| Literature DB >> 822797 |
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 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.Entities:
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Year: 1976 PMID: 822797 DOI: 10.1007/BF00425113
Source DB: PubMed Journal: Arch Microbiol ISSN: 0302-8933 Impact factor: 2.552