title: Structural, thermodynamic, and kinetic basis for the activities of some nucleic acid repair enzymes.
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.
authors.affiliation: Institute of Chemical Biology and Fundamental Medicine, Siberian Division of Russian Academy of Sciences, Novosibirsk 63009, Russia. nevinsky@niboch.nsc.ru
authors.forename: Georgy A
authors.initials: GA
authors.lastname: Nevinsky
mesh_terms: D045647:DNA Glycosylases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D045643:DNA Repair Enzymes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D011938:Rec A Recombinases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013816:Thermodynamics; D051981:Uracil-DNA Glycosidase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D011938:Rec A Recombinases; D045647:DNA Glycosylases; D051981:Uracil-DNA Glycosidase; C479058:oxoguanine glycosylase 1, human; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase; D045643:DNA Repair Enzymes