exists in a dynamic monomer-dimer equilibrium, SDS-PAGE | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.9 | 10.1 | - |
Saccharomyces cerevisiae |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
8 | 10.1 | pH 8.0: 75% of maximal activity, pH 8.9-10.1: optimum | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | specific for NAD+, activity drops to less than 5% when NADP+ is substituted for NAD+ | Saccharomyces cerevisiae |