Peroxisomal oxidation of L‐2‐hydroxyphytanic acid in rat kidney cortex

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Abstract
A previously unreported metabolite of mammalian phytanic acid catabolism, 2‐oxophytanic acid, was identified by gas chromatography/mass spectrometry analysis. The formation of 2‐oxophytanic acid was demonstrated to result from the oxidation of L‐2‐hydroxyphytanic acid, a reaction catalysed by a rat‐kidnev‐corted H2O2‐generating oxidase. The pH optimum for the L‐2‐hydroxyphytanate oxidase activity was 8.5 and its apparent Km and Vm were about 0.15 mM and 0.35 μmol min1 (g tissue)−1, respectively. L‐2‐Hydroxyisocaproate, a substrate of rat kidney L‐α‐hydroxyacid oxidase type B, inhibited the formation of 2‐oxophytanate from L‐2‐hydroxyphytanic acid. Fractionation studies have indicated that 40% of L‐2‐hydroxyphytanate oxidase was associated with a particulate fraction and that the activity distribution of the oxidase closely paralleled that of catalase, a well known peroxisomal marker enzyme.

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