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Literature summary for 1.1.1.85 extracted from

  • Kohlhaw, G.B.
    beta-Isopropylmalate dehydrogenase from yeast (1988), Methods Enzymol., 166, 429-435.
    View publication on PubMed
Search for more literature for 1.1.1.85

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli or yeast Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
 Saccharomyces cerevisiae
Ni2+
-
 Saccharomyces cerevisiae

KM Value [mM]

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

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 [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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
18.4
-
-
 Saccharomyces cerevisiae

Storage Stability

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 and Products (Substrate)

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

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.9 10.1
-
 Saccharomyces cerevisiae

pH Range

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

Cofactor Comment Organism Structure
NAD+ specific for NAD+, activity drops to less than 5% when NADP+ is substituted for NAD+ Saccharomyces cerevisiae