2mmn

Structural highlights

Function

THIO1_PLAF7 Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (PubMed:11013257, PubMed:20673832). By modifying the redox status of targeted proteins, induces changes in their structure and activity (PubMed:19360125, PubMed:20673832). Reduces oxidized glutathione (GSSG), thereby acting as a backup for the glutathione redox system (PubMed:11013257). Reduces nitroglutathione (GSNO), a compound involved in the transport of nitric oxide (NO) (PubMed:11013257). Also reduces oxidative stress by detoxifying hydrogen peroxide, tert-butyl hydroperoxide and cumene hydroperoxide (PubMed:14962358). Activates ornithine aminotransferase OAT by reducing a disulfide bond in the substrate binding loop, thereby enhancing the affinity of OAT for its substrates (PubMed:20673832). May reduce S-adenosyl-L-homocysteine hydrolase SAHH (PubMed:19360125).^{[1] [2] [3] [4]}

See Also

• Thioredoxin 3D structures

References

1. ↑ Kanzok SM, Schirmer RH, Turbachova I, Iozef R, Becker K. The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited. J Biol Chem. 2000 Dec 22;275(51):40180-6. doi: 10.1074/jbc.M007633200. PMID:11013257 doi:http://dx.doi.org/10.1074/jbc.M007633200
2. ↑ Rahlfs S, Nickel C, Deponte M, Schirmer RH, Becker K. Plasmodium falciparum thioredoxins and glutaredoxins as central players in redox metabolism. Redox Rep. 2003;8(5):246-50. PMID:14962358 doi:10.1179/135100003225002844
3. ↑ Sturm N, Jortzik E, Mailu BM, Koncarevic S, Deponte M, Forchhammer K, Rahlfs S, Becker K. Identification of proteins targeted by the thioredoxin superfamily in Plasmodium falciparum. PLoS Pathog. 2009 Apr;5(4):e1000383. PMID:19360125 doi:10.1371/journal.ppat.1000383
4. ↑ Jortzik E, Fritz-Wolf K, Sturm N, Hipp M, Rahlfs S, Becker K. Redox regulation of Plasmodium falciparum ornithine delta-aminotransferase. J Mol Biol. 2010 Sep 17;402(2):445-59. Epub 2010 Jul 29. PMID:20673832 doi:10.1016/j.jmb.2010.07.039