Conway T, Osman Y A, Konnan J I, Hoffmann E M, Ingram L O
J Bacteriol. 1987 Mar;169(3):949-54. doi: 10.1128/jb.169.3.949-954.1987.
DNA sequence analysis showed that pyruvate decarboxylase (one of the most abundant proteins in Zymomonas mobilis) contains 559 amino acids. The promoter for the gene encoding pyruvate decarboxylase was not recognized by Escherichia coli, although the cloned gene was expressed at relatively high levels under the control of alternative promoters. The promoter region did not contain sequences which could be identified as being homologous to the generalized promoter structure for E. coli. Hydropathy plots for the amino acid sequence indicated that pyruvate decarboxylase contains a large number of hydrophobic domains which may contribute to the thermal stability of this enzyme.
DNA序列分析表明,丙酮酸脱羧酶(运动发酵单胞菌中最丰富的蛋白质之一)含有559个氨基酸。尽管克隆的基因在替代启动子的控制下以相对较高的水平表达,但编码丙酮酸脱羧酶的基因启动子未被大肠杆菌识别。该启动子区域不包含可被鉴定为与大肠杆菌通用启动子结构同源的序列。氨基酸序列的亲水性图谱表明,丙酮酸脱羧酶含有大量疏水结构域,这可能有助于该酶的热稳定性。