Vasil'ev V Iu, Krylova E B
Biokhimiia. 1976 Jul;41(6):1044-6.
The analysis of the interaction of ethanolamine-O-sulphate with 4-aminobutyrate transaminase revealed that the inhibitory effect is exerted upon the substrate subsite of the active site of the enzyme in aldimine form. The inhibition in irreversible. The inactivation rate versus pH-curve was shown to have a sigmoid character with inclination point at neutral pH. The study of inhibition kinetics by the Kitz and Wilson method revealed a complex inhibitory pattern compatible with a minimal two-step mechanism. Rate constant of inactivation was found to be equal to 0.22 min-1 and the value of the inhibitory constant--to 1.1-10(-2) M.
乙醇胺 - O - 硫酸盐与4 - 氨基丁酸转氨酶相互作用的分析表明，抑制作用是在醛亚胺形式的酶活性位点的底物亚位点上发挥的。这种抑制是不可逆的。失活速率与pH曲线呈S形，拐点在中性pH处。用基茨和威尔逊方法对抑制动力学的研究揭示了一种与至少两步机制相符的复杂抑制模式。发现失活速率常数等于0.22分钟⁻¹，抑制常数的值为1.1×10⁻² M。
