The process is a dynamic interaction between the protein, the DNA substrate, and the incoming nucleoside triphosphate. This oxygen atom attacks the alpha-phosphate of the incoming dNTP, displacing the beta and gamma phosphates as pyrophosphate.
Acid-Base Balance During Nucleotide Addition
This enzyme does not act randomly; it reads the existing strand and selects only those building blocks that can form correct base pairs. Concurrently, a proton is released, maintaining the acid-base balance of the immediate environment.
The palm domain of the enzyme closes around the reacting groups, creating an environment that excludes water. The result is the formation of a phosphodiester bond that links the new nucleotide to the chain.
Acid-Base Balance During Nucleotide Addition and Its Role in Fidelity
It enters the exonuclease active site, where the mismatched bond is hydrolytically cleaved. The enzyme scans the template strand and assesses whether an incoming deoxynucleoside triphosphate, or dNTP, can form the correct hydrogen bonds.
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