Catalases protect cellular proteins from oxidative modification in

Abstract

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.

Antifungal and antiaflatoxigenic activities of coumarinyl thiosemicarbazides against Aspergillus flavus NRRL 3251

“…The catalase (CAT; EC 1.11.1.6) activity was determined according to Reverberi et al (16) using the spectrophotometric method at 240 nm, while the glutathione peroxidase (GPX; EC 1.11.1.9) activity assay was performed according to Esworthy et al (17) using the spectrophotometric method at 340 nm. Lipid peroxides (TBARS) were determined using the spectrophotometric method at 535 nm according to Luschak and Gospodaryov (18).…”

Underinvestigated Roles of Glucose-6-Phosphate Dehydrogenase

“…Strong oxidative stress may lead to irreversible oxidation of G6PDH resulted in its inactivation. For instance, G6PDH was inactivated during growth of catalase-deficient yeast on ethanol, a nonfermentable carbon source [41]. It was shown in this and other cases that G6PDH activity positively correlated with catalase activity, suggesting potential G6PDH protection against oxidation by catalase [5,37].…”

Oxidative Stress: Cause and Consequence of Diseases

“…There are also several studies on budding yeasts revealed changes in gene expression and protein synthesis in response to oxidants (Godon et al, 1998;Thorpe et al, 2004;Temple et al, 2005). Experiments conducted in our laboratory with acatalatic budding yeast had shown that the loss of mitochondrial catalase is not crucial for yeast surviving, while loss of the cytosolic enzyme or both isoenzymes lead to serious growth retardation and is accompanied by inhibition of other enzymes (Lushchak & Gospodaryov, 2005). Interestingly, like in some cases with antioxidant enzyme deficiencies in humans, only special conditions revealed catalase deficiency in the yeast, e.g.…”

“…On the other hand, iron is a component of haem, a prosthetic group in catalase holoenzyme. Susceptibility to oxidative modification is described for catalase, glutathione peroxidase, Cu,Zn-SOD (Pigeolet et al, 1990;Tabatabaie & Floyd, 1994;Avery, 2011), and G6PDH (Lushchak & Gospodaryov, 2005). The latter is believed to be one of the most susceptible to oxidation enzymes (Lushchak, 2010).…”