Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli BL21 (DE3) | Corynebacterium glutamicum |
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 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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | the enzyme utilizes Mg2+ in the enzyme catalysis | Corynebacterium glutamicum |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
36100 | - |
SDS-PAGE | Corynebacterium glutamicum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium glutamicum | Q57179 | - |
- |
Corynebacterium glutamicum ATCC 13032 | Q57179 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Corynebacterium glutamicum |
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 | Comment | Organism |
---|---|---|
dimer | 2 * 36000, SDS-PAGE | Corynebacterium glutamicum |
Synonyms | Comment | Organism |
---|---|---|
KARI | - |
Corynebacterium glutamicum |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
- |
Corynebacterium glutamicum |
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 | 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 | Comment | Organism |
---|---|---|
metabolism | second enzyme in the branched-chain amino acid pathway | Corynebacterium glutamicum |
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 |