Summary
2008, Vol. 40, No. 3, Pages 427-446

Structural Biology and Biochemistry of Cytochrome P450 Systems in Mycobacterium tuberculosis

Kirsty J. McLean and Andrew W. Munro
Manchester Interdisciplinary Biocentre, The University of Manchester, Faculty of Life Sciences, Manchester, M1, 7DN, UK

Manchester Interdisciplinary Biocentre, The University of Manchester, Faculty of Life Sciences, 131 Princess Street, Manchester, M1, 7DN, UK



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.

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Authors:
Kirsty J. McLean
Andrew W. Munro
Keywords:
Mycobacterium tuberculosis
Cytochrome P450
Azole drugs
Antitubercular therapy
Protein structure
Enzyme mechanism.