Browse by author
Lookup NU author(s): Professor Robert HirtORCiD,
Emeritus Professor T. Martin Embley FMedSci FRS
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
The thioredoxin system is a major line of cellular defence against oxygen damage. Two distinct thioredoxin reductases found in eukaryotes have different catalytic mechanisms and a mutually exclusive distribution reflecting a complex evolutionary history. Most eukaryotes, including several important parasites, contain a low molecular weight thioredoxin reductase, apparently of bacterial origin. By contrast, animals and apicomplexan protozoa, including Plasmodium, appear to have lost this enzyme. Instead, they contain a high molecular weight thioredoxin reductase, which shares common ancestry with glutathione reductase. This article reviews these fundamental differences between the thioredoxin reductases of some parasites and their hosts, discusses their phylogenetic relationships and considers the potential of the enzymes as therapeutic targets.
Author(s): Embley TM; Hirt RP; Muller S; Coombs GH
Publication type: Article
Publication status: Published
Journal: Trends in Parasitology
ISSN (print): 1471-4922
ISSN (electronic): 1471-5007
Altmetrics provided by Altmetric