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Literature summary extracted from

  • Blombach, B.; Hans, S.; Bathe, B.; Eikmanns, B.J.
    Acetohydroxyacid synthase, a novel target for improvement of L-lysine production by Corynebacterium glutamicum (2009), Appl. Environ. Microbiol., 75, 419-427.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.2.1.6 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

EC Number Protein Variants Comment Organism
2.2.1.6 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

EC Number Inhibitors Comment Organism Structure
2.2.1.6 L-isoleucine
-
 Corynebacterium glutamicum
2.2.1.6 L-leucine
-
 Corynebacterium glutamicum
2.2.1.6 L-valine
-
 Corynebacterium glutamicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.2.1.6 4.7
-
 pyruvate mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C Corynebacterium glutamicum
2.2.1.6 5.6
-
 2-oxobutanoate wild-type, pH 7.3, 37°C Corynebacterium glutamicum
2.2.1.6 6.9
-
 2-oxobutanoate mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C Corynebacterium glutamicum
2.2.1.6 7.8
-
 pyruvate wild-type, pH 7.3, 37°C Corynebacterium glutamicum
2.2.1.6 50
-
 pyruvate wild-type, pH 7.3, 37°C, presence of 10 mM L-valine Corynebacterium glutamicum
2.2.1.6 54
-
 pyruvate wild-type, pH 7.3, 37°C, presence of 10 mM L-isoleucine Corynebacterium glutamicum
2.2.1.6 65
-
 pyruvate wild-type, pH 7.3, 37°C, presence of 10 mM L-leucine Corynebacterium glutamicum
2.2.1.6 104
-
 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
2.2.1.6 104
-
 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
2.2.1.6 104
-
 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

EC Number Organism UniProt Comment Textmining
2.2.1.6 Corynebacterium glutamicum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.6 2-oxobutanoate + pyruvate
-
 Corynebacterium glutamicum 2-hydroxy-2-methyl-3-oxopentanoate + CO2
-
 ?
2.2.1.6 pyruvate
-
 Corynebacterium glutamicum 2-acetolactate + CO2
-
 ?

General Information

EC Number General Information Comment Organism
2.2.1.6 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