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203 109 109 1 2 Norbert Obermeier Karl Poralla Lehrbereich Mikrobiologie I Institut für Biologie II der Universität Auf der Morgenstelle 28 D-7400 Tübingen 1 Germany Abstract Mutants of Bacillus subtilis constitutive for L -leucine dehydrogenase synthesis were selected. Using these mutants we could determine two functional roles for the L -leucine dehydrogenase. This enzyme liberates ammonium ions from branched chain amino acids when supplied as the sole nitrogen source. Another function is to synthesize from L -isoleucine, L -leucine, and L -valine the branched chain α-keto acids which are precursors of branched chain fatty acid biosynthesis. These results together with the inducibility of the enzyme suggest that the L -leucine dehydrogenase has primarily a catabolic rather than an anabolic function in the metabolism of Bacillus subtilis .
Archives of Microbiology – Springer Journals
Published: Aug 1, 1976
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