The 3-hydroxyacyl-ACP dehydratase of mitochondrial fatty acid synthesis in Trypanosoma brucei.
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.
Autio
Kaija J
KJ
Department of Biochemistry and Biocenter Oulu, University of Oulu, Oulu, Finland. kaija.autio@oulu.fi
Guler
Jennifer L
JL
Kastaniotis
Alexander J
AJ
Englund
Paul T
PT
Hiltunen
J Kalervo
JK
D000595:Amino Acid Sequence; D000818:Animals; D004586:Electrophoresis; D005227:Fatty Acids / Q000096:biosynthesis*; D005816:Genetic Complementation Test; D006801:Humans; D006836:Hydro-Lyases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008928:Mitochondria / Q000201:enzymology*; D008969:Molecular Sequence Data; D021381:Protein Transport; D011993:Recombinant Fusion Proteins / Q000302:isolation & purification / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000378:metabolism; D016415:Sequence Alignment; D008063:Thioctic Acid / Q000378:metabolism; D014346:Trypanosoma brucei brucei / Q000166:cytology / Q000201:enzymology*
D005227:Fatty Acids; D011993:Recombinant Fusion Proteins; D008063:Thioctic Acid; D006836:Hydro-Lyases