Elucidation of activation mechanism of human acetyl-CoA carboxylase

为了阐明催化脂肪酸生物合成限速步骤的乙酰辅酶a羧化酶（ACC）的激活机制，我们对人类ACC的中心结构域（hBCCP1、hBCCP2）及其活化酶生物素蛋白连接酶（hBPL）进行了蛋白质晶体学研究。利用大肠杆菌合成了这些基因并进行了大规模表达。这些蛋白通常以包涵体形式表达，不能通过变性/重折叠和用丙氨酸取代半胱氨酸等方法溶解。

Toward the elucidation of the activation mechanism of acetyl-CoA carboxylase (ACC) that catalyzes the rate-limiting step of the fatty-acid biosynthesis, we tried the protein crystallography of the central domain of human ACC (hBCCP1, hBCCP2) and its activation enzyme biotin protein ligase (hBPL). The genes were synthesized for a large-scale expression using E.coli. These proteins were generally expressed as inclusion bodies that could not be solubilized by methods including the denaturation/refolding and the substitution of cysteine with alanine.