Structural, thermodynamic, and kinetic basis for the activities of some nucleic acid repair enzymes
Article first published online: 17 MAY 2011
Copyright © 2011 John Wiley & Sons, Ltd.
Journal of Molecular Recognition
Volume 24, Issue 4, pages 656–677, July/August 2011
How to Cite
Nevinsky, G. A. (2011), Structural, thermodynamic, and kinetic basis for the activities of some nucleic acid repair enzymes. J. Mol. Recognit., 24: 656–677. doi: 10.1002/jmr.1096
- Issue published online: 7 APR 2011
- Article first published online: 17 MAY 2011
- Manuscript Revised: 27 AUG 2010
- Manuscript Accepted: 27 AUG 2010
- Manuscript Received: 19 JUL 2010
- mechanism of functioning;
- repair enzymes
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.