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Literature summary for 2.7.7.7 extracted from

  • Sandalli, C.; Singh, K.; Modak, M.J.
    Characterization of catalytic carboxylate triad in non-replicative DNA polymerase III (pol E) of Geobacillus kaustophilus HTA (2012), Cell. Mol. Biol. (Noisy-le-grand), 58, 44-49.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D378A site-directed mutagenesis, the mutant is inactive in presence of Mg2+ Geobacillus kaustophilus
D378E site-directed mutagenesis, the mutant is inactive in presence of Mg2+, it shows 35% of maximal activity in presenceof Mn2+ Geobacillus kaustophilus
D380A site-directed mutagenesis, the mutant is inactive in presence of Mg2+ Geobacillus kaustophilus
D380E site-directed mutagenesis, the mutant is inactive in presence of Mg2+ or Mn2+ Geobacillus kaustophilus
D531A site-directed mutagenesis, the mutant is inactive in presence of Mg2+ Geobacillus kaustophilus
D531E site-directed mutagenesis, the mutant is inactive in presence of Mg2+, it shows 60% of maximal activity in presenceof Mn2+ Geobacillus kaustophilus
additional information DNA binding, dNTP binding and catalytic activity of mutant enzyme in the presence of two metal ions, Mg2+ and Mn2+, overview Geobacillus kaustophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Geobacillus kaustophilus
Mn2+ activates Geobacillus kaustophilus
additional information DNA binding, dNTP binding and catalytic activity of mutant enzyme in the presence of two metal ions, Mg2+ and Mn2+, overview. Amino acid residues D378 and D531 are mainly responsible for the binding of metal chelated substrate dNTP Geobacillus kaustophilus

Organism

Organism UniProt Comment Textmining
Geobacillus kaustophilus
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-
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Synonyms

Synonyms Comment Organism
non-replicative DNA polymerase III
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Geobacillus kaustophilus
pol E
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Geobacillus kaustophilus

General Information

General Information Comment Organism
malfunction abolished catalytic activity of mutant enzyme in the presence of two metal ions, Mg2+ and Mn2+, overview Geobacillus kaustophilus
additional information three aspartic acid residues D378, D380 and D531 form the catalytic carboxylate triad in pol E. Amino acid residues D378 and D531 are mainly responsible for the binding of metal chelated substrate dNTP, while D380 is solely responsible for the chemical step of phosphodiester bond formation Geobacillus kaustophilus