EC Number |
Natural Substrates |
---|
2.7.7.7 | a 2'-deoxyribonucleoside 5'-triphosphate + DNAn |
- |
2.7.7.7 | a 2'-deoxyribonucleoside 5'-triphosphate + DNAn |
DNA replication can be accomplished using dNDPs as substrates. In thermophiles, genome replication may be less sensitive to the energy charge of the cell than in mesophiles because thermostable polymerases can accept the diphosphorylated as well as the triphosphorylated substrates. DNA replication is thus less affected by the intracellular ATP/ADP ratio, and the relatively high efficiency with which DNA is synthesized at elevated temperatures suggests that thermophiles may be able to dispense with the triphosphorylated substrates entirely |
2.7.7.7 | a 2'-deoxyribonucleoside 5'-triphosphate + DNAn |
the catalytic core of yeast DNA polymerase eta prefers to incorporate dCTP opposite 7,8-dihydro-8-oxo-2'-deoxyguanosine (damage produced by reactive oxygen species in DNA). dCTP incorporation is slower than the dissociation of the polymerase from DNA. 57% of the extension products beyond the 7,8-dihydro-8-oxo-2'-deoxyguanosine are the products corresponding to the correct incorporation (C) and 43% corresponding to dATP misincorporation |
2.7.7.7 | a 2'-deoxyribonucleoside 5'-triphosphate + DNAn |
the template-dependent polymerase that can repair non-complementary DNA double strand breaks with unpaired 3' primer termini by nonhomologous end joining. Its role is to fill short gaps arising as intermediates in the process of V(D)J recombination and during processing of accidental double strand breaks |
2.7.7.7 | deoxynucleoside triphosphate + DNAn |
- |
2.7.7.7 | deoxynucleoside triphosphate + DNAn |
natural substrate is gapped DNA |
2.7.7.7 | deoxynucleoside triphosphate + DNAn |
physiological role of pol I |
2.7.7.7 | deoxynucleoside triphosphate + DNAn |
polymerase I plays a role in repair of chromosomal damage |
2.7.7.7 | deoxynucleoside triphosphate + DNAn |
physiological role of pol I and pol III |
2.7.7.7 | deoxynucleoside triphosphate + DNAn |
overview: functional role of mammalian DNA polymerases |