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The generation time ofPseudomonas putida withl -leucine was 20 h in synthetic media but only 3 h withd -leucine. Slow growth in the presence ofl -leucine was partially overcome by addition of 0.1 mM amounts of eitherd -valine,l -valine, or 2-ketoisovalerate. The activities of five enzymes which take part in the oxidation of leucine byP. putida were measured under various conditions of growth. Four enzymes were induced by growth withdl -leucine as sole source of carbon:d -amino acid dehydrogenase, branched-chain keto acid dehydrogenase, 3-methylcrotonyl-coenzyme A carboxylase, and 3-hydroxy-3-methylglutaryl-coenzyme A lyase. The segment of the pathway required for oxidation of 3-methylcrotonate was induced by growth on isovalerate or 3-methylcrotonate without formation of the preceding enzymes. The synthesis of carboxylase and lyase appeared to have been repressed by the addition ofl -glutamate or glucose to cells growing ondl -leucine as the sole carbon source. Mutants unable to grow at the expense of isovalerate had reduced levels of carboxylase and lyase, whereas the levels of three enzymes common to the catabolism of all three branched-chain amino acids and those of two isoleucine catabolic enzymes were normal.

Regulation of Leucine Catabolism in Pseudomonas putida