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羧基酶(ACC)的激活机制，我们尝试了人ACC中央结构域的蛋白质结晶学(hBCCP1，hBCCP2)及其激活酶生物素蛋白连接酶(HBPL)。这些基因是用大肠杆菌合成的，可以大规模表达。这些蛋白通常以包涵体的形式表达，不能通过变性/复性和半胱氨酸替代丙氨酸等方法溶解。

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.