High impact information on PF14_0545

• The glutathione and thioredoxin systems represent the two major antioxidant defence lines in most eukaryotes and prokaryotes [1].
• Comparing the thioredoxin systems of different parasites and their respective host cells enhances our understanding of parasite biology and evolution, of parasite-host interactions and mechanisms of drug resistance [1].
• 2. Moderate or high concentrations of GSSG, but neither thioredoxin nor NADPH, resulted in a markedly hysteretic kinetic, characterized by a lag time before the steady state velocity was reached [2].
• Purification, characterization and kinetic properties of the multifunctional thioredoxin-glutathione reductase from Taenia crassiceps metacestode (cysticerci) [2].
• The bi-substrate reaction displays ping-pong kinetics and the K(m) values for H2O2 and thioredoxin were determined to be 0.78+/-0.14 microM and 18.94+/-3.01 microM, respectively [3].

Anatomical context of PF14_0545

• In this article we summarize the present knowledge on the thioredoxin and peroxiredoxin metabolism in malaria parasitized red blood cells [4].

Associations of PF14_0545 with chemical compounds

• Both thioredoxin and GSSG disulfide reductase activities were fully inhibited by nanomolar concentrations of the gold compound auranofin, supporting the existence of an essential selenocysteine residue [2].
• Under the same conditions, Km values of 17, 15, and 3 microM were respectively calculated for thioredoxin, GSSG and NADPH [2].

Analytical, diagnostic and therapeutic context of PF14_0545

• mRNA and protein expression profiles for three peroxiredoxins (PfTPx-1, PfTPx-2 and Pf1-Cys-Prx) and a thioredoxin (PfTrx-1) of Plasmodium falciparum during the erythrocytic stage were examined by real-time quantitative reverse transcription-PCR (RT-PCR), Western blotting and confocal laser scanning microscopy [5].

References