EC Number |
Application |
Reference |
---|
2.2.1.6 | drug development |
acetohydroxyacid synthase (AHAS) of Mycobacterium tuberculosis is a promising target for the development of anti-tuberculosis agents |
-, 733745 |
2.2.1.6 | synthesis |
acetoin (i.e. 3-hydroxybutanone), is a major product at temperatures below 80 °C. Acetolactate synthase ALS, which is involved in branched-chain amino acid biosynthesis, is responsible and deletion of the Als gene abolishes acetoin production. Deletion of Als in a strain of Pyrococcus furiosus heterologously expressing an alcohol dehydrogenase gene from Thermoanaerobacter sp. X514 for ethanol production significantly improves the yield of ethanol |
734625 |
2.2.1.6 | drug development |
AHAS is the target of the sulfonylurea and imidazolinone herbicides |
677228 |
2.2.1.6 | pharmacology |
AHAS might be a target protein for the development of anti-tuberculosis therapeutics |
-, 673626 |
2.2.1.6 | synthesis |
Bacillus subtilis acetolactate synthase can act as key biocatalyst in the formation of isobutanol which is deemed to be a next-generation biofuel and a renewable platform chemical. The enzyme AlsS catalyzes the conversion of 2-ketoisovalerate into isobutyraldehyde, the immediate precursor of isobutanol |
-, 733658 |
2.2.1.6 | synthesis |
co-expression of acetolactate synthase and omega-transaminase in Escherichia coli as a whole-cell biocatalyst for production of (S)-alpha-benzylamine. Product (S)-alpha-benzylamine can be moved into the extraction solution via an organic solvent |
696828 |
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 |
695780 |
2.2.1.6 | biotechnology |
construction of a vector system for chloroplast transformation with acetolactate synthase, generation of a series of Arabidopsis thaliana mutated acetolactate synthase genes and introduction of constructs with the aminoglycoside 3'-adenyltransferase gene into the Nicotiana tabacum chloroplast genome by particle bombardment |
700807 |
2.2.1.6 | synthesis |
construction of isobutanol production systems by overexpression of effective 2-oxoacid decarboxylase KivD and combinatorial overexpression of valine biosynthetic enzymes in Saccharomyces cerevisiae D452-2. Isobutanol production by the engineered strain is assessed in micro-aerobic batch fermentations using glucose as a sole carbon source, leading to production of 93 mg/l isobutanol, which corresponds to a fourfold improvement as compared with the control strain. Isobutanol production is further enhanced to 151 mg/l by additional overexpression of acetolactate synthase Ilv2p, acetohydroxyacid reductoisomerase Ilv5p, and dihydroxyacid dehydratase Ilv3p in the cytosol |
735780 |
2.2.1.6 | synthesis |
engineering of the wild type of Corynebacterium glutamicum for the growth-decoupled production of 2-ketoisovalerate from glucose by deletion of the aceE gene encoding the E1p subunit of the pyruvate dehydrogenase complex, deletion of the transaminase B gene ilvE, and additional overexpression of the ilvBNCD genes, encoding the L-valine biosynthetic enzymes acetohydroxyacid synthase (AHAS), acetohydroxyacid isomeroreductase, and dihydroxyacid dehydratase. 2-Ketoisovalerate production is further improved by deletion of the pyruvate:quinone oxidoreductase gene pqo. In fed-batch fermentations at high cell densities, the newly constructed strains produce up to 188 mM (21.8 g/liter) 2-ketoisovalerate and showd a product yield of about 0.47 mol per mol (0.3 g/g) of glucose and a volumetric productivity of about 4.6 mM (0.53 g/liter) 2-ketoisovalerate per h in the overall production phase |
-, 713840 |