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Distribution of the Isopropylmalate Pathway to Leucine Among Diverse Bacteria

1974; American Society for Microbiology; Volume: 118; Issue: 3 Linguagem: Inglês

10.1128/jb.118.3.935-941.1974

1098-5530

Barry Stieglitz, Joseph M. Calvo,

Enzyme Structure and Function

α-Isopropylmalate synthase and β-isopropylmalate dehydrogenase activities were detected in extracts of the following organisms: Chromatium D, Rhodopseudomonas spheroides, Hydrogenomonas H16, Pseudomonas aeruginosa, Pseudomonas fluorescens, Vibrio extorquens, Rhizobium japonicum, Alcaligenes viscolactis, Escherichia coli B, Proteus vulgaris, Aerobacter aerogenes, Salmonella typhimurium, Micrococcus sp., Micrococcus lysodeikticus, Bacillus polymyxa, Bacillus subtilis , and Nocardia opaca . The α-isopropylmalate synthase activity in these extracts was inhibited by low concentrations of l -leucine. Taken together with other data, these results suggest that the isopropylmalate pathway is widespread among organisms that can synthesize leucine.