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The diversity and evolution of thioredoxin reductase: new perspectives

Lookup NU author(s): Professor Robert HirtORCiD, Emeritus Professor T. Martin Embley FMedSci FRSORCiD

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Abstract

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.

Publication metadata

Author(s): Embley TM; Hirt RP; Muller S; Coombs GH

Publication type: Article

Publication status: Published

Journal: Trends in Parasitology

Year: 2002

Volume: 18

Issue: 7

Pages: 302-308

ISSN (print): 1471-4922

ISSN (electronic): 1471-5007

Publisher: Elsevier

URL: http://dx.doi.org/10.1016/S1471-4922(02)02293-6

DOI: 10.1016/S1471-4922(02)02293-6

Notes: 1471-4922 Journal Article Review Review, Tutorial

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