Oxidation of dimethylamine and trimethylamine in methazotrophic yeasts by microsomal mono-oxygenases sensitive to carbon monoxide.
Whole cells of Candida boidinii grown on di- or tri-methylamine as sole nitrogen source readily oxidized both amines. The oxidation was potently inhibited by carbon monoxide. Cell-free extracts required the presence of 20 microM FAD before mono-oxygenase activity with both amines could be demonstrated. NADH was a better electron donor than NADPH. Activity was present in cells grown on secondary and tertiary amines but not on primary amines, and was detected in a number of different yeasts. Enzyme activity could be sedimented at 187 000 x g, and was associated with NADPH-cytochrome c reductase activity. It is thus probably microsomal. Activity was inhibited by cyanide, mercaptoethanol, carbon monoxide and proadifen hydrochloride (SKF 525-A).
D002175:Candida / Q000201:enzymology*; D002248:Carbon Monoxide / Q000494:pharmacology*; D004123:Dimethylamines / Q000378:metabolism*; D008744:Methylamines / Q000378:metabolism*; D008861:Microsomes / Q000201:enzymology; D009243:NAD / Q000378:metabolism; D010084:Oxidation-Reduction / Q000187:drug effects; D010105:Oxygenases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013045:Species Specificity
D004123:Dimethylamines; D008744:Methylamines; D009243:NAD; D002248:Carbon Monoxide; C034516:dimethylamine; C027451:methylamine; D010105:Oxygenases; C023336:trimethylamine