Structure-function of cytochromes P450 and flavin-containing monooxygenases: implications for drug metabolism.
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.
Halpert
J R
JR
Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, USA. jhalpert@utmb.edu
Domanski
T L
TL
Adali
O
O
Biagini
C P
CP
Cosme
J
J
Dierks
E A
EA
Johnson
E F
EF
Jones
J P
JP
Ortiz de Montellano
P
P
Philpot
R M
RM
Sibbesen
O
O
Wyatt
W K
WK
Zheng
Z
Z
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000378:metabolism*; D005415:Flavins / Q000378:metabolism*; D006801:Humans; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D004364:Pharmaceutical Preparations / Q000378:metabolism*; D013329:Structure-Activity Relationship
D005415:Flavins; D004364:Pharmaceutical Preparations; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases