Staphylococcal Nuclease: Size and Specificity of the Active Site
Staphylococcal Nuclease: Size and Specificity of the Active Site
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葡萄球菌核酸酶：活性位点的大小和特异性
DOI：
10.1126/science.162.3861.1491
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发表时间：
1968
期刊：
影响因子：
56.9
通讯作者：
C. Anfinsen
中科院分区：
文献类型：
--
作者：
P. Cuatrecasas;M. Wilchek;C. Anfinsen
用葡萄球菌核酸酶和一系列链长不断增加的5'-磷酸化寡胸苷基衍生物测定的解离常数和络合物形成的标准自由能表明，含有三个核苷酸单位的寡核苷酸达到最大的稳定性。一个活性位点的模型包含了该酶的特异性和催化机制的其他知识，假设存在三个不相等的磷酸结合亚位点和一个密切相关的磷酸二酯水解亚位点。
The dissociation constants and standard free energies of complex formation determined with staphylococcal nuclease and a series of 5'-phosphoryloligothymidyl derivatives of increasing chain length suggest that maximum stability is reached with an oligonucleotide containing three nucleotide units. A proposed model of the active site that contains other knowledge of the specificity and the catalytic mechanism of this enzyme postulates the existence of three nonequivalent phosphate binding subsites and a closely related phosphodiester hydrolytic subsite.