The flavin-containing monooxygenases in rat liver: evidence for the expression of a second form different from FMO1.
A second form of rat liver FMO, FMO-A, was separated and purified by chromatography on Blue Sepharose Fast flow 6. This FMO-A is different from FMO1 by antigenic properties (anti-FMO-A did not cross-react with FMO1, and reciprocally) and by catalytic properties (the Km for trimethylamine was 3.8 microM and 141.4 microM for FMO-A and FMO1, respectively; the Km for imipramine was 536 microM and 17.4 microM for FMO-A and FMO1, respectively). Furthermore, N-terminal amino sequencing revealed differences in the primary structure of these two FMOs although they both contained the highly conserved FAD-binding domain (Gly-X-Gly-X-X-Gly).
Moroni
P
P
Unité de Toxicologie Métabolique et d'Ecotoxicologie (INRA-DGER), Marcy l'Etoile, France.
Longin-Sauvageon
C
C
Benoit
E
E
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D003429:Cross Reactions; D015870:Gene Expression; D007120:Immunochemistry; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010105:Oxygenases / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats; D013379:Substrate Specificity
D007527:Isoenzymes; D010105:Oxygenases; C020066:dimethylaniline monooxygenase (N-oxide forming)