Alkyl hydroperoxide reductase dependent on thioredoxin-like protein from Pyrococcus horikoshii.
Pyrococcus horikoshii is an obligate anaerobic hyperthermophilic archaeon. In P. horikoshii cells, a hydroperoxide reductase homologue ORF (PH1217) was found to be induced by oxygen. The recombinant protein, which was expressed in E. coli under aerobic conditions, exhibited no activity. However, the recombinant protein prepared under semi-anaerobic conditions exhibited alkyl hydroperoxide reductase activity. Furthermore, it was clarified that it was coupled with the thioredoxin-like system in P. horikoshii. Western blot analysis revealed that the protein was induced by oxygen and hydrogen peroxide. This protein seems to be sensitive to oxygen but forms a thioredoxin-dependent system to eliminate reactive oxygen species in P. horikoshii.
Kashima
Yasuhiro
Y
Special Division of Human Life Technology, National Institute of Advanced Industrial Science and Technology (AIST Kansai) 1-8-31 Midorigaoka, Ikeda, Osaka 563-8577.
Ishikawa
Kazuhiko
K
D000595:Amino Acid Sequence; D015153:Blotting, Western; D004926:Escherichia coli / Q000378:metabolism; D054477:Glutaredoxins; D006861:Hydrogen Peroxide / Q000378:metabolism; D008969:Molecular Sequence Data; D009249:NADP / Q000378:metabolism; D010088:Oxidoreductases; D010100:Oxygen / Q000494:pharmacology; D010544:Peroxidases / Q000235:genetics / Q000378:metabolism*; D054464:Peroxiredoxins; D011506:Proteins / Q000378:metabolism; D043902:Pyrococcus horikoshii / Q000201:enzymology*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D013880:Thioredoxin-Disulfide Reductase / Q000378:metabolism; D013879:Thioredoxins / Q000378:metabolism*
D054477:Glutaredoxins; D011506:Proteins; D011994:Recombinant Proteins; D013879:Thioredoxins; D009249:NADP; D006861:Hydrogen Peroxide; D010088:Oxidoreductases; D010544:Peroxidases; D054464:Peroxiredoxins; D013880:Thioredoxin-Disulfide Reductase; D010100:Oxygen