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A glycine-cleavage complex as part of the folate one-carbon metabolism of Plasmodium falciparum.
Salcedo, Enrique; Sims, Paul F G; Hyde, John E.
Afiliação
  • Salcedo E; Centro de Investigaciones, Facultad de Medicina, Universidad Militar Nueva Granada, Bogotá, Colombia.
Trends Parasitol ; 21(9): 406-11, 2005 Sep.
Article em En | MEDLINE | ID: mdl-16039160
The glycine-cleavage complex (GCV) and serine hydroxymethyltransferase represent the two systems of one-carbon transfer that are employed in the biosynthesis of active folate cofactors in eukaryotes. Although the understanding of this area of metabolism in Plasmodium falciparum is still at an early stage, we discuss evidence that genes and transcription products of the GCV are present and expressed in this parasite. The potential role of the GCV and its relevance to the life cycle and pathogenesis of the malaria erythrocytic stages are also considered. According to its expression profile, the GCV seems to be particularly active in gametocytes. The GCV enzyme dihydrolipoamide dehydrogenase has two isoforms encoded by two different genes. It has been demonstrated recently that both genes are functional, with one of them identified as being part of a pyruvate dehydrogenase complex that is present exclusively in the apicoplast of Plasmodium species. The other isoform probably forms part of the Plasmodium GCV. The GCV is the first enzyme complex involved in folate metabolism in this parasite that can be assumed, with a good degree of certainty, to be located in the mitochondria.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Plasmodium falciparum / Glicina Hidroximetiltransferase / Transferases / Proteínas de Transporte / Eritrócitos / Ácido Fólico / Aminoácido Oxirredutases / Complexos Multienzimáticos Limite: Animals Idioma: En Revista: Trends Parasitol Assunto da revista: PARASITOLOGIA Ano de publicação: 2005 Tipo de documento: Article País de afiliação: Colômbia País de publicação: Reino Unido

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Plasmodium falciparum / Glicina Hidroximetiltransferase / Transferases / Proteínas de Transporte / Eritrócitos / Ácido Fólico / Aminoácido Oxirredutases / Complexos Multienzimáticos Limite: Animals Idioma: En Revista: Trends Parasitol Assunto da revista: PARASITOLOGIA Ano de publicação: 2005 Tipo de documento: Article País de afiliação: Colômbia País de publicação: Reino Unido