Microsomal cytochrome P4502C5: comparison to microbial P450s and unique features

Authors
Williams, PA Cosme, J Sridhar, V Johnson, EF McRee, DE
Citation
Pa. Williams et al., Microsomal cytochrome P4502C5: comparison to microbial P450s and unique features, J INORG BIO, 81(3), 2000, pp. 183-190
Citations number
20
Categorie Soggetti
Biochemistry & Biophysics","Inorganic & Nuclear Chemistry
Journal title
JOURNAL OF INORGANIC BIOCHEMISTRY
ISSN journal
01620134 → ACNP
Volume
81
Issue
3
Year of publication
2000
Pages
183 - 190
Database
ISI
SICI code
0162-0134(20000831)81:3<183:MCPCTM>2.0.ZU;2-U
Abstract
Although microsomal P450s represent the majority of P450s, only microbial P 450s have been amenable to crystal structure solution. We have recently sol ved the first crystal structure of a microsomal P450, 2C5, a progesterone h ydroxylase from rabbit. We discuss the features of the protein in common wi th existing structures of microbial P450s and limitations of homology model ing mammalian P450s based on the microbial structures. Unique features invo lving membrane, substrate and cytochrome P450 reductase interactions are al so discussed. (C) 2000 Elsevier Science S.A. All rights reserved.