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http://purl.uniprot.org/citations/10455197http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10455197http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10455197http://www.w3.org/2000/01/rdf-schema#comment"The 3' --> 5' exonuclease activity of proofreading DNA polymerases requires two divalent metal ions, metal ions A and B. Mutational studies of the 3' --> 5' exonuclease active center of the bacteriophage T4 DNA polymerase indicate that residue Asp-324, which binds metal ion A, is the single most important residue for the hydrolysis reaction. In the absence of a nonenzymatic source of hydroxide ions, an alanine substitution for residue Asp-324 reduced exonuclease activity 10-100-fold more than alanine substitutions for the other metal-binding residues, Asp-112 and Asp-219. Thus, exonuclease activity is reduced 10(5)-fold for the D324A-DNA polymerase compared with the wild-type enzyme, while decreases of 10(3)- to 10(4)-fold are detected for the D219A- and D112A/E114A-DNA polymerases, respectively. Our results are consistent with the proposal that a water molecule, coordinated by metal ion A, forms a metal-hydroxide ion that is oriented to attack the phosphodiester bond at the site of cleavage. Residues Glu-114 and Lys-299 may assist the reaction by lowering the pK(a) of the metal ion-A coordinated water molecule, whereas residue Tyr-320 may help to reorient the DNA from the binding conformation to the catalytically active conformation."xsd:string
http://purl.uniprot.org/citations/10455197http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.35.25151"xsd:string
http://purl.uniprot.org/citations/10455197http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.35.25151"xsd:string
http://purl.uniprot.org/citations/10455197http://purl.uniprot.org/core/author"Elisseeva E."xsd:string
http://purl.uniprot.org/citations/10455197http://purl.uniprot.org/core/author"Elisseeva E."xsd:string
http://purl.uniprot.org/citations/10455197http://purl.uniprot.org/core/author"Mandal S.S."xsd:string
http://purl.uniprot.org/citations/10455197http://purl.uniprot.org/core/author"Mandal S.S."xsd:string
http://purl.uniprot.org/citations/10455197http://purl.uniprot.org/core/author"Reha-Krantz L.J."xsd:string
http://purl.uniprot.org/citations/10455197http://purl.uniprot.org/core/author"Reha-Krantz L.J."xsd:string
http://purl.uniprot.org/citations/10455197http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10455197http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10455197http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10455197http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10455197http://purl.uniprot.org/core/pages"25151-25158"xsd:string
http://purl.uniprot.org/citations/10455197http://purl.uniprot.org/core/pages"25151-25158"xsd:string
http://purl.uniprot.org/citations/10455197http://purl.uniprot.org/core/title"Mutational and pH studies of the 3' --> 5' exonuclease activity of bacteriophage T4 DNA polymerase."xsd:string
http://purl.uniprot.org/citations/10455197http://purl.uniprot.org/core/title"Mutational and pH studies of the 3' --> 5' exonuclease activity of bacteriophage T4 DNA polymerase."xsd:string
http://purl.uniprot.org/citations/10455197http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/10455197http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/10455197http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10455197
http://purl.uniprot.org/citations/10455197http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10455197
http://purl.uniprot.org/citations/10455197http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10455197
http://purl.uniprot.org/citations/10455197http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10455197