Shiloach J, Bauer S, de Groot N, Lapidot Y
Nucleic Acids Res. 1975 Oct;2(10):1941-50. doi: 10.1093/nar/2.10.1941.
The dependence of the Vmax and Km on the length of the peptide moiety in the peptidyl-tRNA series (Gly)n-Val tRNA, was measured in the system peptidyl-tRNA hydrolase-peptidyl-tRNA. It was found that the Km value decreases from 7.2 X 10-7 M for Gly-Val-tRNA to 4.6 X 10-7 M FOR (Gly)2-Val-tRNA and to 1.7 X 10-7M for (Gly)3-Val-tRNA; further increase of the peptide chain is not followed by decrease of the Km. The Vmax values are 5.7 pmole/min/EU for Gly-Val-tRNA and 42 pmole/min/EU for (Gly)3-Val-tRNA. The enzyme activity is inhibited competitively by uncharged tRNA with a KI value of about 10-5M. The significance of these results described in this paper, in relation to the fact that peptides and peptide esters do not inhibit the enzyme activity, and in relation to the proposed physiological role of the enzyme, is discussed.
在肽基 - tRNA水解酶 - 肽基 - tRNA系统中,测定了Vmax和Km对肽基 - tRNA系列(Gly)n - Val tRNA中肽部分长度的依赖性。结果发现,Km值从Gly - Val - tRNA的7.2×10 - 7M降至(Gly)2 - Val - tRNA的4.6×10 - 7M,再降至(Gly)3 - Val - tRNA的1.7×10 - 7M;肽链进一步延长,Km值并未下降。Gly - Val - tRNA的Vmax值为5.7皮摩尔/分钟/酶活力单位,(Gly)3 - Val - tRNA的Vmax值为42皮摩尔/分钟/酶活力单位。无电荷的tRNA对该酶活性有竞争性抑制作用,其KI值约为10 - 5M。本文讨论了这些结果的意义,涉及到肽和肽酯不抑制酶活性这一事实,以及该酶拟议的生理作用。