Berman-Kurtz M, Lin E C, Richey D P
J Bacteriol. 1971 Jun;106(3):724-31. doi: 10.1128/jb.106.3.724-731.1971.
A glycerol-specific phenotypic revertant isolated from a mutant of Escherichia coli missing enzyme I of the phosphoenolpyruvate phosphotransferase system was studied. This revertant is capable of producing higher levels of glycerol kinase and the protein mediating the facilitated diffusion of glycerol (facilitator) than wild-type cells. The kinase of the revertant is indistinguishable from the wild-type enzyme with respect to its sensitivity to feedback inhibition by fructose-1,6-diphosphate, its pH optimum, and its turnover number. The synthesis of glycerol kinase in strains bearing the suppressor locus is resistant to catabolite repression. The suppressor mutation mapped at the known glpK locus. Thus, it is suggested that the mutation occurred in the promoter of the operon specifying the kinase and the facilitator.
对从大肠杆菌磷酸烯醇丙酮酸磷酸转移酶系统缺失酶I的突变体中分离出的甘油特异性表型回复突变体进行了研究。该回复突变体能够产生比野生型细胞更高水平的甘油激酶和介导甘油易化扩散的蛋白质（促进剂）。就其对1,6-二磷酸果糖反馈抑制的敏感性、最适pH值和周转数而言，回复突变体的激酶与野生型酶没有区别。携带抑制基因座的菌株中甘油激酶的合成对分解代谢物阻遏具有抗性。抑制基因突变定位于已知的glpK基因座。因此，有人认为该突变发生在指定激酶和促进剂的操纵子的启动子中。
