5-Substituted Pyrimidine and 7-Substituted 7-Deazapurine dNTPs as Substrates for DNA Polymerases in Competitive Primer Extension in the Presence of Natural dNTPs

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F16%3A00469259" target="_blank" >RIV/61388963:_____/16:00469259 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/16:10330187
Result on the web
<a href="http://pubs.acs.org/doi/full/10.1021/acschembio.6b00714" target="_blank" >http://pubs.acs.org/doi/full/10.1021/acschembio.6b00714</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acschembio.6b00714" target="_blank" >10.1021/acschembio.6b00714</a>

Result language
angličtina
Original language name
5-Substituted Pyrimidine and 7-Substituted 7-Deazapurine dNTPs as Substrates for DNA Polymerases in Competitive Primer Extension in the Presence of Natural dNTPs
Original language description
A complete series of 5-substituted uracil or cytosine, as well as 7-substituted 7-deazaadenine and 7-deazaguanine 2'-deoxyribonucleoside triphosphates (dNTPs) bearing substituents of increasing bulkiness (H, Me, vinyl, ethynyl, and phenyl) were systematically studied in competitive primer extension in the presence of their natural counterparts (nonmodified dNTPs), and their kinetic data were determined. The results show that modified dNTPs bearing, pi-electron containing substituents (vinyl, ethynyl, Ph) are typically excellent substrates for DNA polymerases comparable to or better than natural dNTPs. The kinetic studies revealed that these modified dNTPs have higher affinity to the active site of the enzyme primer template complex, and the calculations (semiempirical quantum mechanical scoring function) suggest that it is due to the cation-pi interaction of the modified dNTP with Arg629 in the active site of Bst DNA polymerase.
Czech name
—
Czech description
—

Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10608 - Biochemistry and molecular biology

Project
<a href="/en/project/GA14-04289S" target="_blank" >GA14-04289S: Modifications and bioorthogonal reactions in the major groove of DNA for regulation of protein binding and gene expression</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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