Glutathione peroxidase in yeast. Presence of the enzyme and induction by oxidative conditions.
The presence of glutathione peroxidase activity is reported for the first time for a wild type strain of Saccharomyces cerevisiae. Both forms of enzyme, i.e. that specifically active toward H2O2 alone and that decomposing also organic peroxides, were found to be present. The H2O2 specific form disappeared when cells were grown in the absence of oxygen, while the other form was much increased under the same conditions. Addition of copper to the culture greatly increased both forms. The results show that glutathione peroxidase is to be included, as an important component that is also highly responsive to oxidative environments, in the enzyme defense system of yeast against oxidative damage.
Galiazzo
F
F
Department of Biology, Tor Vergata University, Rome, Italy.
Schiesser
A
A
Rotilio
G
G
D000332:Aerobiosis; D000693:Anaerobiosis; D003300:Copper / Q000494:pharmacology; D005979:Glutathione Peroxidase / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D003300:Copper; D005979:Glutathione Peroxidase