Journal article

Publication year: 2001

Pages: 1404-1409

Journal: European Journal of Biochemistry

Volume number: 268

Issue number: 5

ISSN: 0014-2956

eISSN: 1432-1033

Open access status: Bronze

DOI Link: https://doi.org/10.1046/j.1432-1327.2001.02005.x

Publisher: Wiley: No OnlineOpen

Abstract: 
The open reading frames of two different proteins with homologies to 2-Cys peroxiredoxins have been identified in the P. falciparum genome. Both genes, with a length of 585 and 648 bp, respectively, were amplified from a gametocyte cDNA and overexpressed in Escherichia coli. The gene products (deduced m 21.8 and 24.6 kDa) with an overall identity of 51.8% were found to be active in the glutamine synthetase protector assay. The smaller protein (named Pf-thioredoxin peroxidase 1; PfTPx1) is reduced by P. falciparum thioredoxin (PfTrx) and accepts H2O2, t-butylhydroperoxide, and cumene hydroperoxide as substrates, the respective k(cat) values for the N-terminally His-tagged protein in the presence of 10 muM PfTrx and 200 mum substrate being 67, 56, and 41 min(-1) at 25 degreesC. As described for many peroxiredoxins, PfTPx1 does not follow saturation kinetics. Furthermore, in oxidizing milieu both proteins are converted to another protein species migrating faster in SDS gel electrophoresis. For PfTPx1 also this second species was found to be active, however, with different kinetic properties which might indicate a mechanism of enzyme regulation in vivo.

Harvard Citation style: Rahlfs, S. and Becker, K. (2001) Thioredoxin peroxidases of the malarial parasite Plasmodium falciparum, European Journal of Biochemistry, 268(5), pp. 1404-1409. https://doi.org/10.1046/j.1432-1327.2001.02005.x

APA Citation style: Rahlfs, S., & Becker, K. (2001). Thioredoxin peroxidases of the malarial parasite Plasmodium falciparum. European Journal of Biochemistry. 268(5), 1404-1409. https://doi.org/10.1046/j.1432-1327.2001.02005.x