Merck

Structure and mechanism of DNA polymerase β.

Biochemistry (2014-04-11)
William A Beard, Samuel H Wilson
摘要

DNA polymerase (pol) β is a small eukaryotic DNA polymerase composed of two domains. Each domain contributes an enzymatic activity (DNA synthesis and deoxyribose phosphate lyase) during the repair of simple base lesions. These domains are termed the polymerase and lyase domains, respectively. Pol β has been an excellent model enzyme for studying the nucleotidyl transferase reaction and substrate discrimination at a molecular level. In this review, recent crystallographic studies of pol β in various liganded and conformational states during the insertion of right and wrong nucleotides as well as during the bypass of damaged DNA (apurinic sites and 8-oxoguanine) are described. Structures of these catalytic intermediates provide unexpected insights into mechanisms by which DNA polymerases enhance genome stability. These structures also provide an improved framework that permits computational studies to facilitate the interpretation of detailed kinetic analyses of this model enzyme.

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Sigma-Aldrich
镁, turnings, reagent grade, 98%
Sigma-Aldrich
鸟嘌呤, 98%
Sigma-Aldrich
镁, purum, for Grignard reactions, ≥99.5%, turnings
Supelco
鸟嘌呤, Pharmaceutical Secondary Standard; Certified Reference Material
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鸟嘌呤, BioUltra
Sigma-Aldrich
镁, 20-230 mesh, reagent grade, 98%
Sigma-Aldrich
镁, grit, ≥99.0% (KT)
Sigma-Aldrich
镁, in a Sure/Seal bottle, turnings, 37.5 mmol
Sigma-Aldrich
镁, in a Sure/Seal bottle, turnings, anhydrous tetrahydrofuran 37.5 mmol