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Literature summary for 2.7.7.7 extracted from

  • Raper, A.T.; Suo, Z.
    Investigation of intradomain motions of a Y-family DNA polymerase during substrate binding and catalysis (2016), Biochemistry, 55, 5832-5844 .
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q97W02
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Saccharolobus solfataricus ATCC 35092 Q97W02
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn the complex DNA binding mechanism of a Y-family DNA polymerase involves aspects of both induced-fit and conformational selection mechanisms. Intradomain protein motions are observed throughout nucleotide binding and incorporation, some of which may kinetically limit the rate of correct nucleotide incorporation Saccharolobus solfataricus diphosphate + DNAn+1
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?
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn the complex DNA binding mechanism of a Y-family DNA polymerase involves aspects of both induced-fit and conformational selection mechanisms. Intradomain protein motions are observed throughout nucleotide binding and incorporation, some of which may kinetically limit the rate of correct nucleotide incorporation Saccharolobus solfataricus ATCC 35092 diphosphate + DNAn+1
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?

Synonyms

Synonyms Comment Organism
Dpo4
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Saccharolobus solfataricus