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Literature summary for 2.7.7.7 extracted from

  • Sherrer, S.M.; Beyer, D.C.; Xia, C.X.; Fowler, J.D.; Suo, Z.
    Kinetic basis of sugar selection by a Y-family DNA polymerase from Sulfolobus solfataricus P2 (2010), Biochemistry, 49, 10179-10186.
    View publication on PubMed
Search for more literature for 2.7.7.7

Protein Variants

Protein Variants Comment Organism
Y12A mutation causes an average increase of 220fold in matched ribonucleotide incorporation efficiency and an average decrease of 9fold in correct deoxyribonucleotide incorporation efficiency, leading to an average reduction of 2000fold in sugar selectivity. The mutant incorporates more than 20 consecutive ribonucleotides into primer/template (DNA/DNA) duplexes, suggesting that this mutant protein possesses both aDNA-dependent DNA polymerase activity and a DNA-dependent RNA polymerase activity Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
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Saccharolobus solfataricus P2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the DNA lesion bypass polymerase can bind up to eight base pairs of double-stranded DNA which is entirely in B-type. Thus, the DNA binding cleft of Dpo4 is flexible and can accommodate both A- and B-type oligodeoxyribonucleotide duplexes as well as damaged DNA Saccharolobus solfataricus ?
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 ?
additional information the DNA lesion bypass polymerase can bind up to eight base pairs of double-stranded DNA which is entirely in B-type. Thus, the DNA binding cleft of Dpo4 is flexible and can accommodate both A- and B-type oligodeoxyribonucleotide duplexes as well as damaged DNA Saccharolobus solfataricus P2 ?
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 ?

Synonyms

Synonyms Comment Organism
DNA polymerase IV
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 Saccharolobus solfataricus
Dpo4
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 Saccharolobus solfataricus