Tobias Bartek

TL;DR: A second generation of high-yield L-valine producers was constructed by successive deletion of the genes encoding pyruvate:quinone oxidoreductase, phosphoglucose isomerase, and pyruVate carboxylase and overexpression of ilvBNCE.

TL;DR: Corynebacterium glutamicum was engineered for the production of l-valine from glucose by deletion of the aceE gene encoding the E1p enzyme of the pyruvate dehydrogenase complex and additional overexpression of the ilvBNCE genes encoding the l-Valine biosynthetic enzymes acetohydroxyacid synthase, isomeroreductase, and transaminase B.

TL;DR: Three different optimal routes for L‐Valine biosynthesis were identified by elementary mode (EM) analysis, substantiating that the cofactor supply may be crucial for efficient L‐valine production.

TL;DR: Transhydrogenase activity offers an alternative perspective for sufficient NADPH supply, which is relevant for most amino acid production systems, as demonstrated for l-valine, this bypass leads to a significant increase of product yield due to a concurrent reduction in carbon dioxide formation via the PPP.

TL;DR: The effect of different amounts of supplemented l-isoleucine and pantothenate has been analysed with the auxotrophic strain Corynebacterium glutamicumΔilvAΔpanB, showing that the final biomass concentration of this preliminary l-valine production strain can be controlled by the amount of added l- isoleucines.