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• W2181393419 abstract "Cytochromes P-450 are a group of monooxygenase enzymes. These heme-containing enzymes are best characterized from mammalian liver where they have been shown to be responsible for the monooxygenation of a very wide variety of substrates, including endogenous substrates, such as fatty acids and steroids, and xenobiotics, such as drugs, carcinogens, and pesticides. Cytochrome P-450 enzymes are therefore of great interest not only for their biochemistry but also for their role in drug metabolism and toxicology. Cytochromes P-450 are widely distributed throughout nature. This chapter presents the enzyme from Saccharomyces cerevisiae as a model system. This yeast enzyme system has many properties in common with those of mammalian hepatic microsomal cytochrome P-450. It consists of two protein components, cytochrome P-450 and NADPH-cytochrome P-450 reductase, and phospholipid and is located in the yeast endoplasmic reticulum. The cytochrome P-450 enzyme from S. cerevisiae has a peak at 447–448 nm in purified form, and thus is a member of the narrower-specificity cytochrome P-448 class of cytochrome P-450 enzymes. An endogenous substrate of yeast cytochromes P-450 is thought to be lanosterol, which undergoes 14α-demethylation as a key step in the formation of ergosterol, the major sterol component of yeast membranes." @default.
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• W2181393419 date "1988-01-01" @default.
• W2181393419 modified "2023-09-24" @default.
• W2181393419 title "[63] Immobilization of a cytochrome P-450 enzyme from Saccharomyces cerevisiae" @default.
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• W2181393419 doi "https://doi.org/10.1016/0076-6879(88)37065-5" @default.
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