SUMMARY: Glutamate-α-ketoadipate transaminase, saccharopine reductase, and saccharopine dehydrogenase activities were demonstrated in extracts of but α-aminoadipate reductase activity could not be measured in whole cells or in extracts. Lysine auxotroph grew in the presence of L-lysine or DL-α-aminoadipate and incorporated radioactivity from DL-α-amino-[1-C]adipate into lysine during growth. Growing wild-type cells converted L-[U-C]lysine into α-amino-[C]adipate, suggesting both biosynthetic and degradative roles for α-aminoadipate. Lysine auxotrophs and of unlike lysine auxotrophs of satisfied their growth requirement with L-pipecolate. Moreover, extracts of wild-type catalysed the conversion of L-pipecolate to α-aminoadipate-Δ-semialdehyde. These results suggest a bio-synthetic role for L-pipecolate in but not in


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