Zverlov V V, Bankovskiĭ V K, Churikova O V, Mogutov M A, Iur'ev M Z
Mol Gen Mikrobiol Virusol. 1989 Sep(9):11-3.
The pyruvate decarboxylase gene of Zymomonas mobilis CP4 has been cloned in Escherichia coli strain TG1 cells on the pUC18 vector plasmid. Activity of the enzyme in the lysates of the obtained clones is about 30 units per 1 mg of protein. Neither the dependence of the pyruvate decarboxylase activity on the presence of IPTG or glucose in the cultivation medium nor the difference in activity of the enzyme for the clones harbouring the recombinant plasmids with the different orientation of the pyruvate decarboxylase gene to lac-promoter have been demonstrated in the presented work. These facts imply the transcription of pyruvate decarboxylase gene from its own promoter.
运动发酵单胞菌CP4的丙酮酸脱羧酶基因已通过pUC18载体质粒克隆到大肠杆菌TG1细胞中。所得克隆裂解物中该酶的活性约为每1毫克蛋白质30单位。本次研究未证明丙酮酸脱羧酶活性对培养基中IPTG或葡萄糖存在的依赖性,也未证明携带丙酮酸脱羧酶基因与lac启动子方向不同的重组质粒的克隆之间酶活性的差异。这些事实表明丙酮酸脱羧酶基因是从其自身启动子转录的。