Aspartate Aminotransferase - Bridging Carbohydrate and Energy Metabolism in Plasmodium Falciparum

Carsten Wrenger, Ingrid B. Mueller, Ariel M. Silber, Rositsa Jordanova, Victor S. Lamzin, Matthew R. Groves*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

16 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)332-336
Number of pages5
JournalCurrent drug metabolism
Volume13
Issue number3
Publication statusPublished - Mar-2012

Keywords

  • Carbohydrate metabolism
  • energy metabolism
  • malarial parasite
  • aspartate aminotransferase
  • MITOCHONDRIAL ELECTRON-TRANSPORT
  • DRUG-RESISTANT MALARIA
  • PARASITE
  • DEHYDROGENASE
  • BIOSYNTHESIS
  • INHIBITION
  • ENZYME
  • MODEL
  • CHAIN
  • HOST

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