Beta-oxidation of unsaturated fatty acids in humans. Isoforms of delta 3, delta 2-enoyl-CoA isomerase.

This investigation was undertaken in order to elucidate the human enzymes which participate in metabolism of the double bonds of unsaturated fatty acids during beta-oxidation. The results indicate that the human monofunctional delta 3, delta 2-enoyl-CoA isomerase (EC 5.3.3.8) with the native M(r) of 70,000 differed significantly from its rat counterpart [Palosaari et al. (1990) J. Biol. Chem. 265, 3347-3353]; the isoelectric point of the human isoform was over three pH-units more acidic, it showed different chromatographic behaviour, the human enzyme did not show any clear-cut substrate chain-length specificity and only a weak immunological cross-reactivity was detected with the antibody to rat liver mitochondrial short-chain enzyme. This explains the failure of attempts to apply the rat data directly to human beings. Another isomerase activity from human liver was found to be a part of the isomerase-hydratase-dehydrogenase polypeptide showing immunological cross-reactivity with the previously characterized peroxisomal multifunctional enzyme (MFE) from rat liver.