Characterization of peroxisomal and mitochondrial carnitine acetyltransferases purified from alkane-grown Candida tropicalis.

Properties of peroxisomal and mitochondrial carnitine acetyltransferases purified from an alkane-grown yeast, Candida tropicalis, were compared each other. The molecular weight of both enzymes was estimated to be about 420 000 by analytical ultracentrifugation and gel filtration chromatography with Sepharose 6B. However, each enzyme gave two subunits on the polyacrylamide slab gel electrophoresis in the presence of sodium dodecyl sulfate: the peroxisomal enzyme (64 000 and 57 000) and the mitochondrial enzyme (64 000 and 52 000). The subcellularly distinct enzymes gave a similar amino acid composition except for the contents of some amino acids: glycine, valine, glutamic acid and aspartic acid. Their isoelectric point was somewhat different: 5.11 for the peroxisomal enzyme and 5.22 for the mitochondrial enzyme. Both enzymes had the same amino-terminal residue (glutamic acid or glutamine) and the heat stability, and was indistinguishable immunochemically. These results suggest that peroxisomal and mitochondrial carnitine acetyltransferases of C. tropicalis cells may be products of the same nuclear gene. Differences in the molecular weight of the subunits of the enzymes would result from modification or processing of the common protein in the step of distribution to the respective organelles, that is, so-called post-translational modification.