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Literature summary extracted from
- Crystal structure and biochemical characterization of ketol-acid reductoisomerase from Corynebacterium glutamicum (2019), J. Agric. Food Chem., 67, 8527-8535 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.1.1.86 | expression in Escherichia coli BL21 (DE3) | Corynebacterium glutamicum |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.1.1.86 | 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]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.86 | 0.022 | - |
NADPH | pH 8.0, 22°C | Corynebacterium glutamicum |  |
| 1.1.1.86 | 0.05 | - |
NADH | pH 8.0, 22°C | Corynebacterium glutamicum | |
| 1.1.1.86 | 2.16 | - |
(2S)-2-acetolactate | pH 8.0, 22°C | Corynebacterium glutamicum |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.86 | Mg2+ | the enzyme utilizes Mg2+ in the enzyme catalysis | Corynebacterium glutamicum | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.86 | 36100 | - |
SDS-PAGE | Corynebacterium glutamicum |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.1.86 | Corynebacterium glutamicum | Q57179 | - |
- |
| 1.1.1.86 | Corynebacterium glutamicum ATCC 13032 | Q57179 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.1.1.86 | - |
Corynebacterium glutamicum |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.86 | (2S)-2-aceto-2-hydroxybutyrate + NADPH + H+ | - |
Corynebacterium glutamicum | (R)-2,3-dihydroxy-3-methylvalerate + NADP+ | - |
? | |
| 1.1.1.86 | (2S)-2-aceto-2-hydroxybutyrate + NADPH + H+ | - |
Corynebacterium glutamicum ATCC 13032 | (R)-2,3-dihydroxy-3-methylvalerate + NADP+ | - |
? | |
| 1.1.1.86 | (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+ | - |
? | |
| 1.1.1.86 | (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+ | - |
? | |
| 1.1.1.86 | (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+ | - |
? | |
| 1.1.1.86 | (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
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.1.1.86 | dimer | 2 * 36000, SDS-PAGE | Corynebacterium glutamicum |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.1.86 | KARI | - |
Corynebacterium glutamicum |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.86 | 0.0027 | - |
NADH | pH 8.0, 22°C | Corynebacterium glutamicum | |
| 1.1.1.86 | 0.228 | - |
NADPH | pH 8.0, 22°C | Corynebacterium glutamicum | |
| 1.1.1.86 | 0.235 | - |
(2S)-2-acetolactate | pH 8.0, 22°C | Corynebacterium glutamicum |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.86 | 8 | - |
- |
Corynebacterium glutamicum |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.86 | 7 | 10 | pH 7.0: 87% of maximal activity, pH 10.0: 61% of maximal activity | Corynebacterium glutamicum |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.86 | 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
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.1.1.86 | metabolism | second enzyme in the branched-chain amino acid pathway | Corynebacterium glutamicum |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.86 | 0.054 | - |
NADH | pH 8.0, 22°C | Corynebacterium glutamicum | |
| 1.1.1.86 | 0.11 | - |
(2S)-2-acetolactate | pH 8.0, 22°C | Corynebacterium glutamicum | |
| 1.1.1.86 | 10.36 | - |
NADPH | pH 8.0, 22°C | Corynebacterium glutamicum | |
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Release 2023.1 (January 2023)
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