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Literature summary for 2.7.7.7 extracted from

  • Fiala, K.A.; Hypes, C.D.; Suo, Z.
    Mechanism of abasic lesion bypass catalyzed by a Y-family DNA polymerase (2007), J. Biol. Chem., 282, 8188-8198.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q97W02
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Saccharolobus solfataricus P2 Q97W02
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNAn while showing efficient bypass, the enzyme pauses when incorporating nucleotides directly opposite and one position downstream from an abasic lesion because of a drop of several orders of magnitude in catalytic efficiency. Biphasic kinetics for incorporation indicating that Dpo4 primarily forms a nonproductive complex with DNA that converts slowly to a productive complex. These strong pause sites are mutational hot spots with the embedded lesion even affecting the efficiency of five to six downstream incorporations Saccharolobus solfataricus diphosphate + DNAn+1
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?
deoxynucleoside triphosphate + DNAn while showing efficient bypass, the enzyme pauses when incorporating nucleotides directly opposite and one position downstream from an abasic lesion because of a drop of several orders of magnitude in catalytic efficiency. Biphasic kinetics for incorporation indicating that Dpo4 primarily forms a nonproductive complex with DNA that converts slowly to a productive complex. These strong pause sites are mutational hot spots with the embedded lesion even affecting the efficiency of five to six downstream incorporations Saccharolobus solfataricus P2 diphosphate + DNAn+1
-
?

Synonyms

Synonyms Comment Organism
Dpo4
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Saccharolobus solfataricus