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- W341719741 abstract "ABSTRACT In yeast, the three enzymes specifically involved in leucine biosynthesis are found in two intracellular compartments. α-Isopropylmalate (α-IPM) synthesis is associated with the mitochondria, whereas IPM isomerase and β-IPM dehydrogenase are cytosolic. Regulation occurs at the level of both enzyme activity and enzyme synthesis. α-IPM synthase is subject to at least two controls of its activity, namely feedback inhibition by leucine and inactivation by CoA. The CoA-mediated inactivation apparently links the biosynthesis of leucine to the availability of acetyl-CoA and can be reversed or prevented by ATP. The synthesis of α-IPM synthase appears to be under the “general control” of amino acid biosynthesis. The specific activities of all three leucine pathway enzymes are lowered when cells are grown in the presence of leucine and threonine. This repression effect was studied more closely with β-IPM dehydrogenase, the LEU2 gene product. Our results indicate that the expression of the LEU2 gene is controlled at the transcriptional level. Repression is unchanged with a strain in which LEU2 has been transposed from its original position on chromosomes III to chromosome XII (experiments done in cooperation with T. Petes, Univ. of Chicago). We conclude that the recombinant plasmid used for transformation carries specific regulatory information in addition to LEU2 structural information. KEYWORDS Subcellular distribution; mitochondria; feedback inhibition; CoA inactivation; repression; LEU2 gene control; transposed LEU2 gene." @default.
- W341719741 created "2016-06-24" @default.
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- W341719741 date "1981-01-01" @default.
- W341719741 modified "2023-09-28" @default.
- W341719741 title "REGULATION OF LEUCINE BIOSYNTHESIS IN SACCHAROMYCES CEREVTSIAE" @default.
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- W341719741 doi "https://doi.org/10.1016/b978-0-08-025382-4.50036-8" @default.
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