Kang S, Markovitz A
J Bacteriol. 1967 Jul;94(1):87-91. doi: 10.1128/jb.94.1.87-91.1967.
p-Fluorophenylalanine (FPA) causes a 100-fold increase in alkaline phosphatase in Escherichia coli B, strain PR1 at 30 C in minimal medium that contains excess inorganic phosphate (1.92 x 10(-3)m). Little increase in alkaline phosphatase synthesis occurs under these conditions at 22 C. [This strain is known to have a mutation in a regulator gene (R(2)) that, in the absence of FPA, permits derepression of alkaline phosphatase synthesis at 37 C, but not at 30 C or below.] In contrast, E. coli B3 (the strain from which E. coli B strain PR1 was derived) is not derepressed at 30 C by FPA. (14)C-FPA is incorporated into bacterial proteins. Temperature-shift experiments (30 Cright harpoon over left harpoon22 C) in the presence of FPA are consistent with the following mechanism. FPA is incorporated into the genetically altered R(2) protein at 30 and 22 C. This further alteration due to the incorporation of analogue makes the R(2) protein inactive at 30 C, but active at 22 C.
对氟苯丙氨酸（FPA）在含有过量无机磷酸盐（1.92×10⁻³m）的基本培养基中，于30℃时可使大肠杆菌B菌株PR1的碱性磷酸酶增加100倍。在22℃的这些条件下，碱性磷酸酶合成几乎没有增加。[已知该菌株在调节基因（R₂）中有一个突变，在没有FPA的情况下，允许碱性磷酸酶合成在37℃时去阻遏，但在30℃或更低温度时则不行。]相比之下，大肠杆菌B3（大肠杆菌B菌株PR1的亲本菌株）在30℃时不会因FPA而去阻遏。¹⁴C - FPA被掺入细菌蛋白质中。在FPA存在下进行的温度转换实验（30℃⇌22℃）与以下机制一致。FPA在30℃和22℃时被掺入经基因改变的R₂蛋白中。由于类似物的掺入导致的这种进一步改变，使R₂蛋白在30℃时无活性，但在22℃时有活性。
