Oxidation of β‐Phenylethylamine by Both Types of Monoamine Oxidase: Examination of Enzymes in Brain and Liver Mitochondria of Eight Species

  title={Oxidation of $\beta$‐Phenylethylamine by Both Types of Monoamine Oxidase: Examination of Enzymes in Brain and Liver Mitochondria of Eight Species},
  author={Osamu Suzuki and Yoshinao Katsumata and Masakazu Oya},
  journal={Journal of Neurochemistry},
Abstract: β‐Phenylethylamine (PEA) was characterized as a substrate for type A and type B monoamine oxidase (MAO) in brain and liver mitochondria of eight species at different substrate concentrations. In all species, at 10.0 μM, PEA was almost specific for type B MAO. At 1000 μM, however, the amine was common for both types of MAO in rat brain and liver, human brain and liver, mouse brain, guinea pig brain and liver, and bovine brain, while it was specific for type B MAO in mouse liver, rabbit… 

The deamination of dopamine by human brain monoamine oxidase

Enzyme titration studies and comparisons of the substrate specificities of MAO-A andMAO-B across the brain indicated that dopamine was metabolised by the same MAO active centres as other monoamines.

Enzyme properties of monoamine oxidase in the frontal cortex and liver of the gerbil (Meriones unguiculatus).

The Metabolism of Dopamine by Both Forms of Monoamine Oxidase in the Rat Brain and Its Inhibition by Cimoxatone

The activity of MAO‐A was lower in old rats than in young rats, and the same degree of decrease was found for 5‐hydroxy‐tryptamine as for dopamine as substrates for this enzyme form.

Monoamine oxidase: from genes to behavior.

MAO A and B knock-out mice are valuable models for investigating the role of monoamines in psychoses and neurodegenerative and stress-related disorders and show increased reactivity to stress.

MDL 72145, an Enzyme‐Activated Irreversible Inhibitor with Selectivity for Monoamine Oxidase Type B

In vitro, the compound displayed time‐dependent pseudo‐first‐order irreversible inhibitory characteristics with high selectivity for the B form of rat brain mitochondrial MAO and selective protection against inactivation of the two forms of MAO by MDL 72145 was obtained by preincu‐bating the enzyme with suitable concentrations of the selective A and B substrates.

Selective Inhibition by Monoamine Oxidase (MAO) Inhibitors of the Iodotyrosine Formation Induced by MAO Substrates in Bovine Thyroid Tissue

Monoamine oxidase (EC (MAO) may probably be involved in the hydrogen peroxide generation required for the iodination process in the thyroid tissue and was observed that rat thyroid MAO activity was increased by TSH administration and reduced after hypophysectomy.

Inhibition of monoamine oxidase modulates the behaviour of semicarbazide-sensitive amine oxidase (SSAO)

Findings suggest a link between SSAO and cellular stress and may have importance in the context of the recent finding that tissue-SSAO is identical to a vascular adhesion protein (VAP1), involved in the process of inflammation.

Regional Inhibition of Monoamine Oxidase Activity by Administration of Clorgyline in Rat Brain

The MAO‐inhibiting effect of clorgyline administered intraperitoneally was unevenly distributed in the discrete brain nuclei and the regional difference depended upon the dose and the duration of the clorGYline administration.



Beta-phenylethylamine: a specific substrate for type B monoamine oxidase of brain.

  • H. Y. YangN. Neff
  • Chemistry, Biology
    The Journal of pharmacology and experimental therapeutics
  • 1973
It is concluded that the amines of brain may be cataboblized by specific types of monoamine oxidase in vivo.

The reaction of bovine and rat liver monoamine oxidase with [14C]-clorgyline and [14C]-deprenyl.

Highly purified monoamine oxidase from beef and rat liver has been compared with regard to the presence of A and B type enzymes and stoichiometrically bound pargyline is bound to the beef enzyme in amounts in considerable stoichiometric excess indicating nonspecific binding.