Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.7.7 extracted from

  • Boudsocq, F.; Kokoska, R.J.; Plosky, B.S.; Vaisman, A.; Ling, H.; Kunkel, T.A.; Yang, W.; Woodgate, R.
    Investigating the role of the little finger domain of Y-family DNA polymerases in low fidelity synthesis and translesion replication (2004), J. Biol. Chem., 279, 32932-32940.
    View publication on PubMed
Search for more literature for 2.7.7.7

Protein Variants

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

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q97W02
-
-
Saccharolobus solfataricus P2 Q97W02
-
-
Sulfolobus acidocaldarius Q4JB80
-
-
Sulfolobus acidocaldarius DSM 639 Q4JB80
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus
-
 Sulfolobus acidocaldarius

Substrates and Products (Substrate)

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

Synonyms Comment Organism
DBH
-
 Sulfolobus acidocaldarius
Dpo4
-
 Saccharolobus solfataricus
Saci_0554
-
 Sulfolobus acidocaldarius

pI Value

Organism Comment pI Value Maximum pI Value
Saccharolobus solfataricus calculated from sequence
-
 9.1
Sulfolobus acidocaldarius calculated from sequence
-
 9.1