The Mycobacterium tuberculosis cytochrome P450 system

Tuberculosis remains a leading cause of human mortality. The emergence of strains of Mycobacterium tuberculosis, the causative agent, that are resistant to the major frontline antitubercular drugs increases the urgency for the development of new therapeutic agents. Sequencing of the M. tuberculosis...

Full description

Saved in:
Bibliographic Details
Published in:Archives of biochemistry and biophysics 2010-01, Vol.493 (1), p.82-95
Main Authors: Ouellet, Hugues, Johnston, Jonathan B., Ortiz de Montellano, Paul R.
Format: Article
Language:English
Subjects:
Azole drugs
Cyclodipeptide
CYP121
CYP128
CYP130
CYP51
Cytochrome P-450 Enzyme Inhibitors
Cytochrome P-450 Enzyme System - genetics
Cytochrome P-450 Enzyme System - metabolism
Cytochrome P450
FprA
Genomics
Models, Molecular
Mycobacterium tuberculosis
Mycobacterium tuberculosis - enzymology
Oxidation-Reduction
Phylogeny
Protein Conformation
Proteomics
Sulfolipid
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Tuberculosis remains a leading cause of human mortality. The emergence of strains of Mycobacterium tuberculosis, the causative agent, that are resistant to the major frontline antitubercular drugs increases the urgency for the development of new therapeutic agents. Sequencing of the M. tuberculosis genome revealed the existence of 20 cytochrome P450 enzymes, some of which are potential candidates for drug targeting. The recent burst of studies reporting microarray-based gene essentiality and transcriptome analyses under in vitro, ex vivo and in vivo conditions highlight the importance of selected P450 isoforms for M. tuberculosis viability and pathogenicity. Current knowledge of the structural and biochemical properties of the M. tuberculosis P450 enzymes and their putative redox partners is reviewed, with an emphasis on findings related to their physiological function(s) as well as their potential as drug targets.
ISSN:0003-9861
1096-0384
DOI:10.1016/j.abb.2009.07.011