Inhibition of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine metabolic activity of porcine FAD-containing monooxygenase by selective monoamine oxidase-B inhibitors

Ru Feng Wu; Yoshiyuki Ichikawa

doi:10.1016/0014-5793(94)01412-T

Inhibition of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine metabolic activity of porcine FAD-containing monooxygenase by selective monoamine oxidase-B inhibitors

Ru Feng Wu, Yoshiyuki Ichikawa

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	145-148
Number of pages	4
Journal	FEBS Letters
Volume	358
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(94)01412-T
State	Published - Jan 23 1995

Keywords

Deprenyl
FAD-containing monooxygenase
Monoamine oxidase-B inhibitor
Pargyline

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(94)01412-T

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title = "Inhibition of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine metabolic activity of porcine FAD-containing monooxygenase by selective monoamine oxidase-B inhibitors",

abstract = "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 Ki and Km 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.",

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T1 - Inhibition of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine metabolic activity of porcine FAD-containing monooxygenase by selective monoamine oxidase-B inhibitors

AU - Wu, Ru Feng

AU - Ichikawa, Yoshiyuki

PY - 1995/1/23

Y1 - 1995/1/23

N2 - 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 Ki and Km 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.

AB - 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 Ki and Km 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.

KW - Deprenyl

KW - FAD-containing monooxygenase

KW - Monoamine oxidase-B inhibitor

KW - Pargyline

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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

Abstract

Keywords

ASJC Scopus subject areas

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