Species variation in organellar location and activity of L-pipecolic acid oxidation in mammals.

The oxidation of L-pipecolic acid to alpha-aminoadipic acid was studied in eight species of mammals using an assay system more sensitive than those previously employed. After percoll-gradient fractionation, activity was localized to the mitochondrial-enriched fractions in tissues from rabbit, guinea pig, pig, dog, and sheep, with guinea pig kidney cortex showing greatest specific activity. These results contrast with the peroxisomal oxidation of L-pipecolic acid observed in macaques and man (Mihalik and Rhead 1989; Mihalik et al. 1989). Rats and mice had undetectable levels of both peroxisomal and mitochondrial L-pipecolic acid oxidation. In the rat, peroxisomal oxidation activity was not induced by feeding with either clofibrate or clofibrate and L-pipecolic acid. Thus, among mammals, both the ability to oxidize L-pipecolic acid and the organellar location of this oxidation is species dependent.