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Assimilatory reduction of trimethylamine N-oxide in the yeast Sporopachydermia cereana
Authors:David Whitfield  Peter J Large
Institution:(1) Department of Biochemistry, University of Hull, HU6 7RX Hull, UK;(2) Present address: Biology Division, Chemical Defence Establishment, Porton Down, SP4 0JQ Salisbury, Wilts, UK
Abstract:Summary Washed microsomal preparations (100 000 xg sediment) from the yeast Sporopachydermia cereana that had been grown on trimethylamine N-oxide as sole nitrogen source catalysed the NAD(P)H-dependent reduction of trimethylamine N-oxide to trimethylamine. Under anaerobic conditions, this was the sole reaction product, but under aerobic conditions only small amounts of trimethylamine accumulated, most being further metabolized to methylamine and formaldehyde (no detectable dimenthylamine accumulated due to its rapid turnover). In the absence of NAD(P)H, no formation of amines or formaldehyde from trimethylamine N-oxide was detected. The trimethylamine N-oxide reductase activity was inhibited by quinacrine, Cu2+ ions, triethylamine N-oxide (apparent K i 0.43 mM) and dimethyl sulphoxide (K i 0.94 mM). Chlorate and nitrate failed to inhibit the enzyme. The K m for trimethylamine N-oxide was 29 mgrM. Triethylamine N-oxide was also reduced by the microsomal preparation with the formation of acetaldehyde, and this reduction was sensitive to the same inhibitors as trimethylamine N-oxide, suggesting that both amine oxides are metabolized by the same enzyme(s). It is concluded that trimethylamine N-oxide is metabolized in this yeast via an NAD(P)H-dependent reductase.Abbreviations TMAO triemthylamine N-oxide
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