"2"^^ . . . . "B Family DNA Polymerases Asymmetrically Recognize Pyrimidines and Purines" . . . "We utilized a series of modified pyrimidine analogues to determine the mechanism used by human DNA polymerase \u03B1 and herpes simplex virus I DNA polymerase to polymerize pyrimidine dNTPs. Removing O2 of a pyrimidine dNTP vastly decreased incorporation by these enzymes and also compromised fidelity in the case of C analogues, while removing O2 from the templating base had more modest effects. Removing the Watson-Crick hydrogen bonding groups greatly impaired polymerization. The Watson-Crick hydrogen bonding plays an important role in enhancing correct dNTP polymerization, but are not essential for preventing misincorporation. These studies also indicate that DNA polymerases recognize bases extremely asymmetrically, both in terms of whether they are a purine or pyrimidine and whether they are in the template or are the incoming dNTP. The mechanistic implications of these results regarding how polymerases discriminate between right and wrong dNTPs are discussed."@en . . "Lund, T. J." . . "Kuchta, R. D." . "Urban, M." . "RIV/61388963:_____/11:00364221!RIV12-AV0-61388963" . . . "RIV/61388963:_____/11:00364221" . "Cavanaugh, N. A." . "Patro, J. N." . "active-site tightness; genetic alphabet; deoxynucleoside; phosphoramidites"@en . . "Hocek, Michal" . "Biochemistry" . "B Family DNA Polymerases Asymmetrically Recognize Pyrimidines and Purines" . . "[F1F268603062]" . "B Family DNA Polymerases Asymmetrically Recognize Pyrimidines and Purines"@en . "P(IAA400550902), P(LC512), Z(AV0Z40550506)" . . . "10.1021/bi2006916" . "7"^^ . "50" . . . "B Family DNA Polymerases Asymmetrically Recognize Pyrimidines and Purines"@en . "Joubert, Nicolas" . "000294076100018" . "33" . "0006-2960" . "US - Spojen\u00E9 st\u00E1ty americk\u00E9" . . . "We utilized a series of modified pyrimidine analogues to determine the mechanism used by human DNA polymerase \u03B1 and herpes simplex virus I DNA polymerase to polymerize pyrimidine dNTPs. Removing O2 of a pyrimidine dNTP vastly decreased incorporation by these enzymes and also compromised fidelity in the case of C analogues, while removing O2 from the templating base had more modest effects. Removing the Watson-Crick hydrogen bonding groups greatly impaired polymerization. The Watson-Crick hydrogen bonding plays an important role in enhancing correct dNTP polymerization, but are not essential for preventing misincorporation. These studies also indicate that DNA polymerases recognize bases extremely asymmetrically, both in terms of whether they are a purine or pyrimidine and whether they are in the template or are the incoming dNTP. The mechanistic implications of these results regarding how polymerases discriminate between right and wrong dNTPs are discussed." . "187728" . "Joubert, Nicolas" . . "8"^^ . . .