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 β-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.
Original language | English |
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Pages (from-to) | 513-517 |
Number of pages | 5 |
Journal | Archives of Microbiology |
Volume | 153 |
Issue number | 5 |
DOIs | |
Publication status | Published - Apr-1990 |
Keywords
- H2O2-Metabolism
- Microbodies
- β-Oxidation
- Catalase T
- Catalase A
- Saccharomyces cerevisiae