Old J M, Jones D S
Biochem J. 1976 Dec 1;159(3):503-11. doi: 10.1042/bj1590503.
Several amino acid analogues that are able to replace amino acid residues in binding positions of the biologically active C-terminal tetrapeptide amide sequence, Trp-Met-Asp-PheNH2, of the gastrins were examined for their ability to inhibit the aminoacylation of tRNA in an Escherichia coli and rat liver system. Although in both systems the amino acid side chains are involved in the recognition process, the structural requirements of the side chain in the two systems are not comparable. Analogues of methionine and phenylalanine behaved similarly in the E. coli and rat liver systems, whereas analogues of tryptophan behaved differently. From the results it is possible to suggest structural features of the amino acid side chains which are required for recognition by the aminoacyl-tRNA synthetases.
研究了几种能够取代胃泌素生物活性C末端四肽酰胺序列Trp-Met-Asp-PheNH2结合位置上氨基酸残基的氨基酸类似物,考察它们在大肠杆菌和大鼠肝脏系统中抑制tRNA氨酰化的能力。尽管在这两个系统中氨基酸侧链都参与识别过程,但两个系统中侧链的结构要求并不相同。甲硫氨酸和苯丙氨酸的类似物在大肠杆菌和大鼠肝脏系统中的表现相似,而色氨酸的类似物表现不同。从结果中可以推测出氨酰-tRNA合成酶识别所需的氨基酸侧链的结构特征。