
doi: 10.1007/bf00215581
pmid: 6287206
Various DNA glycosylases exist, which initiate the first step in base-excision repair. A summary of the kinetic and physical characteristics of three classes of DNA glycosylases are presented here. The first class discussed, include glycosylases which recognize alkylated DNA. Various data from enzymes derived from both prokaryotic and eukaryotic sources is discussed. The second class deals with a glycosylase that recognizes and initiates the excision of pyrimidine dimers in DNA. To date, this enzyme has only been uncovered from two sources, Micrococcus luteus and the T4 bacteriophage of E. coli. The third class consists of the most studied of the glycosylases, the uracil-DNA glycosylase enzymes. Various characteristics are presented for the uracil-DNA glycosylases derived from various sources. Recent information from our laboratory is presented implicating that herpes simplex virus may mediate a uracil-DNA glycosylase activity in productivity infected cells.
Deoxyribonucleases, Chemical Phenomena, DNA Repair, Endonucleases, Deoxyribonuclease IV (Phage T4-Induced), DNA Glycosylases, Micrococcus, Chemistry, Kinetics, Pyrimidine Dimers, DNA-(Apurinic or Apyrimidinic Site) Lyase, Simplexvirus, T-Phages, Uracil, Uracil-DNA Glycosidase, N-Glycosyl Hydrolases
Deoxyribonucleases, Chemical Phenomena, DNA Repair, Endonucleases, Deoxyribonuclease IV (Phage T4-Induced), DNA Glycosylases, Micrococcus, Chemistry, Kinetics, Pyrimidine Dimers, DNA-(Apurinic or Apyrimidinic Site) Lyase, Simplexvirus, T-Phages, Uracil, Uracil-DNA Glycosidase, N-Glycosyl Hydrolases
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