Hofsteenge J, Vicentini A, Zelenko O
Friedrich Miescher Institute, Basel, Switzerland.
Cell Mol Life Sci. 1998 Aug;54(8):804-10. doi: 10.1007/s000180050209.
The structural and enzymatic properties of RNase 4 are reviewed. This RNase shows a much higher interspecies similarity (approximately 90%) than the other members of the RNase A superfamily. The enzyme is ubiquitous, with the highest amounts present in liver and lung. Its unique uridine specificity results from alterations in and around the pyrimidine-binding site. In particular, the shortened C-terminus and the side chains of Phe-42, Asp-80 and Arg-101 appear to be involved. RNase 4 binds tightly to the intracellular RNase inhibitor, with a Kd of 4 x 10(-15) M.
本文综述了核糖核酸酶4(RNase 4)的结构和酶学特性。与核糖核酸酶A超家族的其他成员相比,这种核糖核酸酶表现出更高的种间相似性(约90%)。该酶广泛存在,在肝脏和肺中含量最高。其独特的尿苷特异性源于嘧啶结合位点及其周围的改变。特别是,缩短的C末端以及苯丙氨酸-42、天冬氨酸-80和精氨酸-101的侧链似乎与之有关。RNase 4与细胞内核糖核酸酶抑制剂紧密结合,解离常数(Kd)为4×10⁻¹⁵ M。