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Lookup NU author(s): Dr David Jamieson,
Professor Alan Boddy
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NRH:Quinone Oxidoreductase 2 (NQO2) has been described as having no enzymatic activity with nicotinamide adenine dinucleotide (NADH) or NADPH as electron donating cosubstrates. Mitomycin C (MMC) is both a substrate for and a mechanistic inhibitor of the NQO2 homologue NQO1. NRH:quinone oxidoreductase 2 catalysed the reduction of MMC at pH 5.8 with NADH as a co-factor. This reaction results in species that inhibit the NQO2-mediated metabolism of CB1954. In addition, MMC caused an increase in DNA cross-links in a cell line transfected to overexpress NQO2 to an extent comparable to that observed with an isogenic NQO1-expressing cell line. These data indicate that NQO2 may contribute to the metabolism of MMC to cytotoxic species. © 2006 Cancer Research UK.
Author(s): Jamieson, D., Tung, A., Knox, R., Boddy, A.
Publication type: Article
Publication status: Published
Journal: British Journal of Cancer
Print publication date: 06/11/2006
ISSN (print): 0007-0920
ISSN (electronic): 1532-1827
PubMed id: 17031400
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