Summary
This is the second of a series of four articles in which the chemical, enzymological and crystallographic work on Ribonucleate (deoxyribonucleate)-3′-nucleotidohydrolase EC 3.1.4.4 (staphylococcal nuclease, micrococcal nuclease) will be reviewed and correlated. This article discusses studies in solution delineating the extent of the binding site of the enzyme and identifying some of the particular amino acid residues that form this site. In addition, the effects of the very potent inhibitory combination of thymidine-3′,5′-diphosphate and Ca2+ on the conformation of the enzyme and its physical, chemical and enzymological properties will be reviewed.
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This article is the second of a series of four which provide a comprehensive review of the biochemistry of the staphylococcal nuclease. Part I (1) presented the details of its isolation and enzymology. Part III, in the next issue of this journal, will continue with a review of the three-dimensional structure and mechanism of enzyme action. Part IV will discuss polypeptide chain folding. Work from this laboratory has been supported by grants from the National Institute of General Medical Sciences and the Robert A. Welch Foundation to F. A. Cotton and E. E. Hazen, Jr.
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Tucker, P.W., Hazen, E.E. & Cotton, F.A. Staphylococcal nuclease reviewed: A Prototypic study in contemporary enzymology. II. Solution studies of the nucleotide binding site and the effects of nucleotide binding.. Mol Cell Biochem 23, 3–16 (1979). https://doi.org/10.1007/BF00226675
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DOI: https://doi.org/10.1007/BF00226675