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Literature summary extracted from

  • Roeder, P.R.; Kohlhaw, G.B.
    alpha-Isopropylmalate synthase from yeast. A zinc metalloenzyme (1980), Biochim. Biophys. Acta, 613, 482-487.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.3.13 EDTA dialysis at an initial concentration of 50 mM reduces the zinc content by more than 80%, complete loss of activity, restored by addition of Zn2+, Mn2+, Fe2+, Co2+, or Cd2+ Saccharomyces cerevisiae
2.3.3.13 leucine
-
Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.3.13 additional information
-
additional information Km of enzyme with and without Zn2+ or Mn2+ Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.3.13 Zinc contains approximately 4 gatoms of zinc per dimer of 130000 Da Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
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 additional information
-
-
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 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.3.3.13 additional information
-
leucine Ki with and without Zn2+ or Mn2+ Saccharomyces cerevisiae