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- W271990168 abstract "Abstract a- Isopropylmalate synthase activity was demonstrated in the Sephadex G 25 gel filtrated crude extracts of one yeast and 43 bacterial strains belonging to 14 families. The enzyme was inhibited by leucine from all strains Bacteroides fragilis, Clostridia and several phototropic bacteria. The enzyme was inhibited by leucine from all strains investigated. In crude extracts of 17 species (8 genera) the leucine-mediated inhibition could be relieved by the addition of valine or isoleucine , but not by the addition of threonine or alanine. The enzymes from 11 species (7 genera) were inhibited by 1 mM valine and isoleucine, whereas the enzyme activity from 5 bacteria (4genera) were not so affected. These results suggest that valine and isoleucine are specifically involved in the regulation of leucine biosynthesis in several bacteria. The affect of valine and isoleucine on the IPM-synthase activity from mycobacteria and Corynebacterium autotrophicum lends support to the reclassification of Mycobacterium flavum 301 to C. autotrophicum . The antagonism between 5′,5′,5′-trifluoroleucine and amino acids and a- ketoisovalerate was a- isopropylmalate synthase in the presence or abssence of leucine and the reversal of the 5′,5′,5′-trifluoroleucine-mediated growth inhibition by these amino acids." @default.
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- W271990168 date "1977-01-01" @default.
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- W271990168 title "Leucine biosynthesis: effect of branched-chain amino acids and threonine on synthase activity from aerobic and anaerobic microorganisms" @default.
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- W271990168 doi "https://doi.org/10.1016/0305-1978(77)90001-1" @default.
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