EC Number |
Application |
Reference |
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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 | 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 | 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 |
2.2.1.6 | synthesis |
overexpression of the als gene leads to high levels of 2,3-butanediol |
-, 736789 |
2.2.1.6 | synthesis |
the enzyme in Pyrococcus furiosus is a potential platform for the biological production of acetoin at temperatures in the 70-80°C range. Acetoin, or 3-hydroxybutanone, is an important four-carbon compound that serves as a building block for valuable bio-based chemical compounds and is a common flavor additive and preservative in the food industry |
734625 |
2.2.1.6 | synthesis |
transformation of a H+-ATPase defective strain with a C-terminal truncation of acetohydroxyacid synthase gene ilvBN results in increased valine production from 21.7 mM for wild-type to 46.7 mM and increase in the valine intermediate acetoin. Inserting acetohydroxyacid isomeroreductase gene into the ilvBN plasmid further increases valine producion |
696827 |