Deamination of aliphatic amines of different chain lengths by rat liver monoamine oxidase A and B.

  • Peter Hoifu Yu
  • Published 1989 in The Journal of pharmacy and pharmacology

Abstract

Monoamines with from 1 to 18 straight chain carbon atoms have been analysed as rat liver monoamine oxidase substrates. Methylamine and ethylamine are clearly not substrates of monoamine oxidase (MAO). n-Propylamine, n-butylamine, n-dodecylamine and n-octadecylamine are relatively poor substrates, i.e. with high Km and low Vmax values for the enzyme. n-Pentylamine, n-hexylamine, n-heptylamine, n-octylamine, n-nonylamine and n-decylamine are all very good MAO substrates. All these aliphatic amines are found to be typical type B substrates according to the sensitivities of the enzyme towards the selective MAO-B inhibitor selegiline and the MAO-A inhibitor, clorgyline. The sensitivity towards selegiline with respect to these amines is even higher, i.e. Ki = 1 x 10(-9) M for butylamine, than that of the typical type B substrate beta-phenylethylamine (Ki = 1 x 10(-8) M). The sensitivity towards selegiline decreases slightly with increasing chain length of these aliphatic amines.

Cite this paper

@article{Yu1989DeaminationOA, title={Deamination of aliphatic amines of different chain lengths by rat liver monoamine oxidase A and B.}, author={Peter Hoifu Yu}, journal={The Journal of pharmacy and pharmacology}, year={1989}, volume={41 3}, pages={205-8} }