Abstract
A strain of Pseudomonas putida was found to oxidize L-lysine by an inducible pathway through δ-aminovalerate, and D-lysine via Δ 1-piperideine-2-carboxylate and pipecolic acid. Each pathway is selectively induced by L- or D-lysine and the appropriate intermediates. Lysine racemase is inadequate to permit growth on L-lysine after a block in the L-pathway, but is sufficient to permit cross induction of D-lysine-related enzymes.
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