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β‐Oxidation of unsaturated fatty acids in humans Isoforms of Δ 3 , Δ 2 ‐enoyl‐CoA isomerase
Author(s) -
Kilponen Johanna M.,
Hiltunen J.Kalervo
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81590-v
Subject(s) - isomerase , biochemistry , enzyme , peroxisome , isoelectric point , chemistry , dehydrogenase , isozyme , gene isoform , substrate (aquarium) , triosephosphate isomerase , biology , gene , ecology
This investigation was undertaken in order to elucidate the human enzymes which participate in metabolism of the double bonds of unsaturated fatty acids during, β‐oxidation. The results indicate that the human monofunctional Δ 3 , Δ 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.