氨基烷基腺苷酸与大肠杆菌MRE 600异亮氨酰-tRNA合成酶的结合
On the binding of aminoalkyl adenylates to isoleucyl-tRNA synthetase from Escherichia coli MRE 600.
作者信息
Flossdorf J, Marutzky R, Messer K, Kula M R
出版信息
Nucleic Acids Res. 1977 Mar;4(3):673-83. doi: 10.1093/nar/4.3.673.
Abstract
The binding of nine aminoalkyl adenylates to isoleucyl-tRNA synthetase from Escherichia coli MRE 600 was measured and compared with the binding of the cognate amino acids. It was found that they bind rather tightly to the enzyme, the Kd's ranging from 3.1.10(-4) M with glycinol-AMP ester to 3.7.10(-9) M with L-isoleucinol-AMP ester. The binding is not affected by magnesium. It is shown that the free energies of binding of the esters can be calculated adding a constant contribution of the AMP-moiety of about - 4.1 (- 17) kcal/mole (kJ/mole) to the free energies of binding of the cognate amino acids, which we have reported earlier (19, 25, 26).
摘要
测定了9种氨基烷基腺苷酸与大肠杆菌MRE 600异亮氨酰 - tRNA合成酶的结合情况，并与同源氨基酸的结合进行了比较。发现它们与该酶结合相当紧密，解离常数（Kd）范围从甘氨醇 - AMP酯的3.1×10⁻⁴ M到L - 异亮氨醇 - AMP酯的3.7×10⁻⁹ M。这种结合不受镁的影响。结果表明，通过向我们之前报道的（19, 25, 26）同源氨基酸结合自由能中添加约 - 4.1（ - 17）千卡/摩尔（千焦/摩尔）的AMP部分的恒定贡献，可以计算酯的结合自由能。
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