1-Benzylcyclopropylamine and 1-(Phenylcyclopropyl)methylamine: An Inactivator and a Substrate of Monoamine Oxidase

Richard B Silverman, Paul A. Zieske

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

1-Benzylcyclopropylamine (1) and 1-(phenylcyclopropyl)methylamine (2), cyclopropane analogues of phenethylamine, were tested as inactivators for monoamine oxidase (MAO). Compound 1 is a potent competitive reversible inhibitor of the oxidation of benzylamine and also is a mechanism-based inactivator. It requires 2.3 equiv of 1 to inactivate 1 equiv of MAO. The excess equivalents of 1 are converted into benzyl vinyl ketone. A one-electron mechanism of inactivation is proposed. Compound 2 is a substrate for MAO and is converted into 1-phenylcyclopropanecarboxaldehyde without inactivation of the enzyme. Mechanistic consequences are discussed as a result of this observation.

Original languageEnglish (US)
Pages (from-to)1953-1957
Number of pages5
JournalJournal of Medicinal Chemistry
Volume28
Issue number12
DOIs
StatePublished - Jan 1 1985

Fingerprint

Monoamine Oxidase
Ketones
Electrons
Enzymes
1-benzylcyclopropylamine
1-(phenylcyclopropyl)methylamine

ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery

Cite this

@article{c351eb3bccc1477782efdb2e26cf1b3e,
title = "1-Benzylcyclopropylamine and 1-(Phenylcyclopropyl)methylamine: An Inactivator and a Substrate of Monoamine Oxidase",
abstract = "1-Benzylcyclopropylamine (1) and 1-(phenylcyclopropyl)methylamine (2), cyclopropane analogues of phenethylamine, were tested as inactivators for monoamine oxidase (MAO). Compound 1 is a potent competitive reversible inhibitor of the oxidation of benzylamine and also is a mechanism-based inactivator. It requires 2.3 equiv of 1 to inactivate 1 equiv of MAO. The excess equivalents of 1 are converted into benzyl vinyl ketone. A one-electron mechanism of inactivation is proposed. Compound 2 is a substrate for MAO and is converted into 1-phenylcyclopropanecarboxaldehyde without inactivation of the enzyme. Mechanistic consequences are discussed as a result of this observation.",
author = "Silverman, {Richard B} and Zieske, {Paul A.}",
year = "1985",
month = "1",
day = "1",
doi = "10.1021/jm00150a033",
language = "English (US)",
volume = "28",
pages = "1953--1957",
journal = "Journal of Medicinal Chemistry",
issn = "0022-2623",
publisher = "American Chemical Society",
number = "12",

}

1-Benzylcyclopropylamine and 1-(Phenylcyclopropyl)methylamine : An Inactivator and a Substrate of Monoamine Oxidase. / Silverman, Richard B; Zieske, Paul A.

In: Journal of Medicinal Chemistry, Vol. 28, No. 12, 01.01.1985, p. 1953-1957.

Research output: Contribution to journalArticle

TY - JOUR

T1 - 1-Benzylcyclopropylamine and 1-(Phenylcyclopropyl)methylamine

T2 - An Inactivator and a Substrate of Monoamine Oxidase

AU - Silverman, Richard B

AU - Zieske, Paul A.

PY - 1985/1/1

Y1 - 1985/1/1

N2 - 1-Benzylcyclopropylamine (1) and 1-(phenylcyclopropyl)methylamine (2), cyclopropane analogues of phenethylamine, were tested as inactivators for monoamine oxidase (MAO). Compound 1 is a potent competitive reversible inhibitor of the oxidation of benzylamine and also is a mechanism-based inactivator. It requires 2.3 equiv of 1 to inactivate 1 equiv of MAO. The excess equivalents of 1 are converted into benzyl vinyl ketone. A one-electron mechanism of inactivation is proposed. Compound 2 is a substrate for MAO and is converted into 1-phenylcyclopropanecarboxaldehyde without inactivation of the enzyme. Mechanistic consequences are discussed as a result of this observation.

AB - 1-Benzylcyclopropylamine (1) and 1-(phenylcyclopropyl)methylamine (2), cyclopropane analogues of phenethylamine, were tested as inactivators for monoamine oxidase (MAO). Compound 1 is a potent competitive reversible inhibitor of the oxidation of benzylamine and also is a mechanism-based inactivator. It requires 2.3 equiv of 1 to inactivate 1 equiv of MAO. The excess equivalents of 1 are converted into benzyl vinyl ketone. A one-electron mechanism of inactivation is proposed. Compound 2 is a substrate for MAO and is converted into 1-phenylcyclopropanecarboxaldehyde without inactivation of the enzyme. Mechanistic consequences are discussed as a result of this observation.

UR - http://www.scopus.com/inward/record.url?scp=0022411891&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022411891&partnerID=8YFLogxK

U2 - 10.1021/jm00150a033

DO - 10.1021/jm00150a033

M3 - Article

C2 - 4068012

AN - SCOPUS:0022411891

VL - 28

SP - 1953

EP - 1957

JO - Journal of Medicinal Chemistry

JF - Journal of Medicinal Chemistry

SN - 0022-2623

IS - 12

ER -