Structural biology and biochemistry of cytochrome P450 systems in Mycobacterium tuberculosis

Kirsty J. McLean, Andrew W. Munro

    Research output: Contribution to journalArticlepeer-review


    The global spread of tuberculosis (TB) has been fuelled by the development of strains of the causative bacterium (Mycobacterium tuberculosis, Mtb) that are resistant to all the leading drugs. New TB therapies are desperately needed, but recent genome sequence, genetic and protein characterization studies have helped identify novel Mtb drug targets and key biochemical pathways for strategic intervention. Of particular interest are the multiple cytochrome P450 (P450) enzymes encoded in the Mtb genome. Structural, biochemical and mechanistic studies on these systems have demonstrated their potential as antitubercular targets, as well as revealing novel aspects of P450 form and function. Copyright © Informa UK, Ltd.
    Original languageEnglish
    Pages (from-to)427-446
    Number of pages19
    JournalDrug Metabolism Reviews
    Issue number3
    Publication statusPublished - Jul 2008


    • Antitubercular therapy
    • Azole drugs
    • Cytochrome P450
    • Enzyme mechanism
    • Mycobacterium tuberculosis
    • Protein structure


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