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Literature summary extracted from

  • Patel, K.M.; Teran, D.; Zheng, S.; Kandale, A.; Garcia, M.; Lv, Y.; Schembri, M.A.; McGeary, R.P.; Schenk, G.; Guddat, L.W.
    Crystal structures of Staphylococcus aureus ketol-acid reductoisomerase in complex with two transition state analogues that have biocidal activity (2017), Chemistry, 23, 18289-18295 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.86 expressed in Escherichia coli BL21 cells Staphylococcus aureus
1.1.1.86 expression in Escherichia coli BL21 cells Staphylococcus aureus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.86 crystal structures of the enzyme in complex with two transition state analogues, cyclopropane-1,1-dicarboxylate and N-isopropyloxalyl hydroxamate. Hanging-drop vapor-diffusion method Staphylococcus aureus
1.1.1.86 hanging-drop vapor-diffusion method. Crystal structures of Staphylococcus aureus KARI in complex with two transition state analogues, cyclopropane-1,1-dicarboxylate and N-isopropyloxalyl hydroxamate Staphylococcus aureus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.86 cyclopropane-1,1-dicarboxylate binds in a competitively and in multi-dentate manner to the enzyme; the compounds bind competitively and in multi-dentate manner to the enzyme Staphylococcus aureus
1.1.1.86 N-isopropyloxalyl hydroxamate binds slowly to the enzyme, binds in a competitively and in multi-dentate manner to the enzyme. The observation that the inhibitor is processed to its deoxygenated form in crystallo provides an alternative explanation for the relatively weak herbicidal/antimicrobial activity affordsed by N-isopropyloxalyl hydroxamate despite its low Ki value; the compounds bind competitively and in multi-dentate manner to the enzyme. Binds slowly to the enzyme. Intact N-isopropyloxalyl hydroxamate is present in only 25% of binding sites, whereas its deoxygenated form is present in the remaining sites. This deoxy form of N-isopropyloxalyl hydroxamate binds rapidly to the enzyme, but with much weaker affinity (Ki: 0.021 mM) Staphylococcus aureus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.86 0.285
-
 (S)-2-acetolactate pH 8.0, 25°C Staphylococcus aureus
1.1.1.86 0.285
-
 (2S)-2-acetolactate pH 8.0, 25°C Staphylococcus aureus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.86 Mg2+ Mg2+-dependent enzyme 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 (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-acetolactate + NADPH + H+ Staphylococcus aureus
-
 3-hydroxy-3-methyl-2-oxobutyrate + NADP+
-
 ?
1.1.1.86 2-acetolactate + NADPH + H+ Staphylococcus aureus NCTC 8325
-
 3-hydroxy-3-methyl-2-oxobutyrate + NADP+
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.86
-
 Staphylococcus aureus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.86 (2S)-2-acetolactate + NADPH + H+
-
 Staphylococcus aureus 3-hydroxy-3-methyl-2-oxobutyrate + NADP+
-
 ?
1.1.1.86 (2S)-2-acetolactate + NADPH + H+
-
 Staphylococcus aureus NCTC 8325 3-hydroxy-3-methyl-2-oxobutyrate + 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-acetolactate + NADPH + H+
-
 Staphylococcus aureus 3-hydroxy-3-methyl-2-oxobutyrate + NADP+
-
 ?
1.1.1.86 2-acetolactate + NADPH + H+
-
 Staphylococcus aureus NCTC 8325 3-hydroxy-3-methyl-2-oxobutyrate + NADP+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.86 KARI
-
 Staphylococcus aureus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.86 0.00023
-
 (S)-2-acetolactate pH 8.0, 25°C Staphylococcus aureus
1.1.1.86 0.00023
-
 (2S)-2-acetolactate pH 8.0, 25°C Staphylococcus aureus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.86 NADPH
-
 Staphylococcus aureus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.1.86 0.0000079
-
 N-isopropyloxalyl hydroxamate pH 8.0, 25°C Staphylococcus aureus
1.1.1.86 0.0000079
-
 N-isopropyloxalyl hydroxamate pH 8.0, 25°C, intact N-isopropyloxalyl hydroxamate is present in only 25% of binding sites, whereas its deoxygenated form is present in the remaining sites. This deoxy form of N-isopropyloxalyl hydroxamate binds rapidly to the enzyme, but with much weaker affinity (Ki: 0.021 mM) Staphylococcus aureus
1.1.1.86 0.00273
-
 cyclopropane-1,1-dicarboxylate pH 8.0, 25°C Staphylococcus aureus
1.1.1.86 0.00277
-
 cyclopropane-1,1-dicarboxylate pH 8.0, 25°C Staphylococcus aureus