Exclusive activation of aromatic amines in the marine mussel Mytilus edulis by FAD-containing monooxygenase.
Microsomes from the marine mussel Mytilus edulis possess the enzyme activity that selectively metabolizes primary aromatic amines and not polycyclic aromatic hydrocarbons. This activity is NADPH-dependent and has a pH optimum at 8.4. By these characteristics this enzyme is identical with the purified pig liver FAD-containing monooxygenase (EC 1.14.13.8, dimethylaniline monooxygenase). The exposure of mussels to Diesel-2 oil does not induce the enzyme activity. These results are discussed in terms of possible ecological and environmental significance.
D000588:Amines / Q000378:metabolism*; D000818:Animals; D001564:Benzo(a)pyrene / Q000494:pharmacology; D049872:Bivalvia / Q000201:enzymology*; D004064:Digestive System / Q000201:enzymology; D005648:Fuel Oils; D006863:Hydrogen-Ion Concentration; D008861:Microsomes / Q000201:enzymology; D008862:Microsomes, Liver / Q000201:enzymology; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000378:metabolism*
D000588:Amines; D005648:Fuel Oils; D001564:Benzo(a)pyrene; D009249:NADP; D010105:Oxygenases; C020066:dimethylaniline monooxygenase (N-oxide forming)