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The glyoxalase pathway in protozoan parasites

Title
The glyoxalase pathway in protozoan parasites
Type
Article in International Scientific Journal
Year
2012
Authors
silva, ms
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ferreira, aen
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gomes, r
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tomas, am
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freire, ap
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cordeiro, c
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Journal
Vol. 302
Pages: 225-229
ISSN: 1438-4221
Publisher: Elsevier
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Scientific classification
FOS: Natural sciences > Biological sciences
Other information
Authenticus ID: P-002-4N6
Abstract (EN): The glyoxalase system is the main catabolic route for methylglyoxal, a non-enzymatic glycolytic byproduct with toxic and mutagenic effects. This pathway includes two enzymes, glyoxalase I and glyoxalase II, which convert methylglyoxal to D-lactate by using glutathione as a catalytic cofactor. In protozoan parasites the glyoxalase system shows marked deviations from this model. For example, the functional replacement of glutathione by trypanothione (a spermidine-glutathione conjugate) is a characteristic of trypanosomatids. Also interesting are the lack of glyoxalase I and the presence of two glyoxalase II enzymes in Trypanosoma brucei. In Plasmodium falciparum the glyoxalase pathway is glutathione-dependent, and glyoxalase I is an atypical monomeric enzyme with two active sites. Although it is tempting to exploit these differences for their potential therapeutic value, they provide invaluable clues regarding methylglyoxal metabolism and the evolution of protozoan parasites. Glyoxalase enzymes have been characterized in only a few protozoan parasites, namely Plasmodium falciparum and the trypanosomatids Leishmania and Trypanosoma. In this review, we will focus on the key features of the glyoxalase pathway in major human protozoan parasites, with particular emphasis on the characterized systems in Plasmodium falciparum, Trypanosoma brucei, Trypanosoma cruzi, and Leishmania spp. We will also search for genes encoding glyoxalase I and II in Toxoplasma gondii, Entamoeba histolytica, and Giardia lamblia. (C) 2012 Elsevier GmbH. All rights reserved.
Language: English
Type (Professor's evaluation): Scientific
Contact: cacordeiro@fc.ul.pt
No. of pages: 5
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