Exclusive activation of aromatic amines in the marine mussel Mytilus edulis by fad-containing monooxygenase

Microsomes from the marine mussel Mytilusedulis 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...

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Veröffentlicht in:	Biochemical and biophysical research communications 1985-03, Vol.127 (3), p.773-778
1. Verfasser:	Kurelec, Branko
Format:	Artikel
Sprache:	eng
Schlagworte:	Amines - metabolism Animals Applied sciences Benzo(a)pyrene - pharmacology Bivalvia - enzymology Digestive System - enzymology Exact sciences and technology Fuel Oils Hydrogen-Ion Concentration Marine Microsomes - enzymology Microsomes, Liver - enzymology Mytilus edulis NADP - metabolism Other techniques and industries Oxidation-Reduction Oxygenases - metabolism
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Beschreibung
Zusammenfassung:	Microsomes from the marine mussel Mytilusedulis 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.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/S0006-291X(85)80010-3