A main catalyst human polymerase patch BER Pol · β is short, to be able to compensate for its absence Pol λ. These polymerases is a member of the Pol X family, I insert a single nucleotide usually. In addition to the polymerase activity, these enzymes have a removal lyase domain disadvantages of AP endonuclease cleavage 5 “DRP, by patch BER continuous, DNA synthesis by Pol and δ por ε processing power PCNA index polymerases polymerase. these those for performing DNA replication are thought to be brought to, means that in order to form a flap (shown above), it is the “shift” after the 5 ‘end of the DNA Thus, you can. Pol β has been conducted, the displacement synthesis to perform long patch, displacement synthesis, route BER. long patch synthesis of both can not join to insert a new nucleotide usually 2-10 .

Synthesized DNA molecules from the nucleotide components, DNA polymerase, a viral polymerase enzymes or cells. Is essential for replication of DNA, usually, DNA polymerase, operates a pair of copies of double-stranded DNA molecule of double-stranded DNA of the two in a process called semi-conservative DNA replication. I have an important role in DNA polymerase, and DNA repair through a special DNA polymerase, recombination, generation of diversity of antibodies and reverse transcription, in other processes in the cell that contains the terminal deoxynucleotidyl transferase. DNA polymerases are widely used, especially for molecular cloning polymerase chain reaction (PCR), DNA, and it is used in molecular biology laboratories.

Regardless DNA polymerase known in the domain structure of their total catalytic subunit has a structure that is highly conserved to mean different things very little species from the seed. Form, can be described as similar to the right hand thumb, and palm and finger domains. Palm domain appears to function in catalyzing the transfer of a phosphate group in the phosphoryl transfer reaction. palm DNA enzyme is active. I believed that this reaction to be catalyzed by metal ions two mechanisms. Finger domain functionality, coupling the nucleotide triphosphate to template-based. Thumb domain plays a potential role positioning and movement of DNA, of processing power. Structure conservative, exert important maintenance to provide cells, the evolutionary advantage in general, the essential functions.

The DNA polymerase of rapid catalyst for processive nature. Capacity is characteristic of an enzyme acting on the polymer surface. In the case of DNA polymerase, the degree of processing power, added to each enzyme, which means the average number of nucleotides to bind to the template. DNA polymerase An average requires about one second to find the primer / template junction, to be connected. It is bound once, is added nucleotides at a rate of nucleotides per second nonprocessive DNA polymerase Hatsu. However, 207-208 processor DNA polymerase adds nucleotides of several two-dramatic increase in the rate of DNA synthesis. The degree of processing power is directly proportional to the rate of DNA synthesis.
Ability of DNA polymerase to slide to the DNA template allows the processing power increased. There is a dramatic increase in processing power of the replication fork. This increase is facilitated by the binding of DNA polymerase and a protein known as a sliding clamp DNA. Is a subunit protein of several related to the shape of the clamp ring. Using the hydrolysis of ATP, the class of proteins known as the sliding stress proteins slide clamp ring-opening structure of the bracket, and the coupling to the release of the DNA strand and / or DNA. By Make sure that the enzyme is bound to the same primer / template junction and continue replication, DNA polymerase clamp protein-protein interactions can be used to prevent the spread of DNA matrix. In order to allow the release of the clamp when it is connected to the completion of the replication region of decreased DNA affinity with it, :207-208 DNA polymerase conformational change increases the affinity of the clamp.