Implications for Drug Metabolism
Abstract
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.
Footnotes
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Send reprint requests to: Dr. James R. Halpert, Department of Pharmacology and Toxicology, University of Texas Medical Branch at Galveston, 301 University Boulevard, Galveston, TX 77555-1031. e-mail: jhalpert{at}utmb.edu
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This work was supported in part by National Institutes of Health grants GM25515 (P.O.M.), GM54995 (J.R.H.), and United States Public Health Service grant GM31001 (E.F.J.), with support for the mass spectrometry facility (A. Burlingame, director) by grant RR01614 and Liver Center grant (R. Ockner, Director) DK26743 (P.O.M.).
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↵2 Z. Zhang and P. R. Ortiz de Montellano, unpublished results.
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↵3 J.P. Jones, K.J. French, J.L. Osterhuat, and H. Yin, unpublished results.
- Abbreviations used are::
- 1-ABT
- 1-aminobenzotriazole
- DLPC
- dilauroyl-l-α-phosphatidylcholine
- FMO
- flavin-containing monooxygenases
- P450
- cytochrome P450
- SRS
- substrate recognition site
- TR
- trypanothione reductase
- The American Society for Pharmacology and Experimental Therapeutics
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