Vol. 26, Issue 12, 1223-1231, December 1998

Structure-Function of Cytochromes P450 and Flavin-Containing Monooxygenases
Implications for Drug Metabolism

James R. Halpert, Tammy L. Domanski, Orhan Adali, Christine P. Biagini, Jose Cosme, Elizabeth A. Dierks, Eric F. Johnson, Jeffrey P. Jones, Paul Ortiz de Montellano, Richard M. Philpot, Ole Sibbesen, W. Keith Wyatt, and Zhoupeng Zheng

Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona (J.R.H., T.L.D.), Department of Molecular and Experimental Medicine NX-4, Scripps Research Institute (E.F.J., J.C.), Department of Chemistry, Washington State University (J.P.J.), Department of Chemistry and Pharmacology, School of Pharmacy, University of California at San Francisco (P.O.M., E.A.D., O.S., Z.Z.), and Laboratory of Signal Transduction, National Institute of Environmental Health Sciences (R.M.P., O.A., C.P.B., W.K.W.)

This article is a report on a symposium held at Experimental Biology '98 in San Francisco, California. Recent developments in site-directed mutagenesis, computer-modeling, and mechanistic analysis of cytochromes P450 and flavin-containing monooxygenases are described. A unifying theme is the elaboration of general approaches for understanding and predicting the function of individual forms of these enzymes. A related goal is the production of soluble forms of mammalian cytochromes P450 for X-ray crystallography.