Proceedings of the Korean Society of Applied Pharmacology (한국응용약물학회:학술대회논문집)
- 1996.11a
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- Pages.165-169
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- 1996
Identification of Retained N-Formylmethionine in Bacterial Recombinant Mammalian Cytochrome P450 Proteins with the N-Terminal Sequence MALLLAVF‥‥
Abstract
The cytochrome P450 (P450) proteins have been studied extensively because of their prominent roles as catalysts in the oxidations of drugs, carcinogens, steroids, alkaloids, vitamins, and other important chemicals (Guengerich, 1991). In the past decade the study of these enzymes has been advanced by the cloning of cDNAs and expression of the proteins in several heterologous vector systems. One approach that has been employed in this and other laboratories is expression in bacteria. To date at least 31 different mammalian P450s have been expressed in Escherichia coli-band systems (Guengerich et al., 1996). In most of these cases the N-terminus has been altered to facilitate better expression (Barnes et al., 1991).
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