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Oxygen requirements for formation and activity of the squalene expoxidase in Saccharomyces cerevisiaeThe effect of oxygen on squalene epoxidase activity in Saccharomyces cerevisiae was investigated. In cells grown in standing cultures, the epoxidase was localized mainly in the 'mitochondrial' fraction. Upon aeration, enzyme activity increased and the newly formed enzyme was associated with the 'microsomal' fraction. At 0.03 percent (vol/vol) oxygen, epoxidase levels doubled, whereas the ergosterol level was only slightly increased. Cycloheximide inhibited the increase in epoxidase under these conditions. An apparent K sub m for oxygen of 0.38 percent (vol/vol) was determined from a crude particulate preparation for the epoxidase.
Document ID
19840034988
Document Type
Reprint (Version printed in journal)
Authors
Jahnke, L. (NASA Ames Research Center Moffett Field, CA, United States)
Klein, H. P. (NASA Ames Research Center Extraterrestrial Research Div., Moffett Field, CA, United States)
Date Acquired
August 12, 2013
Publication Date
August 1, 1983
Publication Information
Publication: Journal of Bacteriology
ISSN: 0021-9193
Subject Category
LIFE SCIENCES (GENERAL)
Distribution Limits
Public
Copyright
Other