FASEB J. Cell Migration Consortium
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Johnson, E. F.
Right arrow Articles by Hsu, M. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Johnson, E. F.
Right arrow Articles by Hsu, M. H.

The FASEB Journal, Vol 6, 700-705, Copyright © 1992 by The Federation of American Societies for Experimental Biology


REVIEWS

Analysis of the catalytic specificity of cytochrome P450 enzymes through site-directed mutagenesis

EF Johnson, T Kronbach and MH Hsu
Scripps Research Institute, Division of Biochemistry, La Jolla, California 92037.

The way in which structural diversity encodes the capacity of individual P450 enzymes to metabolize multiple, structurally distinct substrates remains largely unknown. The tools of molecular biology provide a means of identifying amino acid residues among closely related P450s that are determinants of their distinct catalytic properties. Work in our laboratory has identified two substrate specificity-determining segments of the amino acid sequences of subfamily 2C P450s. A pattern has emerged from this work, and that of others, which suggests a model for the structural basis of P450 catalytic diversity.


This article has been cited by other articles:


Home page
J. Pharmacol. Exp. Ther.Home page
C. Sridar, U. M. Kent, L. M. Notley, E. M. J. Gillam, and P. F. Hollenberg
Effect of Tamoxifen on the Enzymatic Activity of Human Cytochrome CYP2B6
J. Pharmacol. Exp. Ther., June 1, 2002; 301(3): 945 - 952.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
G. C. Ibeanu, B. I. Ghanayem, P. Linko, L. Li, L. G. Pedersen, and J. A. Goldstein
Identification of Residues 99, 220, and 221 of Human Cytochrome P450 2C19 as Key Determinants of Omeprazole Hydroxylase Activity
J. Biol. Chem., May 24, 1996; 271(21): 12496 - 12501.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
B. Böttner, H. Schrauber, and R. Bernhardt
Engineering a Mineralocorticoid- to a Glucocorticoid-synthesizing Cytochrome P450
J. Biol. Chem., April 5, 1996; 271(14): 8028 - 8033.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. K. Ramarao, P. Straub, and B. Kemper
Identification by in Vitro Mutagenesis of the Interaction of Two Segments of C2MstC1, a Chimera of Cytochromes P450 2C2 and P450 2C1
J. Biol. Chem., January 27, 1995; 270(4): 1873 - 1880.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1992 by The Federation of American Societies for Experimental Biology.