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Biochim Biophys Acta. 2008 Nov;1780(11):1236-48. doi: 10.1016/j.bbagen.2008.03.006. Epub 2008 Mar 18.

Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism.

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  • 1Biochemie-Zentrum der Universit├Ąt Heidelberg, 69120 Heidelberg, Germany. luise.krauth-siegel@bzh.uni-heidelberg.de

Abstract

Trypanosomes and leishmania, the causative agents of several tropical diseases, possess a unique redox metabolism which is based on trypanothione. The bis(glutathionyl)spermidine is the central thiol that delivers electrons for the synthesis of DNA precursors, the detoxification of hydroperoxides and other trypanothione-dependent pathways. Many of the reactions are mediated by tryparedoxin, a distant member of the thioredoxin protein family. Trypanothione is kept reduced by the parasite-specific flavoenzyme trypanothione reductase. Since glutathione reductases and thioredoxin reductases are missing, the reaction catalyzed by trypanothione reductase represents the only connection between the NADPH- and the thiol-based redox metabolisms. Thus, cellular thiol redox homeostasis is maintained by the biosynthesis and reduction of trypanothione. Nearly all proteins of the parasite-specific trypanothione metabolism have proved to be essential.

PMID:
18395526
[PubMed - indexed for MEDLINE]
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