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Literature summary for 2.7.7.7 extracted from

  • Fiala, K.A.; Suo, Z.
    Pre-steady-state kinetic studies of the fidelity of Sulfolobus solfataricus P2 DNA polymerase IV (2004), Biochemistry, 43, 2106-2115.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
Dpo4 fused to a C-terminal His6 tag is expressed in Escherichia coli strain BL21(DE3) Saccharolobus solfataricus

Metals/Ions

Metals/Ions Comment Organism Structure
MgCl2 optimal concentration: 5 mM Saccharolobus solfataricus
NaCl optimal concentration: 0-75 mM Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q97W02
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-
Saccharolobus solfataricus P2 Q97W02
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-

Purification (Commentary)

Purification (Comment) Organism
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Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNAn the fidelity of Dpo4 is in the range of 0.001-0.0001. The ground-state binding affinity of correct nucleotides is 10-50-fold weaker than those of replicative DNA polymerases. The affinity of incorrect nucleotides for Dpo4 is about 2-10-fold weaker than that of correct nucleotides. The mismatched dCTP has an affinity similar to that of the matched nucleotides when it is incorporated against a pyrimidine template base flanked by a 5'-template guanine. The mismatch incorporation rates, regardless of the 5'-template base, are about 2-3 orders of magnitude slower than the incorporation rates for matched nucleotides, which is the predominant contribution to the fidelity of Dpo4 Saccharolobus solfataricus diphosphate + DNAn+1
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?
deoxynucleoside triphosphate + DNAn the fidelity of Dpo4 is in the range of 0.001-0.0001. The ground-state binding affinity of correct nucleotides is 10-50-fold weaker than those of replicative DNA polymerases. The affinity of incorrect nucleotides for Dpo4 is about 2-10-fold weaker than that of correct nucleotides. The mismatched dCTP has an affinity similar to that of the matched nucleotides when it is incorporated against a pyrimidine template base flanked by a 5'-template guanine. The mismatch incorporation rates, regardless of the 5'-template base, are about 2-3 orders of magnitude slower than the incorporation rates for matched nucleotides, which is the predominant contribution to the fidelity of Dpo4 Saccharolobus solfataricus P2 diphosphate + DNAn+1
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?

Synonyms

Synonyms Comment Organism
DNA polymerase IV
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Saccharolobus solfataricus
Dpo4
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Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
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-
Saccharolobus solfataricus

pH Range

pH Minimum pH Maximum Comment Organism
7 9 pH 7.0: about 50% of maximal activity, pH 9.0: about 60% of maximal activity Saccharolobus solfataricus