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Elimination of biosynthetic pathways for l-valine and l-isoleucine in mitochondria enhances isobutanol production in engineered Saccharomyces cerevisiae.

08:00 EDT 31st July 2018 | BioPortfolio

Summary of "Elimination of biosynthetic pathways for l-valine and l-isoleucine in mitochondria enhances isobutanol production in engineered Saccharomyces cerevisiae."

Saccharomyces cerevisiae has a natural ability to produce higher alcohols, making it a promising candidate for production of isobutanol. However, the several pathways competing with isobutanol biosynthesis lead to production of substantial amounts of l-valine and l-isoleucine in mitochondria and isobutyrate, l-leucine, and ethanol in cytosol. To increase flux to isobutanol by removing by-product formation, the genes associated with formation of l-valine (BAT1), l-isoleucine (ILV1), isobutyrate (ALD6), l-leucine (LEU1), and ethanol (ADH1) were disrupted to construct the S. cerevisiae WΔGBIALA1_2vec strain. This strain showed 8.9 and 8.6 folds increases in isobutanol concentration and yield, respectively, relative the corresponding values of the background strain on glucose medium. In a bioreactor fermentation with a gas trapping system, the WΔGBIALA1_2vec strain produced 662 mg/L isobutanol concentration with a yield of 6.71 mg/g. With elimination of the competing pathways, the WΔGBIALA1_2vec strain would serve as a platform strain for isobutanol production.

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This article was published in the following journal.

Name: Bioresource technology
ISSN: 1873-2976
Pages: 271-277

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Medical and Biotech [MESH] Definitions

An enzyme that plays a role in the VALINE; LEUCINE; and ISOLEUCINE catabolic pathways by catalyzing the oxidation of 2-methyl-3-oxopropanate to propanoyl-CoA using NAD+ as a coenzyme. Methylmalonate semialdehyde dehydrogenase deficiency is characterized by elevated BETA-ALANINE and 3-hydropropionic acid.

An NAD+ dependent enzyme that catalyzes the oxidation 3-methyl-2-oxobutanoate to 2-methylpropanoyl-CoA. It plays a role in the degradation of VALINE; LEUCINE; and ISOLEUCINE.

An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. It is involved in the biosynthesis of VALINE; LEUCINE; and ISOLEUCINE.

A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.

An enzyme that catalyzes the oxidation of (R)-2,3-dihydroxy-3-methylbutanoate to (S)-2-hydroxy-2-methyl-3-oxobutanoate in the presence of NADP. It is involved in the biosynthesis of VALINE; LEUCINE; ISOLEUCINE; pentothenate and COENZYME A. This enzyme was formerly classified as EC 1.1.1.89.

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