Structural, thermodynamic, and kinetic basis for the activities of some nucleic acid repair enzymes
- 17 May 2011
- journal article
- review article
- Published by Wiley in Journal of Molecular Recognition
- Vol. 24 (4) , 656-677
Abstract
X‐ray structural analysis provides no quantitative estimate of the relative contribution of specific and nonspecific or strong and weak interactions to the total affinity of enzymes for nucleic acids. We have shown that the interaction between enzymes and long nucleic acids at the molecular level can be successfully analyzed by the method of stepwise increase in ligand complexity (SILC). In the present review we summarize our studies of human uracil DNA glycosylase and apurinic/apyrimidinic endonuclease, E. coli 8‐oxoguanine DNA glycosylase and RecA protein using the SILC approach. The relative contribution of structural (X‐ray analysis data), thermodynamic, and catalytic factors to the discrimination of specific and nonspecific DNA by these enzymes at the stages of complex formation, the following changes in DNA and enzyme conformations and especially the catalysis of the reactions is discussed. Copyright © 2011 John Wiley & Sons, Ltd.Keywords
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