John R A, Jones E D, Fowler L J
Biochem J. 1979 Feb 1;177(2):721-8. doi: 10.1042/bj1770721.
The reactions of two analogues of 4-aminobutyrate, namely 4-aminohex-5-ynoate and 4-aminohex-5-enoate, with three transaminases were studied. Three pure enzymes were used, aminobutyrate transaminase (EC 2.6.1.19), ornithine transaminase (EC 2.6.1.13) and aspartate transaminase (EC 2.6.1.1), and the course of the reactions was studied by observing changes in the absorption spectrum of the bound coenzyme and by observing loss of activity. All of the enzymes were inactivated by either inhibitor, but amino-hexenoate showed a marked specificity for aminobutyrate transaminase. Aminohexynoate was most potent towards ornithine transaminase, and with this enzyme transamination of the inhibitor is an important factor in protecting the enzyme. Most of the reactions could be analysed as first order, with the observed rate constant showing a hyperbolic dependence on inhibitor concentration.
研究了4-氨基丁酸的两种类似物,即4-氨基己-5-炔酸酯和4-氨基己-5-烯酸酯与三种转氨酶的反应。使用了三种纯酶,即氨基丁酸转氨酶(EC 2.6.1.19)、鸟氨酸转氨酶(EC 2.6.1.13)和天冬氨酸转氨酶(EC 2.6.1.1),通过观察结合辅酶吸收光谱的变化以及观察活性丧失来研究反应过程。两种抑制剂都会使所有酶失活,但氨基己烯酸酯对氨基丁酸转氨酶表现出明显的特异性。氨基己炔酸酯对鸟氨酸转氨酶的作用最强,对于这种酶,抑制剂的转氨作用是保护酶的一个重要因素。大多数反应可以分析为一级反应,观察到的速率常数对抑制剂浓度呈双曲线依赖性。