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Literature summary for 3.1.11.2 extracted from

  • Know, Y.W.
    Mechanism of action of Escherichia coli exonuclease III (1989), Biochemistry, 28, 3280-3287.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ sharp optimum requirement at 1 mM for exonucleolytic and endonucleolytic activity Escherichia coli
Mg2+ broad optimum, requirement for exonucleolytic and endonucleolytic activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
double-stranded DNA + H2O recognizes apurinic sites, reduced apurinic sites, urea and O-alkylhydroxylamine residues of PM2 DNA Escherichia coli additional information
-
?
double-stranded DNA + H2O hydrolyzes the phosphodiester bond 5'- to O-alkylhydroxylamine residue Escherichia coli additional information
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
in presence of Mg2+, exonuclease III exists in two temperature-dependent conformations. The transition temperature for the conformation change occurs at 25°C Escherichia coli