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Inhibition of 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine metabolic activity of porcine FAD‐containing monooxygenase by selective monoamine oxidase‐B inhibitors
Author(s) -
Wu Ru-Feng,
Ichikawa Yoshiyuki
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01412-t
Subject(s) - pargyline , monoamine oxidase , chemistry , monooxygenase , stereochemistry , enzyme , monoamine oxidase a , biochemistry , non competitive inhibition , monoamine oxidase b , cytochrome p450
The MPTP metabolic activity of porcine FAD‐containing monooxygenase (FMO) (EC 1.14.13.8) was inhibited considerably by deprenyl and pargyline, selective MAO‐B inhibitors, and they showed typical competitive inhibition. Deprenyl and pargyline, amine derivatives were also examined as to whether they are substrates for the FMO. It was found that deprenyl and pargyline are excellent substrates for the FMO. The K i and K m values of deprenyl and pargyline for the FMO are 14 μM and 9 μM, and 14.3 μM and 11.6 μM, at pH 8.0 and 25°C, respectively.