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PMID: 423893 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Staphylococcal nuclease reviewed: a prototypic study in contemporary enzymology. II. Solution studies of the nucleotide binding site and the effects of nucleotide binding.

Molecular and cellular biochemistry ·Vol. 23 ·No. 1 ·1979-01-15 ·Pages 3-16

Tucker PW, Hazen EE, Cotton FA

Abstract

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.

MeSH Terms
Binding Sites Calcium/pharmacology Calorimetry Kinetics Micrococcal Nuclease/metabolism Protein Binding Protein Conformation Structure-Activity Relationship Thermodynamics Thymine Nucleotides/pharmacology
Chemicals
Thymine Nucleotides Micrococcal Nuclease Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Tucker P W
Hazen E E
Cotton F A
References (47)
47 references, click to expand
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Article Info
Journal
Molecular and cellular biochemistry
Abbr.
Mol Cell Biochem
ISSN
0300-8177
DOI
10.1007/BF00226675
Published
1979-01-15
Pages
3-16
Language
English
Region
Netherlands
NLM ID
0364456
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00226675 View journal details
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