Protein Variants | Comment | Organism |
---|---|---|
additional information | generaion of chimeras of Sulfolobus solfataricus DNA polymerase Dpo4 and Sulfolobus acidocaldarius DNA polymerase Dbh in which their little finger domains have been interchanged. Interestingly, by replacing the little finger domain of Dbh with that of Dpo4, the enzymatic properties of the chimeric enzyme are more Dpo4-like in that the enzyme is more processive, can bypass an abasic site and a thymine-thymine cyclobutane pyrimidine dimer, and predominantly makes base pair substitutions when replicating undamaged DNA. The converse is true for the Dpo4-LF-Dbh chimera, which is more Dbh-like in its processivity and ability to bypass DNA adducts and generate single-base deletion errors. The unique but variable little finger domain of Y-family polymerases plays a major role in determining the enzymatic and biological properties of each individual Y-family member | Saccharolobus solfataricus |
additional information | generaion of chimeras of Sulfolobus solfataricus DNA polymerase Dpo4 and Sulfolobus acidocaldarius DNA polymerase Dbh in which their little finger domains have been interchanged. Interestingly, by replacing the little finger domain of Dbh with that of Dpo4, the enzymatic properties of the chimeric enzyme are more Dpo4-like in that the enzyme is more processive, can bypass an abasic site and a thymine-thymine cyclobutane pyrimidine dimer, and predominantly makes base pair substitutions when replicating undamaged DNA. The converse is true for the Dpo4-LF-Dbh chimera, which is more Dbh-like in its processivity and ability to bypass DNA adducts and generate single-base deletion errors. The unique but variable little finger domain of Y-family polymerases plays a major role in determining the enzymatic and biological properties of each individual Y-family member | Sulfolobus acidocaldarius |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharolobus solfataricus | Q97W02 | - |
- |
Saccharolobus solfataricus P2 | Q97W02 | - |
- |
Sulfolobus acidocaldarius | Q4JB80 | - |
- |
Sulfolobus acidocaldarius DSM 639 | Q4JB80 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Saccharolobus solfataricus |
- |
Sulfolobus acidocaldarius |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
deoxynucleoside triphosphate + DNAn | DNA polymerase Dpo4 can replicate past a variety of DNA lesions. When replicating undamaged DNA, the enzyme is prone to make base pair substitutions | Saccharolobus solfataricus | diphosphate + DNAn+1 | - |
? | |
deoxynucleoside triphosphate + DNAn | DNA polymerase Dpo4 can replicate past a variety of DNA lesions. When replicating undamaged DNA, the enzyme is prone to make base pair substitutions | Sulfolobus acidocaldarius | diphosphate + DNAn+1 | - |
? | |
deoxynucleoside triphosphate + DNAn | DNA polymerase Dpo4 can replicate past a variety of DNA lesions. When replicating undamaged DNA, the enzyme is prone to make base pair substitutions | Saccharolobus solfataricus P2 | diphosphate + DNAn+1 | - |
? | |
deoxynucleoside triphosphate + DNAn | DNA polymerase Dpo4 can replicate past a variety of DNA lesions. When replicating undamaged DNA, the enzyme is prone to make base pair substitutions | Sulfolobus acidocaldarius DSM 639 | diphosphate + DNAn+1 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DBH | - |
Sulfolobus acidocaldarius |
Dpo4 | - |
Saccharolobus solfataricus |
Saci_0554 | - |
Sulfolobus acidocaldarius |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Saccharolobus solfataricus | calculated from sequence | - |
9.1 |
Sulfolobus acidocaldarius | calculated from sequence | - |
9.1 |