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http://purl.uniprot.org/citations/9572863http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9572863http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9572863http://www.w3.org/2000/01/rdf-schema#comment"The amino-terminal 8-kDa domain of vertebrate DNA polymerase beta (pol beta) has an activity to excise deoxyribose phosphate (dRP) groups from 5'-incised apurinic/apyrimidinic (AP) sites during base excision repair. The excision reaction proceeds via a beta-elimination reaction following formation of a Schiff base between an aldehyde group of the AP site and an amino group of the enzyme. Here we report that the Lys-72 residue of this enzyme is the catalytic center for dRP excision. Substitutions of Lys-72 with Arg or Gln reduced the dRP excision activity to less than 1% of the wild-type 8-kDa domain, while substitutions of Lys-35, Lys-68, or Lys-84 did not abolish its activity. The Lys-72 mutations also significantly decreased Schiff base intermediates trapped by reduction with sodium borohydride. The 8-kDa domain alone was able to bind preferentially to a single-nucleotide gap or 5'-incised synthetic AP site on double-stranded DNA. The Lys-72 mutations did not affect this damage-specific DNA binding activity. When introduced into the intact enzyme, a mutation of Lys-72 to Arg did not affect DNA synthesis activity of pol beta, but eliminated the repair activity. Addition of the wild-type 8-kDa domain to this reaction restored the repair activity. These results indicate a specific role of Lys-72 of pol beta in the dRP excision during base excision repair."xsd:string
http://purl.uniprot.org/citations/9572863http://purl.org/dc/terms/identifier"doi:10.1021/bi9727545"xsd:string
http://purl.uniprot.org/citations/9572863http://purl.org/dc/terms/identifier"doi:10.1021/bi9727545"xsd:string
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/author"Kim K."xsd:string
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/author"Kim K."xsd:string
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/author"Matsumoto Y."xsd:string
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/author"Matsumoto Y."xsd:string
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/author"Feng J.-A."xsd:string
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/author"Feng J.-A."xsd:string
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/author"Katz D.S."xsd:string
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/author"Katz D.S."xsd:string
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/pages"6456-6464"xsd:string
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/pages"6456-6464"xsd:string
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/title"Catalytic center of DNA polymerase beta for excision of deoxyribose phosphate groups."xsd:string
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/title"Catalytic center of DNA polymerase beta for excision of deoxyribose phosphate groups."xsd:string
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/volume"37"xsd:string
http://purl.uniprot.org/citations/9572863http://purl.uniprot.org/core/volume"37"xsd:string
http://purl.uniprot.org/citations/9572863http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9572863
http://purl.uniprot.org/citations/9572863http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9572863