鸟苷酸核糖核酸酶对多核苷酸底物的特异性。

Specificity of guanylic RNases to polynucleotide substrates.

作者信息

Both V, Moiseyev G P, Sevcik J

机构信息

Institute of Molecular Biology of the Slovak Academy of Sciences, Bratislava, Czechoslovakia.

出版信息

Biochem Biophys Res Commun. 1991 Jun 14;177(2):630-5. doi: 10.1016/0006-291x(91)91835-z.

DOI:10.1016/0006-291x(91)91835-z

Abstract

Kinetic parameters kcat and KM were measured for cleavage of poly I, poly A, poly U, poly C and poly I poly C by guanyl-specific RNases Sa, Pb1 and T1 and compared with that of guanyl-preferential RNase Bi. Catalytic efficiencies of the investigated enzymes to polynucleotide substrates vary considerably. The structural basis for specificity of these RNases is discussed. A hypothesis is suggested that Ser-56 plays an important role in recognition of poly A by RNase Bi.

摘要

测定了鸟嘌呤特异性核糖核酸酶Sa、Pb1和T1切割多聚I、多聚A、多聚U、多聚C和多聚I-多聚C的动力学参数kcat和KM，并与鸟嘌呤优先核糖核酸酶Bi进行了比较。所研究的酶对多核苷酸底物的催化效率差异很大。讨论了这些核糖核酸酶特异性的结构基础。提出了一个假说，即Ser-56在核糖核酸酶Bi识别多聚A中起重要作用。

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