含铜兵豆（Lens culinaris）幼苗胺氧化酶的瞬态动力学
Transient kinetics of copper-containing lentil (Lens culinaris) seedling amine oxidase.
作者信息
Bellelli A, Brunori M, Finazzi-Agró A, Floris G, Giartosi A, Rinaldi A
出版信息
Biochem J. 1985 Dec 15;232(3):923-6. doi: 10.1042/bj2320923.
The reaction between lentil (Lens culinaris) seedling amine oxidase and its chromogenic substrate, p-dimethylaminomethylbenzylamine, has been studied by the stopped-flow technique. Upon being mixed with substrate in the absence of oxygen, the enzyme is bleached in a complex kinetic process. A yellow intermediate absorbing at 464 nm and the first product (aldehyde) are formed in subsequent steps. When oxygenated buffer is mixed with substrate-reduced amine oxidase, the 496 nm absorption of the oxidized enzyme is very rapidly restored in a second-order process (k = 2.5 X 10(7) M-1 X S-1). This reaction is appreciable even at very low oxygen concentration, in keeping with the fairly low Km for O2 measured by steady-state kinetics.
利用停流技术研究了小扁豆（Lens culinaris）幼苗胺氧化酶与其显色底物对二甲氨基甲基苄胺之间的反应。在无氧条件下与底物混合时，酶在一个复杂的动力学过程中被漂白。在随后的步骤中形成了在464nm处有吸收的黄色中间体和第一种产物（醛）。当将充氧缓冲液与底物还原的胺氧化酶混合时，氧化酶在496nm处的吸收在二级反应过程中非常迅速地恢复（k = 2.5×10⁷ M⁻¹×s⁻¹）。即使在非常低的氧气浓度下，该反应也很明显，这与通过稳态动力学测得的O₂的相当低的Km值一致。
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