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

https://arctichealth.org/en/permalink/ahliterature87070
Source
FEBS Lett. 2008 Mar 5;582(5):729-33
Publication Type
Article
Date
Mar-5-2008
Author
Autio Kaija J
Guler Jennifer L
Kastaniotis Alexander J
Englund Paul T
Hiltunen J Kalervo
Author Affiliation
Department of Biochemistry and Biocenter Oulu, University of Oulu, Oulu, Finland. kaija.autio@oulu.fi
Source
FEBS Lett. 2008 Mar 5;582(5):729-33
Date
Mar-5-2008
Language
English
Publication Type
Article
Keywords
Amino Acid Sequence
Animals
Electrophoresis
Fatty Acids - biosynthesis
Genetic Complementation Test
Humans
Hydro-Lyases - chemistry - isolation & purification - metabolism
Mitochondria - enzymology
Molecular Sequence Data
Protein Transport
Recombinant Fusion Proteins - isolation & purification - metabolism
Saccharomyces cerevisiae - cytology - metabolism
Sequence Alignment
Thioctic Acid - metabolism
Trypanosoma brucei brucei - cytology - enzymology
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.
PubMed ID
18258193 View in PubMed
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