Yakovlev G I, Bocharov A L, Moiseyev G P, Mikhaylov S N
FEBS Lett. 1985 Jan 7;179(2):217-20. doi: 10.1016/0014-5793(85)80521-4.
The rate at which dinucleoside phosphates are cleaved by RNases is supposed to be determined by the mole fraction of enzyme-substrate complexes in which the phosphodiester moiety of a dinucleoside phosphate has a highly reactive conformation. The mole fraction of such complexes for a particular RNase depends on the nature of a nucleoside at the O5'-end of the phosphodiester bond. Experimental data are presented to support this hypothesis.
二核苷磷酸被核糖核酸酶裂解的速率被认为取决于酶-底物复合物的摩尔分数，在该复合物中，二核苷磷酸的磷酸二酯部分具有高反应性构象。特定核糖核酸酶的此类复合物的摩尔分数取决于磷酸二酯键O5'-末端核苷的性质。本文提供了实验数据来支持这一假设。
