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Growth of catalase A and catalase T deficient mutant strains of Saccharomyces cerevisiae on ethanol and oleic acid
Authors:Ida J. van der Klei  Joanna Rytka  Wolf H. Kunau  Marten Veenhuis
Affiliation:(1) Department of Microbiology, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands;(2) Laboratory of Electron Microscopy, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands;(3) Institute of Biochemistry and Biophysics, Polish Academy of Science, Ulica Rakowiecka 36, PL-02-532 Warsaw, Poland;(4) Institute of Physiological Chemistry, Ruhr-Universität Bochum, Universitätsstrasse 150, D-4630 Bochum 1, Germany
Abstract:The parental strain (A+T+) of Saccharomyces cerevisiae and mutants, deficient in catalase T (A+T), catalase A (AT+) or both catalases (AT), grew on ethanol and oleic acid with comparable doubling times. Specific activities of catalase were low in glucose- and ethanol-grown cells. In the two oleic acid-grown A+-strains (A+T+ and A+T) high catalase activities were found; catalase activity invariably remained low in the AT+ strain and was never detected in the AT strain. The levels of beta-oxidation enzymes in oleic acid-grown cells of the parental and all mutant strains were not significantly different. However, cytochrome C peroxidase activity had increased 8-fold in oleic acid grown A strains (AT+ and AT) compared to parental strain cells. The degree of peroxisomal proliferation was comparable among the different strains. Catalase A was shown to be located in peroxisomes. Catalase T is most probably cytosolic in nature and/or present in the periplasmic space.
Keywords:Saccharomyces cerevisiae  Catalase A  Catalase T    /content/p54508415208n2q5/xxlarge946.gif"   alt="  beta"   align="  MIDDLE"   BORDER="  0"  >-Oxidation  Microbodies  H2O2-Metabolism
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