Open AccessKinetics and redox regulation of Gpx1, an atypical 2‐Cys peroxiredoxin, in Saccharomyces cerevisiae
Author(s) -
Ohdate Takumi,
Kita Keiko,
Inoue Yoshiharu
Publication year - 2010
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1111/j.1567-1364.2010.00651.x
Subject(s) - gpx1 , peroxiredoxin , biology , gpx3 , saccharomyces cerevisiae , glutaredoxin , thioredoxin , biochemistry , glutathione , gpx6 , selenoprotein , peroxidase , glutathione peroxidase , enzyme , yeast
The budding yeast Saccharomyces cerevisiae has three homologues of glutathione peroxidase ( GPX1, GPX2 , and GPX3 ). Two structural homologues of the mammalian glutathione peroxidase, Gpx2 and Gpx3, have been proven to be atypical 2‐Cys peroxiredoxins, which prefer to use thioredoxin as an electron donor. Here, we show that Gpx1 is also an atypical 2‐Cys peroxiredoxin, but uses glutathione and thioredoxin almost equally. We determined the redox state of Gpx1 in vivo .