0469259 - ÚOCHB 2017 RIV US eng J - Článek v odborném periodiku
Cahová, Hana - Panattoni, Alessandro - Kielkowski, Pavel - Fanfrlík, Jindřich - Hocek, Michal
5-Substituted Pyrimidine and 7-Substituted 7-Deazapurine dNTPs as Substrates for DNA Polymerases in Competitive Primer Extension in the Presence of Natural dNTPs.
ACS Chemical Biology. Roč. 11, č. 11 (2016), s. 3165-3171. ISSN 1554-8929. E-ISSN 1554-8937
Grant CEP: GA ČR GA14-04289S
GRANT EU: European Commission(XE) 642023 - ClickGene
Institucionální podpora: RVO:61388963
Klíčová slova: enzymatic synthesis * 2'-deoxyribonucleoside triphosphates * restriction endonucleases
Obor OECD: Biochemistry and molecular biology
Impakt faktor: 4.995, rok: 2016
Způsob publikování: Open access
http://pubs.acs.org/doi/full/10.1021/acschembio.6b00714

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.
Trvalý link: http://hdl.handle.net/11104/0267059