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Literature summary for 2.7.7.7 extracted from

  • Jarosz, D.F.; Godoy, V.G.; Delaney, J.C.; Essigmann, J.M.; Walker, G.C.
    A single amino acid governs enhanced activity of DinB DNA polymerases on damaged templates (2006), Nature, 439, 225-228.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
F12A mutant enzyme shows disproportionately reduced activity on the damaged template Escherichia coli
F13V mutant enzyme is almost unable to carry out translesion synthesis over N2-furfuryl-dG, although its activity on undamaged DNA is unaffected. The F13V mutation has a modest effect on the ability of DinB to discriminate against ribonucleotides, increasing the frequency of their misincorporation from less than 0.00001 to 0.001 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNAn wild-type DinB inserts deoxycytidine opposite N2-furfuryl-dG with 10–15fold greater catalytic proficiency than opposite undamaged dG Escherichia coli diphosphate + DNAn+1
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Synonyms

Synonyms Comment Organism
DinB DNA polymerase
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Escherichia coli
DNA polymerase IV
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Escherichia coli