Abstract
Recent advanced technologies of molecular cloning and protein chemistry revealed the entire primary structure of various cytochrome P-450 species so that the multiplicity of P-450 was evidently clarified. The domains responsible for heme binding and subcellular localization were posturated on the basis of the comparison of their primary structures.The rat microsomal P-450MC cDNA was efficiently expressed in the yeast Sacchromyces cerevisiae under the control of alcohol dehydrogenase I promoter and terminator. The P-450MC protein synthesized in yeast was localized in microsomes, contained heme in the molecule and interacted with an yeast electron-transport chain to exhibit monooxygenase activity.The yeast host-vector system combined with the site-directed mutagenesis and chimeric gene construction can be useful for overproduction and characterization of membrane-bound P-450s.
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