Počet záznamů: 1
5-Substituted Pyrimidine and 7-Substituted 7-Deazapurine dNTPs as Substrates for DNA Polymerases in Competitive Primer Extension in the Presence of Natural dNTPs
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SYSNO ASEP 0469259 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název 5-Substituted Pyrimidine and 7-Substituted 7-Deazapurine dNTPs as Substrates for DNA Polymerases in Competitive Primer Extension in the Presence of Natural dNTPs Tvůrce(i) Cahová, Hana (UOCHB-X) RID, ORCID
Panattoni, Alessandro (UOCHB-X) ORCID, RID
Kielkowski, Pavel (UOCHB-X) RID
Fanfrlík, Jindřich (UOCHB-X) RID, ORCID
Hocek, Michal (UOCHB-X) RID, ORCIDZdroj.dok. ACS Chemical Biology. - : American Chemical Society - ISSN 1554-8929
Roč. 11, č. 11 (2016), s. 3165-3171Poč.str. 7 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova enzymatic synthesis ; 2'-deoxyribonucleoside triphosphates ; restriction endonucleases Vědní obor RIV CE - Biochemie Obor OECD Biochemistry and molecular biology CEP GA14-04289S GA ČR - Grantová agentura ČR Způsob publikování Open access Institucionální podpora UOCHB-X - RVO:61388963 UT WOS 000388430100025 EID SCOPUS 84996721494 DOI https://doi.org/10.1021/acschembio.6b00714 Anotace 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. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Rok sběru 2017 Elektronická adresa http://pubs.acs.org/doi/full/10.1021/acschembio.6b00714
Počet záznamů: 1