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Literature summary extracted from

  • Ulm, E.H.; Boehme, R.; Kohlhaw, G.
    alpha-Isopropylmalate synthase from yeast: purification, kinetic studies and effect of ligands on stability (1972), J. Bacteriol., 110, 1118-1126.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.3.13 5',5',5'-trifluoroleucine
-
Saccharomyces cerevisiae
2.3.3.13 CoA
-
Saccharomyces cerevisiae
2.3.3.13 D-leucine amide weak Saccharomyces cerevisiae
2.3.3.13 L-2-Hydroxyisopentanoate
-
Saccharomyces cerevisiae
2.3.3.13 leucine both Fe2+ and Co2+ lower the inhibition by Leu; D-Leu, weak; mixed-type inhibition, strongly pH-dependent, Leu concentration necessary for half-maximal inhibition increases about 10fold as the pH increases from 7.5 to 8.5 Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.3.13 0.009
-
acetyl-CoA
-
Saccharomyces cerevisiae
2.3.3.13 0.016
-
2-oxo-3-methylbutanoate
-
Saccharomyces cerevisiae
2.3.3.13 0.57
-
2-oxobutanoate
-
Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.3.13 K+ required Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.3.13 121000
-
in absence of Leu, gel filtration Saccharomyces cerevisiae
2.3.3.13 137000
-
in presence of substrate, gel filtration Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.3.13 2-oxo-3-methylbutanoate + acetyl-CoA + H2O Saccharomyces cerevisiae first enzyme in biosynthesis of L-Leu ?
-
?
2.3.3.13 2-oxo-3-methylbutanoate + acetyl-CoA + H2O Saccharomyces cerevisiae 60615 first enzyme in biosynthesis of L-Leu ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.3.3.13 Saccharomyces cerevisiae
-
-
-
2.3.3.13 Saccharomyces cerevisiae 60615
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.3.13
-
Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.3.13 1.58
-
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.3.13 2-oxo-3-methylbutanoate + acetyl-CoA + H2O
-
Saccharomyces cerevisiae 3-hydroxy-4-methyl-3-carboxypentanoate + CoA i.e. alpha-isopropylmalate ?
2.3.3.13 2-oxo-3-methylbutanoate + acetyl-CoA + H2O
-
Saccharomyces cerevisiae 60615 3-hydroxy-4-methyl-3-carboxypentanoate + CoA i.e. alpha-isopropylmalate ?
2.3.3.13 2-oxo-3-methylbutanoate + acetyl-CoA + H2O first enzyme in biosynthesis of L-Leu Saccharomyces cerevisiae ?
-
?
2.3.3.13 2-oxo-3-methylbutanoate + acetyl-CoA + H2O first enzyme in biosynthesis of L-Leu Saccharomyces cerevisiae 60615 ?
-
?
2.3.3.13 2-oxo-butanoate + acetyl-CoA + H2O
-
Saccharomyces cerevisiae 2-ethyl-2-hydroxysuccinic acid + CoA
-
?
2.3.3.13 2-oxo-butanoate + acetyl-CoA + H2O
-
Saccharomyces cerevisiae 60615 2-ethyl-2-hydroxysuccinic acid + CoA
-
?
2.3.3.13 pyruvate + acetyl-CoA + H2O
-
Saccharomyces cerevisiae 2-hydroxy-2-methylsuccinic acid + CoA
-
?
2.3.3.13 pyruvate + acetyl-CoA + H2O
-
Saccharomyces cerevisiae 60615 2-hydroxy-2-methylsuccinic acid + CoA
-
?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.3.13 additional information
-
Leu, and to a lesser extent, 2-oxo-3-methylbutanoate stabilize against heat inactivation, acetyl-CoA accelerates inactivation Saccharomyces cerevisiae
2.3.3.13 50
-
pH 6.9, 5 min, 80% loss of activity, 1 mM Leu provides significant but incomplete protection Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.3.13 8
-
-
Saccharomyces cerevisiae