Application | Comment | Organism |
---|---|---|
synthesis | construction of a mutant with a deleted C-terminal domain in the regulatory subunit IlvN. The constructed enzyme shows altered kinetic properties, i.e., an about twofold-lower Km for the substrate pyruvate and an about fourfold-lower Vmax, a slightly increased Km for the substrate alpha-ketobutyrate with an about twofold-lower Vmax, and insensitivity against the inhibitors L-valine, L-isoleucine, and L-leucine. Introduction of the mutant into the L-lysine producers Corynebacterium glutamicum DM1729 and DM1933 increases L-lysine formation by 43% and 36%, respectively. Complete inactivation of the AHAS in Corynebacterium glutamicum DM1729 and DM1933 by deletion of the ilvB gene, encoding the catalytic subunit of AHAS, leads to L-valine, L-isoleucine, and L-leucine auxotrophy and to further-improved L-lysine production. In batch fermentations, the mutant produces about 85% more L-lysine and shows an 85%-higher substrate-specific product yield | Corynebacterium glutamicum |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of a mutant with a deleted C-terminal domain in the regulatory subunit IlvN. The constructed enzyme shows altered kinetic properties, i.e., an about twofold-lower Km for the substrate pyruvate and an about fourfold-lower Vmax, a slightly increased Km for the substrate alpha-ketobutyrate with an about twofold-lower Vmax, and insensitivity against the inhibitors L-valine, L-isoleucine, and L-leucine. Introduction of the mutant into the L-lysine producers Corynebacterium glutamicum DM1729 and DM1933 increases L-lysine formation by 43% and 36%, respectively. Complete inactivation of the AHAS in Corynebacterium glutamicum DM1729 and DM1933 by deletion of the ilvB gene, encoding the catalytic subunit of AHAS, leads to L-valine, L-isoleucine, and L-leucine auxotrophy and to further-improved L-lysine production. In batch fermentations, the mutant produces about 85% more L-lysine and shows an 85%-higher substrate-specific product yield | Corynebacterium glutamicum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-isoleucine | - |
Corynebacterium glutamicum | |
L-leucine | - |
Corynebacterium glutamicum | |
L-valine | - |
Corynebacterium glutamicum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
4.7 | - |
pyruvate | mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C | Corynebacterium glutamicum | |
5.6 | - |
2-oxobutanoate | wild-type, pH 7.3, 37°C | Corynebacterium glutamicum | |
6.9 | - |
2-oxobutanoate | mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C | Corynebacterium glutamicum | |
7.8 | - |
pyruvate | wild-type, pH 7.3, 37°C | Corynebacterium glutamicum | |
50 | - |
pyruvate | wild-type, pH 7.3, 37°C, presence of 10 mM L-valine | Corynebacterium glutamicum | |
54 | - |
pyruvate | wild-type, pH 7.3, 37°C, presence of 10 mM L-isoleucine | Corynebacterium glutamicum | |
65 | - |
pyruvate | wild-type, pH 7.3, 37°C, presence of 10 mM L-leucine | Corynebacterium glutamicum | |
104 | - |
pyruvate | mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C, presence of 10 mM L-isoleucine | Corynebacterium glutamicum | |
104 | - |
pyruvate | mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C, presence of 10 mM L-leucine | Corynebacterium glutamicum | |
104 | - |
pyruvate | mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C, presence of 10 mM L-valine | Corynebacterium glutamicum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium glutamicum | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxobutanoate + pyruvate | - |
Corynebacterium glutamicum | 2-hydroxy-2-methyl-3-oxopentanoate + CO2 | - |
? | |
pyruvate | - |
Corynebacterium glutamicum | 2-acetolactate + CO2 | - |
? |
General Information | Comment | Organism |
---|---|---|
physiological function | complete inactivation of the acetolactate synthase in Corynebacterium glutamicum DM1729 and DM1933 by deletion of the ilvB gene, encoding the catalytic subunit, leads to L-valine, L-isoleucine, and L-leucine auxotrophy and to improved L-lysine production | Corynebacterium glutamicum |