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Physiological and biochemical analysis of cytochrome P‐450 in the yeast Schizosaccharomyces pombe
Author(s) -
Bligh H. F. J.,
Kelly S. L.
Publication year - 1988
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320040202
Subject(s) - schizosaccharomyces pombe , cytochrome , biology , yeast , saccharomyces cerevisiae , biochemistry , pyrene , cytochrome p450 , microsome , substrate (aquarium) , enzyme , ecology , astrobiology
The yeast Schizosacchromyces pombe has been shown to contain a microsomal cytochrome P‐450 (cyt. P‐450) inducible under conditions of glucose repression. Under these conditions the enzyme has maximal expression of 0.43 nmol g −1 wet wt at the end of the exponential phase of growth. Substrate and inhibitor affinity was examined using studies of spectral changes on binding and revealed a type II spectrum with ketoconazole ( K s = 23 μ M ) and a type I spectrum with benzo(a)pyrene ( K s = 77 μ M ). A K m of 112 μ M was found in the aryl hydrocarbon hydroxylas assay. These properties show broad comparability with the cyt. P‐450 of Saccharomyces cerevisiae .