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

Kaija J. Autio, Jennifer L. Guler, Alexander J. Kastaniotis, Paul T. Englund, J. Kalervo Hiltunen

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)729-733
Number of pages5
JournalFEBS Letters
Volume582
Issue number5
DOIs
StatePublished - Mar 5 2008

Keywords

  • 3-Hydroxyacyl-ACP dehydratase
  • Fatty acid synthesis
  • Mitochondria
  • Trypanosoma brucei

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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