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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Aspartate Aminotransferase - Bridging Carbohydrate and Energy Metabolism in Plasmodium Falciparum

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Author(s):
Wrenger, Carsten [1] ; Mueller, Ingrid B. [2] ; Silber, Ariel M. [1] ; Jordanova, Rositsa [3] ; Lamzin, Victor S. [3] ; Groves, Matthew R. [3]
Total Authors: 6
Affiliation:
[1] Univ Sao Paulo, Dept Parasitol, Inst Biomed Sci, BR-05508000 Sao Paulo - Brazil
[2] Bernhard Nocht Inst Trop Med, D-20359 Hamburg - Germany
[3] DESY, European Mol Biol Lab, Hamburg Outstn, D-22670 Hamburg - Germany
Total Affiliations: 3
Document type: Review article
Source: CURRENT DRUG METABOLISM; v. 13, n. 3, p. 332-336, MAR 2012.
Web of Science Citations: 9
Abstract

In this mini-review we briefly examine and summarize evidence on the role of the plasmodial aspartate aminotransferase (AspAT) of the malarial parasite. Recent data have provided information on the products of the purine salvage pathway as well as the glycolytic and oxidative phosphorylation pathways, suggesting that the reaction catalyzed by AspAT is an essential step in all these biochemical processes. While the biological role of the oxidative phosphorylation cycle still remains to be demonstrated, the presence of a single protein that is functional in multiple pathways (i.e. amino acid/purine/pyrimidine biosynthesis and carbohydrate metabolism) provides a high potential for the development of novel strategies to combat the spread of multi-drug resistant malaria. (AU)