Some physiological functions of the L-leucine dehydrogenase in Bacillus subtilis.
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 alpha-keto acids which are precursors of branched chain fatty acid biosythesis. 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.
D000594:Amino Acid Oxidoreductases / Q000096:biosynthesis / Q000378:metabolism*; D000596:Amino Acids / Q000378:metabolism; D001412:Bacillus subtilis / Q000201:enzymology*; D004790:Enzyme Induction; D005227:Fatty Acids / Q000096:biosynthesis; D007651:Keto Acids / Q000096:biosynthesis; D009154:Mutation; D000644:Quaternary Ammonium Compounds / Q000378:metabolism
D000596:Amino Acids; D005227:Fatty Acids; D007651:Keto Acids; D000644:Quaternary Ammonium Compounds; D000594:Amino Acid Oxidoreductases