| pubmed-article:2198936 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2198936 | lifeskim:mentions | umls-concept:C0079870 | lld:lifeskim |
| pubmed-article:2198936 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:2198936 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:2198936 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:2198936 | lifeskim:mentions | umls-concept:C0525039 | lld:lifeskim |
| pubmed-article:2198936 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:2198936 | lifeskim:mentions | umls-concept:C0206415 | lld:lifeskim |
| pubmed-article:2198936 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:2198936 | pubmed:dateCreated | 1990-9-11 | lld:pubmed |
| pubmed-article:2198936 | pubmed:abstractText | By site-directed mutagenesis using synthetic oligonucleotides, amino acid residues 181Phe-Arg-Arg183 of recombinant rat DNA polymerase beta were replaced by other amino acids to clarify the roles of these residues in the DNA synthesizing reaction. Replacement of Phe-181 by alanine reduced the enzyme activity only 30%. Replacement of Arg-182 by alanine and glutamine resulted in reduction of the activity by about 67% and 95%, respectively. The Arg-182----Gln replacement increased the binding strength to single-stranded DNA but did not significantly change the Km's for the primer and dTTP, suggesting that Arg-182 is involved in modulation of binding to the template rather than to the primer or deoxyribonucleoside triphosphate. Replacement of Arg-183 by Gln resulted in reduction of the activity by about 95%, and this change, although causing little change in binding strength to single-stranded DNA, resulted in a 3-4-fold increase in the Km's for the primer and deoxyribonucleoside triphosphate. A more dramatic change was observed when Arg-183 was replaced by Ala, which resulted in a 99.98% reduction of enzyme activity. Although the Km for deoxyribonucleoside triphosphate of this mutant enzyme was hardly changed, that for the primer increased 159-fold. Therefore, it is concluded that Arg-183 occupies an important part of the primer recognition site of DNA polymerase beta. | lld:pubmed |
| pubmed-article:2198936 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2198936 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2198936 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2198936 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2198936 | pubmed:month | May | lld:pubmed |
| pubmed-article:2198936 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:2198936 | pubmed:author | pubmed-author:DateTT | lld:pubmed |
| pubmed-article:2198936 | pubmed:author | pubmed-author:YamamotoSS | lld:pubmed |
| pubmed-article:2198936 | pubmed:author | pubmed-author:MatsukageAA | lld:pubmed |
| pubmed-article:2198936 | pubmed:author | pubmed-author:NishimotoYY | lld:pubmed |
| pubmed-article:2198936 | pubmed:author | pubmed-author:LiuNN | lld:pubmed |
| pubmed-article:2198936 | pubmed:author | pubmed-author:TaniharaKK | lld:pubmed |
| pubmed-article:2198936 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2198936 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:2198936 | pubmed:volume | 29 | lld:pubmed |
| pubmed-article:2198936 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2198936 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2198936 | pubmed:pagination | 5027-34 | lld:pubmed |
| pubmed-article:2198936 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:2198936 | pubmed:meshHeading | pubmed-meshheading:2198936-... | lld:pubmed |
| pubmed-article:2198936 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2198936 | pubmed:articleTitle | Site-directed mutagenesis of recombinant rat DNA polymerase beta: involvement of arginine-183 in primer recognition. | lld:pubmed |
| pubmed-article:2198936 | pubmed:affiliation | Department of Biochemistry, Kanazawa Medical University, Ishikawa, Japan. | lld:pubmed |
| pubmed-article:2198936 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2198936 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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