Staphylococcal Nuclease: Size and Specificity of the Active Site

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Science  27 Dec 1968:
Vol. 162, Issue 3861, pp. 1491-1493
DOI: 10.1126/science.162.3861.1491


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.

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