Cloning of the dihydroxyacid dehydratase-encoding gene (ILV3) from Saccharomyces cerevisiae
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Excessive by-product formation: A key contributor to low isobutanol yields of engineered Saccharomyces cerevisiae strains
2016, Metabolic Engineering CommunicationsCitation Excerpt :In vivo activity of the heterologous enzymes involved in the conversion of pyruvate to α-ketoisovalerate (KIV) via the pathway design described above was tested by complementation of S. cerevisiae mutants lacking key enzymes in the native branched-chain amino-acid biosynthesis pathway (Fig. 1). Consistent with earlier studies (Kingsbury and McCusker, 2010; Velasco et al., 1993; Zelenayatroitskaya et al., 1995) strains containing deletions of individual ‘catalytic’ genes IMK463 (ilv2Δ), IMK464 (ilv3Δ), IMK465 (ilv5Δ) did not grow on media lacking both valine and isoleucine (Fig. 2). In these strains, the presence of valine is sufficient to restore leucine synthesis since KIV formed by transamination of valine can feed leucine biosynthesis (Fig. 1).
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