The glyoxalase pathway in protozoan parasites

• Type: Article in International Scientific Journal
• Date: 2012

Authors

silva, ms (Author) Other; ferreira, aen (Author) Other; gomes, r (Author) Other; tomas, am (Author) FCUP; freire, ap (Author) Other; cordeiro, c (Author) Other

Journal

Title: International Journal of Medical Microbiology

Vol. 302

Pages: 225-229

ISSN: 1438-4221

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 5 Citations

Scopus - 6 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-002-4N6

DOI: 10.1016/j.ijmm.2012.07.005

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

No. of pages: 5