| Type | cofactor | Description | Can act both with Mn(2+) and Mg(2+) as cofactor in vitro, but Mn(2+) is the preferred cofactor in vivo. The polymerase activity incorporates correct dNTPs with much higher efficiency with Mn(2+) than with Mg(2+). The fidelity is slightly more accurate when Mg(2+) is the cofactor compared to Mn(2+). In the presence of Mn(2+), a conformational transition step from non-productive to productive PRIMPOL:DNA complexes limits the enzymatic turnover, whereas in the presence of Mg(2+), the chemical step becomes rate limiting. |
