The glyoxalase pathway in protozoan parasites

• Tipo: Artigo em Revista Científica Internacional
• Data: 2012

Autores

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

Revista

Título: International Journal of Medical Microbiology

Vol. 302

Páginas: 225-229

ISSN: 1438-4221

Editora: Elsevier

Indexação

ISI Web of Knowledge - 5 Citações

Scopus - 6 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Ciências biológicas

Outras Informações

ID Authenticus: 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.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 5