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Literature summary for 2.3.3.13 extracted from

  • Hampsey, D.M.; Kohlhaw, G.B.
    Inactivation of yeast alpha-isopropylmalate synthase by CoA. Antagonism between CoA and adenylates and the mechanism of CoA inactivation (1981), J. Biol. Chem., 256, 3791-3796.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
CoA in presence of Zn2+, protection by high concentrations of ATP, and to a much lesser extent, ADP, by a high adenylate charge, by chelators, and by 3'-dephospho-CoA Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-oxo-3-methylbutanoate + acetyl-CoA + H2O Saccharomyces cerevisiae first enzyme in biosynthesis of L-Leu ?
-
?
2-oxo-3-methylbutanoate + acetyl-CoA + H2O Saccharomyces cerevisiae SK101 first enzyme in biosynthesis of L-Leu ?
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae SK101
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxo-3-methylbutanoate + acetyl-CoA + H2O
-
Saccharomyces cerevisiae 3-hydroxy-4-methyl-3-carboxypentanoate + CoA i.e. alpha-isopropylmalate ?
2-oxo-3-methylbutanoate + acetyl-CoA + H2O
-
Saccharomyces cerevisiae SK101 3-hydroxy-4-methyl-3-carboxypentanoate + CoA i.e. alpha-isopropylmalate ?
2-oxo-3-methylbutanoate + acetyl-CoA + H2O first enzyme in biosynthesis of L-Leu Saccharomyces cerevisiae ?
-
?
2-oxo-3-methylbutanoate + acetyl-CoA + H2O first enzyme in biosynthesis of L-Leu Saccharomyces cerevisiae SK101 ?
-
?