Growth of catalase A and catalase T deficient mutant strains of Saccharomyces cerevisiae on ethanol and oleic acid |
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Authors: | Ida J. van der Klei Joanna Rytka Wolf H. Kunau Marten Veenhuis |
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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 |
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Abstract: | The parental strain (A+T+) of Saccharomyces cerevisiae and mutants, deficient in catalase T (A+T–), catalase A (A–T+) or both catalases (A–T–), 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 A–T+ strain and was never detected in the A–T– strain. The levels of -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 (A–T+ and A–T–) 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. |
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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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