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Expression of Recombinant Human Flavin Monooxygenase and application for N-oxidation of Moclobemide

Hanlon, Steven and Camattari, Andrea and Abad, Sandra and Glieder, Anton and Kittelmann, Matthias and Luetz, Stephan and Wirz, Beat and Winkler, Margit (2012) Expression of Recombinant Human Flavin Monooxygenase and application for N-oxidation of Moclobemide. Chemical communications. ISSN 1359-7349

Abstract

Rec. h. flavine containing monooxygenases (FMOs), isoforms 1-5, were cloned and expressed in E. coli BL21. Highest activity (methimazole oxidation) of solubilized enzyme was obtained with the FMO3 construct in an NADPH depletion assay. Moclobemide, a MAO-inhibitor marketed by Roche, was applied as the substrate in whole cell biotransformation assays. Citrate and NADP+ were required for effective bioconversion with FMO3 containing E. coli cells. In a whole cell biotransformation on one L scale with rec h FMO3 and 40 mg of moclobemide 81 % conversion to the N-oxide was achieved. The product was isolated from the reaction mixture and its structure confirmed by MS and NMR spectroscopy (poduct isolation and structure elucidation still ongoing).

Item Type: Article
Related URLs:
Additional Information: Collaboration with Roche AG, Basel and TU-Graz in the project "Non-CYP-Metabolizing Enzymes (NCME)" in the frame of the competence centre "ACIB - Austrian Research Centre of Industrial Biotechnology"
Keywords: Flavine containing monooxygenase, heterologous expression, biocatalysis, biotransformation, N-oxidation, moclobemide
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Date Deposited: 13 Oct 2015 13:14
Last Modified: 13 Oct 2015 13:14
URI: https://oak.novartis.com/id/eprint/6282

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