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Literature summary for 1.1.1.86 extracted from

  • Mrachko, G.T.; Chunduru, S.K.; Calvo, K.C.
    The pH dependence of the kinetic parameters of ketol acid reductoisomerase indicates a proton shuttle mechanism for alkyl migration (1992), Arch. Biochem. Biophys., 294, 446-453.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2-Methyllactate competitive Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli
Mg2+ Km: 0.4 mM, pH 8.5 Escherichia coli
Mg2+ Km: 0.35 mM, pH 10, reaction with acetolactate Escherichia coli
Mg2+ Km: 0.45 mM, pH 6.7, reaction with acetolactate Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-acetolactate + NADPH Escherichia coli enzyme of branched chain amino acid synthesis 2,3-dihydroxy-3-methylbutanoate + NADP+
-
r
2-acetolactate + NADPH Escherichia coli second common reaction in the biosynthesis of the branched chain amino acids 2,3-dihydroxy-3-methylbutanoate + NADP+
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-acetolactate + NADPH enzyme of branched chain amino acid synthesis Escherichia coli 2,3-dihydroxy-3-methylbutanoate + NADP+
-
r
2-acetolactate + NADPH second common reaction in the biosynthesis of the branched chain amino acids Escherichia coli 2,3-dihydroxy-3-methylbutanoate + NADP+
-
r
acetolactate + NADPH + H+
-
Escherichia coli 2,3-dihydroxy-2-methylbutanoate + NADP+
-
r
NADPH + 2-acetolactate
-
Escherichia coli NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
?

pH Stability

pH Stability pH Stability Maximum Comment Organism
10
-
rapid loss of activity above pH 10 with 2-acetolactate as substrate Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Escherichia coli