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    FEBS Lett. 2008 Mar 5;582(5):729-33. Epub 2008 Feb 5.

    The 3-hydroxyacyl-ACP dehydratase of mitochondrial fatty acid synthesis in Trypanosoma brucei.

    Autio KJ, Guler JL, Kastaniotis AJ, Englund PT, Hiltunen JK.

    Department of Biochemistry and Biocenter Oulu, University of Oulu, Oulu, Finland. kaija.autio@oulu.fi

    The trypanosomatid parasite Trypanosoma brucei synthesizes fatty acids in the mitochondrion using the type II fatty acid synthesis (FAS) machinery. When mitochondrial FAS was characterized in T. brucei, all of the enzymatic components were identified based on their homology to yeast mitochondrial FAS enzymes, except for 3-hydroxyacyl-ACP dehydratase. Here we describe the characterization of T. brucei mitochondrial 3-hydroxyacyl-ACP dehydratase (TbHTD2), which was identified by its similarity to the human mitochondrial dehydratase. TbHTD2 can rescue the respiratory deficient phenotype of the yeast knock-out strain and restore the lipoic acid content, is localized in the mitochondrion and exhibits hydratase 2 activity.

    PMID: 18258193 [PubMed - indexed for MEDLINE]

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