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    Biochem Biophys Res Commun. 1994 Mar 15;199(2):818-25.

    Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein.

    Kamijo T, Aoyama T, Komiyama A, Hashimoto T.

    Department of Pediatrics, Shinshu University School of Medicine, Nagano, Japan.

    Trifunctional protein deficiency, a typical mitochondrial long-chain fatty acid beta-oxidation defect, is caused by the abnormality of mitochondrial long-chain enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein consisting of four moles of alpha-subunit and four moles of beta-subunit. We cloned, sequenced, and expressed the following cDNAs for the alpha- and beta-subunits of human trifunctional protein. The 2,690-bp cDNA clone had a 2,289-bp open reading frame encoding a 82,958-Da precursor and a 78,969-Da mature subunit (alpha-subunit). Expression of this cDNA in mammalian cells yielded a polypeptide with the long-chain enoyl-CoA hydratase and long-chain 3-hydroxyacyl-CoA dehydrogenase activities. The 1,991-bp cDNA clone had a 1,422-bp open reading frame encoding a 51,293-Da precursor and a 47,484-Da mature subunit (beta-subunit). Expression of this cDNA in mammalian cells yielded a polypeptide with the long-chain 3-ketoacyl-CoA thiolase activity.

    PMID: 8135828 [PubMed - indexed for MEDLINE]

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