Epstein W, Whitelaw V, Hesse J
J Biol Chem. 1978 Oct 10;253(19):6666-8.
A K+ -stimulated ATPase in membranes of Escherichia coli has been identified as an activity of the Kdp system, and ATP-driven K+ transport system. Three characteristics support association of the ATPase with the Kdp system: (i) ATPase and Kdp transport are both repressed by growth in media containing high concentrations of K+; (ii) the ATPase and Kdp system accept only K+ as substrate, neither requires Na+ nor accepts Rb+ as a substrate; (iii) the affinity of the ATPase and that of th Kdp system for K+ is similar and is altered by mutations in the structural genes of the Kdp system. Discovery of an ATPase associated with a bacterial transport system suggests functional similarities with the ATP-driven transport systems of animal cells.
大肠杆菌膜中的一种钾离子刺激型ATP酶已被确定为Kdp系统的一种活性，即一种由ATP驱动的钾离子转运系统。有三个特征支持该ATP酶与Kdp系统相关联：（i）在含有高浓度钾离子的培养基中生长时，ATP酶活性和Kdp转运都会受到抑制；（ii）该ATP酶和Kdp系统都只接受钾离子作为底物，既不需要钠离子，也不接受铷离子作为底物；（iii）该ATP酶与Kdp系统对钾离子的亲和力相似，并且会因Kdp系统结构基因的突变而改变。与细菌转运系统相关的ATP酶的发现表明，它与动物细胞中由ATP驱动的转运系统在功能上具有相似性。
