| Literature DB >> 21074581 |
Mary Morada1, Ondrej Smid, Vladimir Hampl, Robert Sutak, Brian Lam, Paola Rappelli, Daniele Dessì, Pier L Fiori, Jan Tachezy, Nigel Yarlett.
Abstract
The arginine dihydrolase (ADH) pathway has an analogous function to the urea cycle in mitochondria-containing cells, by removing nitrogen from amino acids and generating ATP. Subcellular localization of the ADH pathway enzymes in Trichomonas vaginalis revealed that arginine deiminase (ADI) localizes to the hydrogenosome, a mitochondrion-like organelle of anaerobic protists. However the other enzymes of the ADH pathway, ornithine carbamyltransferase and carbamate kinase localize to the cytosol. Three gene sequences of T. vaginalis ADI (ADI 1-3) were identified in the T. vaginalis genome, all having putative mitochondrial targeting sequences. The ADI sequences were cloned and used to probe T. vaginalis using a carboxyterminal di-hemogglutinin epitope tag which demonstrated co-localization with malic enzyme confirming the hydrogenosome localization of this enzyme. Copyright ÂEntities:
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Year: 2010 PMID: 21074581 PMCID: PMC3026898 DOI: 10.1016/j.molbiopara.2010.10.004
Source DB: PubMed Journal: Mol Biochem Parasitol ISSN: 0166-6851 Impact factor: 1.759