2-Chloro-2-phenylethylamine as a mechanistic probe and active site-directed inhibitor of monoamine oxidase from bovine liver mitochondria.

doi:10.1016/0003-9861(87)90408-5

Paper

2-Chloro-2-phenylethylamine as a mechanistic probe and active site-directed inhibitor of monoamine oxidase from bovine liver mitochondria.

Published Jun 1, 1987 · W. Weyler

Archives of biochemistry and biophysics

Q1 SJR score

5

Citations

0

Influential Citations

Full textSemantic Scholar

Abstract

Abstract hidden due to publisher request; this does not indicate any issues with the research. Click the full text link above to read the abstract and view the original source.

In Vitro Study

Study Snapshot

2-chloro-2-phenylethylamine or its oxidation product 2-chloro-2-phenylacetaldehyde may serve as an active site affinity reagent for monoamine oxidase, affecting its enzyme activity under both aerobic and anaerobic conditions.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

Sign up to use Study Snapshot

Consensus is limited without an account. Create an account or sign in to get more searches and use the Study Snapshot.

Create an account

Paper

2-Chloro-2-phenylethylamine as a mechanistic probe and active site-directed inhibitor of monoamine oxidase from bovine liver mitochondria.

Sign up to use Study Snapshot

References

1-Phenylcyclobutylamine, the first in a new class of monoamine oxidase inactivators. Further evidence for a radical intermediate.

1-Phenylcyclobutylamine (PCBA) is a time-dependent inactivator of monoamine oxidase (MAO) and supports a radical mechanism for MAO-catalyzed amine oxidations.

Purification and properties of mitochondrial monoamine oxidase type A from human placenta.

This study presents a high-yield purification method for human placental monoamine oxidase A, resulting in a 90% catalytically active enzyme with a subunit molecular mass of 60-64 kDa.

Resolution of the flavocytochrome p-cresol methylhydroxylase into subunits and reconstitution of the enzyme.

The improved procedure for separating flavocytochrome p-cresol methylhydroxylase subunits and reassembling the enzyme allows for complete recovery of catalytic activity and stoichiometric reconstitution.

Mechanism of inactivation of monoamine oxidase by 1-phenylcyclopropylamine.

1-PCPA is a mechanism-based inactivator of mitochondrial monoamine oxidase, with two different pathways leading to irreversible inactivation and a covalent reversible adduct.

Bovine serum amine oxidase: a mammalian enzyme having covalently bound PQQ as prosthetic group

Bovine plasma amine oxidase has a covalently bound pyrroloquinoline quinone (PQQ) as a prosthetic group, making it the first quinoprotein oxidoreductase discovered in a eukaryotic organism.

Citations

Functional expression of C-terminally truncated human monoamine oxidase type A in Saccharomyces cerevisiae.

The hydrophobic behavior of human monoamine oxidase type A is due to more complex features than a single transmembrane anchor, and truncation of the C-terminus does not significantly affect solubility properties.

Inhibition of monoamine oxidase by the R and S enantiomers of N[3-(2,4-dichlorophenoxy)propyl]-N-methyl-3-butyn-2-amine

The R and S enantiomers of N[3-(2,4-dichlorophenoxy)propyl]-N-methyl-3-butyn-2-amine are reversible, linearly-competitive inhibitors of monoamine oxidase-A and -B,

Biochemistry and genetics of monoamine oxidase.

Monoamine oxidase (MAO) plays a crucial role in human development, aging, and disease, with its biochemistry and genetics being crucial for understanding its role.