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Literature summary for 4.2.99.18 extracted from

  • Schmiedel, R.; Kuettner, E.B.; Keim, A.; Straeter, N.; Greiner-Stoeffele, T.
    Structure and function of the abasic site specificity pocket of an AP endonuclease from Archaeoglobus fulgidus (2009), DNA Repair, 8, 219-231.
    View publication on PubMed

Application

Application Comment Organism
biotechnology is frequently used in gene technology due to its strong exonucleolytic activity Archaeoglobus fulgidus

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Archaeoglobus fulgidus

Crystallization (Commentary)

Crystallization (Comment) Organism
V217G variant is crystallized with decamer dsDNA molecule, and the three-dimensional structure is determined to 1.7 A resolution Archaeoglobus fulgidus

Protein Variants

Protein Variants Comment Organism
F200S site-directed mutagenesis, by expanding the size of the binding pocket the unspecific endonucleolytic activity is increased Archaeoglobus fulgidus
F200S/W215S site-directed mutagenesis, by expanding the size of the binding pocket the unspecific endonucleolytic activity is increased Archaeoglobus fulgidus
V217G site-directed mutagenesis, by expanding the size of the binding pocket the unspecific endonucleolytic activity is increased Archaeoglobus fulgidus
W215S site-directed mutagenesis, by expanding the size of the binding pocket the unspecific endonucleolytic activity is increased Archaeoglobus fulgidus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Archaeoglobus fulgidus

Organism

Organism UniProt Comment Textmining
Archaeoglobus fulgidus O29675
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Archaeoglobus fulgidus

Synonyms

Synonyms Comment Organism
AP endonuclease exonuclease III (ExoIII) Archaeoglobus fulgidus
apurinic/apyrimidinic endonuclease
-
Archaeoglobus fulgidus