Ames B N, Ames G F, Young J D, Tsuchiya D, Lecocq J
Proc Natl Acad Sci U S A. 1973 Feb;70(2):456-8. doi: 10.1073/pnas.70.2.456.
The oligopeptide permease of Escherichia coli has been characterized by Payne, Gilvarg, and their colleagues. We have confirmed its existence in Salmonella typhimurium, and have isolated a series of mutants lacking the permease. We use this transport system for smuggling a histidine biosynthetic intermediate, histidinol phosphate ester, into the bacteria as its glycylglycyl derivative, Gly-Gly-histidinol phosphate. Free histidinol phosphate ester is not transported into Salmonella. Several amino-acid analogues are shown to be much more inhibitory to Salmonella when presented to the bacteria in the form of tripeptides than as the free amino acids. The implications of this work for practical purposes are discussed. The synthesis of Gly-Gly-histidinol phosphate is described.
大肠杆菌的寡肽通透酶已由佩恩、吉尔瓦格及其同事进行了表征。我们已证实其在鼠伤寒沙门氏菌中存在,并分离出了一系列缺乏该通透酶的突变体。我们利用这个转运系统,将组氨酸生物合成中间体磷酸组氨醇以其二甘氨酰衍生物甘氨酰 - 甘氨酰 - 磷酸组氨醇的形式偷运进细菌。游离的磷酸组氨醇不会被转运进沙门氏菌。结果表明,几种氨基酸类似物以三肽形式呈现给细菌时,比以游离氨基酸形式呈现时对沙门氏菌的抑制作用要强得多。本文讨论了这项工作在实际应用方面的意义。文中还描述了甘氨酰 - 甘氨酰 - 磷酸组氨醇的合成方法。