Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia phage RB69 | P04415 | - |
- |
Tequatrovirus T4 | P04415 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Tequatrovirus T4 |
- |
Escherichia phage RB69 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
deoxynucleoside triphosphate + DNAn | bacteriohage T4 and bacteriophage RB69 replicative DNA polymerases exhibit differing abilities to form various base pairs. Formation of Watson-Crick base pairs occurs at similar rates between the two proteins but the incoming nucleotides are bound less tightly by RB69 DNA polymerase. Incorporation of an A opposite furan by T4 DNA polymerase is more rapid than for RB69 DNA polymerase with the two proteins having similar binding constants for the incoming dATP. An A:C mismatch is formed almost equally well by both proteins, while a significant difference exists when a T:T mismatch is formed | Tequatrovirus T4 | diphosphate + DNAn+1 | - |
? | |
deoxynucleoside triphosphate + DNAn | bacteriohage T4 and bacteriophage RB69 replicative DNA polymerases exhibit differing abilities to form various base pairs. Formation of Watson-Crick base pairs occurs at similar rates between the two proteins but the incoming nucleotides are bound less tightly by RB69 DNA polymerase. Incorporation of an A opposite furan by T4 DNA polymerase is more rapid than for RB69 DNA polymerase with the two proteins having similar binding constants for the incoming dATP. An A:C mismatch is formed almost equally well by both proteins, while a significant difference exists when a T:T mismatch is formed | Escherichia phage RB69 | diphosphate + DNAn+1 | - |
? |