title: Endonuclease V: an unusual enzyme for repair of DNA deamination.
abstract: Endonuclease V (endo V) was first discovered as the fifth endonuclease in Escherichia coli in 1977 and later rediscovered as a deoxyinosine 3' endonuclease. Decades of biochemical and genetic investigations have accumulated rich information on its role as a DNA repair enzyme for the removal of deaminated bases. Structural and biochemical analyses have offered invaluable insights on its recognition capacity, catalytic mechanism, and multitude of enzymatic activities. The roles of endo V in genome maintenance have been validated in both prokaryotic and eukaryotic organisms. The ubiquitous nature of endo V in the three domains of life: Bacteria, Archaea, and Eukaryotes, indicates its existence in the early evolutionary stage of cellular life. The application of endo V in mutation detection and DNA manipulation underscores its value beyond cellular DNA repair. This review is intended to provide a comprehensive account of the historic aspects, biochemical, structural biological, genetic and biotechnological studies of this unusual DNA repair enzyme.
authors.affiliation: Department of Genetics and Biochemistry, South Carolina Experiment Station, Clemson University, Room 049 Life Science Building, 190 Collings Street, Clemson, SC, 29634, USA. wgc@clemson.edu
authors.forename: Weiguo
authors.initials: W
authors.lastname: Cao
mesh_terms: D000818:Animals; D004260:DNA Repair; D003641:Deamination; D043224:Deoxyribonuclease (Pyrimidine Dimer) / Q000378:metabolism*; D006801:Humans
chemical_list: D043224:Deoxyribonuclease (Pyrimidine Dimer)