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Literature summary for 1.1.1.86 extracted from

  • Lee, D.; Hong, J.; Kim, K.J.
    Crystal structure and biochemical characterization of ketol-acid reductoisomerase from Corynebacterium glutamicum (2019), J. Agric. Food Chem., 67, 8527-8535 .
    View publication on PubMed
Search for more literature for 1.1.1.86

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 (DE3) Corynebacterium glutamicum

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor-diffusion method at 20°C, crystal structure in complex with NADP+ and two Mg2+ ions at 2.6 A resolution Corynebacterium glutamicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.022
-
 NADPH pH 8.0, 22°C Corynebacterium glutamicum
0.05
-
 NADH pH 8.0, 22°C Corynebacterium glutamicum
2.16
-
 (2S)-2-acetolactate pH 8.0, 22°C Corynebacterium glutamicum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the enzyme utilizes Mg2+ in the enzyme catalysis Corynebacterium glutamicum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36100
-
 SDS-PAGE Corynebacterium glutamicum

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum Q57179
-
-
Corynebacterium glutamicum ATCC 13032 Q57179
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Corynebacterium glutamicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2S)-2-aceto-2-hydroxybutyrate + NADPH + H+
-
 Corynebacterium glutamicum (R)-2,3-dihydroxy-3-methylvalerate + NADP+
-
 ?
(2S)-2-aceto-2-hydroxybutyrate + NADPH + H+
-
 Corynebacterium glutamicum ATCC 13032 (R)-2,3-dihydroxy-3-methylvalerate + NADP+
-
 ?
(2S)-2-acetolactate + NADH + H+ the enzyme prefers NADPH as a cofactor rather than NADH. kcat/Km for NADPH is 322fold higher than kcat/KM for NADH Corynebacterium glutamicum (R)-2,3-dihydroxyisovalerate + NAD+
-
 ?
(2S)-2-acetolactate + NADH + H+ the enzyme prefers NADPH as a cofactor rather than NADH. kcat/Km for NADPH is 322fold higher than kcat/KM for NADH Corynebacterium glutamicum ATCC 13032 (R)-2,3-dihydroxyisovalerate + NAD+
-
 ?
(2S)-2-acetolactate + NADPH + H+ the enzyme prefers NADPH as a cofactor rather than NADH. kcat/Km for NADPH is 322fold higher than kcat/KM for NADH Corynebacterium glutamicum (R)-2,3-dihydroxyisovalerate + NADP+
-
 ?
(2S)-2-acetolactate + NADPH + H+ the enzyme prefers NADPH as a cofactor rather than NADH. kcat/Km for NADPH is 322fold higher than kcat/KM for NADH Corynebacterium glutamicum ATCC 13032 (R)-2,3-dihydroxyisovalerate + NADP+
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 36000, SDS-PAGE Corynebacterium glutamicum

Synonyms

Synonyms Comment Organism
KARI
-
 Corynebacterium glutamicum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0027
-
 NADH pH 8.0, 22°C Corynebacterium glutamicum
0.228
-
 NADPH pH 8.0, 22°C Corynebacterium glutamicum
0.235
-
 (2S)-2-acetolactate pH 8.0, 22°C Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Corynebacterium glutamicum

pH Range

pH Minimum pH Maximum Comment Organism
7 10 pH 7.0: 87% of maximal activity, pH 10.0: 61% of maximal activity Corynebacterium glutamicum

Cofactor

Cofactor Comment Organism Structure
NADPH the enzyme prefers NADPH as a cofactor rather than NADH. kcat/Km for NADPH is 322fold higher than kcat/KM for NADH Corynebacterium glutamicum

General Information

General Information Comment Organism
metabolism second enzyme in the branched-chain amino acid pathway Corynebacterium glutamicum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.054
-
 NADH pH 8.0, 22°C Corynebacterium glutamicum
0.11
-
 (2S)-2-acetolactate pH 8.0, 22°C Corynebacterium glutamicum
10.36
-
 NADPH pH 8.0, 22°C Corynebacterium glutamicum