Abstract
DNA polymerase I enzymes have served as model systems to study the mechanism of template-directed DNA polymerization. This process requires that the enzyme cycles through a series of conformational changes, each cycle leading to the incorporation of a nucleotide to the primer strand of the DNA. The kinetics of nucleotide incorporation has been extensively studied leading to the definition of specific steps along the cycle. Efforts to visualize these steps using X-ray crystallography have recently come to fruition, notably for one particular DNA polymerase I system, that of Klentaq1. This review focuses on the structural characterization of the various steps along the nucleotide incorporation pathway.
Keywords: Klentaq1 DNA Polymerase, Thermus aquaticus, DNTP, deoxynucleoside-5-triphosphate, 5-fluorosulfonyladenosine, NUCLEOTIDYL TRANSFER, REVERSE TRANSITION, PYROPHOSPHATE, Two-metal-ion, TRANSLOCATION, NUCLEOTIDE SELECTIVITY
Call for Papers in Thematic Issues
Catalytic C-H bond activation as a tool for functionalization of heterocycles
The major topic is the functionalization of heterocycles through catalyzed C-H bond activation. The strategies based on C-H activation not only provide straightforward formation of C-C or C-X bonds but, more importantly, allow for the avoidance of pre-functionalization of one or two of the cross-coupling partners. The beneficial impact of ...read more
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