Kinemuchi H, Arai Y, Oreland L, Tipton K F, Fowler C J
Biochem Pharmacol. 1982 Mar 15;31(6):959-64. doi: 10.1016/0006-2952(82)90327-6.
Several reports have suggested that monoamine oxidase activity towards beta-phenethylamine is inhibited by high concentrations of that substrate. This inhibition is not found if initial velocities are measured, but there is a slower time-dependent inhibition at higher beta-phenethylamine concentrations. Such time-dependent inhibition is not found with tyramine as substrate or upon incubation of the enzyme with the reversible inhibitor amphetamine. The inhibition is not due to the accumulation of phenacetaldehyde, phenylethanol or phenacetic acid, or to a reaction of any of these three products either with each other or with beta-phenethylamine. Although the inhibition is time-dependent, the inactivated enzyme slowly regains activity upon removal of the beta-phenethylamine. A model is proposed to explain the observed inhibition.
有几份报告表明，高浓度的β-苯乙胺会抑制单胺氧化酶对β-苯乙胺的活性。如果测量初始速度，则不会发现这种抑制作用，但在较高的β-苯乙胺浓度下会有较慢的时间依赖性抑制作用。以酪胺为底物或用可逆抑制剂苯丙胺孵育酶时，未发现这种时间依赖性抑制作用。这种抑制作用不是由于苯乙酮、苯乙醇或苯乙酸的积累，也不是由于这三种产物中的任何一种相互之间或与β-苯乙胺发生反应。尽管这种抑制作用是时间依赖性的，但去除β-苯乙胺后，失活的酶会缓慢恢复活性。提出了一个模型来解释观察到的抑制作用。
