Catalases protect cellular proteins from oxidative modification in Saccharomyces cerevisiae.
The yeast Saccharomyces cerevisiae cells had higher antioxidant enzyme activities under growth in ethanol than that in glucose as a carbon and energy source. The correlations between catalase activity and protein carbonyl level (r(2)=0.857), between catalase and glucose-6-phosphate dehydrogenase activities (r(2)=0.924) and between protein carbonyl levels and glucose-6-phosphate dehydrogenase activity (r(2)=0.988) under growth in ethanol were found. Growing in ethanol the strain deficient in cytosolic and peroxisomal catalases had 7.1-fold higher level of carbonyl proteins than that of wild-type strain. Our data suggest that in vivo catalases may protect glucose-6-phosphate dehydrogenase against oxidative inactivation.
Lushchak
Volodymyr I
VI
Department of Biochemistry, Vassyl Stefanyk Precarpathian National University, 57 Shevchenko Str., 76025 Ivano-Frankivsk, Ukraine. lushchak@pu.if.ua
Gospodaryov
Dmytro V
DV
D000975:Antioxidants / Q000378:metabolism; D002374:Catalase / Q000502:physiology*; D003600:Cytosol / Q000187:drug effects / Q000201:enzymology; D000431:Ethanol / Q000494:pharmacology; D005947:Glucose / Q000494:pharmacology; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism*; D005980:Glutathione Reductase / Q000378:metabolism*; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D020675:Peroxisomes / Q000187:drug effects / Q000201:enzymology; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000201:enzymology / Q000254:growth & development*; D013482:Superoxide Dismutase / Q000378:metabolism*
D000975:Antioxidants; D000431:Ethanol; D005954:Glucosephosphate Dehydrogenase; D002374:Catalase; D013482:Superoxide Dismutase; D005980:Glutathione Reductase; D005947:Glucose