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Literature summary extracted from

  • Yu, M.J.; Wu, J.; Chen, S.L.
    Mechanism and inhibitor exploration with binuclear Mg ketol-acid reductoisomerase targeting the biosynthetic pathway of branched-chain amino acids (2020), ChemBioChem, 21, 381-391 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.86 hydroxy(methyl)propanedioic acid
-
 Staphylococcus aureus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.86 Mg2+ active site contains two divalent Mg2+ cations Staphylococcus aureus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.86 (2S)-2-acetolactate + NADPH Staphylococcus aureus
-
 (2R)-2,3-dihydroxyisovalerate + NADP+
-
 ?
1.1.1.86 (2S)-2-acetolactate + NADPH Staphylococcus aureus NCTC 8325
-
 (2R)-2,3-dihydroxyisovalerate + NADP+
-
 ?
1.1.1.86 (S)-2-acetolactate + NADPH + H+ Staphylococcus aureus
-
 (2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
-
 ?
1.1.1.86 (S)-2-acetolactate + NADPH + H+ Staphylococcus aureus NCTC 8325
-
 (2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.86 Staphylococcus aureus Q2FWK4
-
-
1.1.1.86 Staphylococcus aureus NCTC 8325 Q2FWK4
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.86 (2S)-2-acetolactate + NADPH
-
 Staphylococcus aureus (2R)-2,3-dihydroxyisovalerate + NADP+
-
 ?
1.1.1.86 (2S)-2-acetolactate + NADPH
-
 Staphylococcus aureus NCTC 8325 (2R)-2,3-dihydroxyisovalerate + NADP+
-
 ?
1.1.1.86 (2S)-2-acetolactate + NADPH + H+ the reaction includes the initial deprotonation of the substrate C2 hydroxy group, bridged by the two Mg2+ ions, alkyl migration from the C2-alkoxide carbon atom to the C3-carbon Staphylococcus aureus (2R)-2,3-dihydroxyisovalerate + NADP+
-
 ?
1.1.1.86 (2S)-2-acetolactate + NADPH + H+ the reaction includes the initial deprotonation of the substrate C2 hydroxy group, bridged by the two Mg2+ ions, alkyl migration from the C2-alkoxide carbon atom to the C3-carbon Staphylococcus aureus NCTC 8325 (2R)-2,3-dihydroxyisovalerate + NADP+
-
 ?
1.1.1.86 (S)-2-acetolactate + NADPH + H+
-
 Staphylococcus aureus (2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
-
 ?
1.1.1.86 (S)-2-acetolactate + NADPH + H+
-
 Staphylococcus aureus NCTC 8325 (2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
-
 ?
1.1.1.86 2-glutaryl lactic acid + NADPH
-
 Staphylococcus aureus ? + NADP+
-
 ?
1.1.1.86 2-glutaryl lactic acid + NADPH
-
 Staphylococcus aureus NCTC 8325 ? + NADP+
-
 ?
1.1.1.86 2-tribromomethyl acetolactic acid + NADPH
-
 Staphylococcus aureus ? + NADP+
-
 ?
1.1.1.86 2-tribromomethyl acetolactic acid + NADPH
-
 Staphylococcus aureus NCTC 8325 ? + NADP+
-
 ?
1.1.1.86 2-trichloromethyl acetolactic acid + NADPH
-
 Staphylococcus aureus ? + NADP+
-
 ?
1.1.1.86 2-trifluormethyl acetolactic acid + NADPH
-
 Staphylococcus aureus ? + NADP+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.86 KARI
-
 Staphylococcus aureus

General Information

EC Number General Information Comment Organism
1.1.1.86 drug target the enzyme is responsible for the second step of the biosynthesis of branched chain amino acids in plants and microorganisms and thus serves as a key inhibition target potentially without effects on mammals Staphylococcus aureus
1.1.1.86 metabolism the enzyme serves as a key inhibition target potentially without effects on mammals Staphylococcus aureus
1.1.1.86 physiological function the enzyme is responsible for the second step of the biosynthesis of branched chain amino acids in plants and microorganisms Staphylococcus aureus