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Literature summary for 3.2.2.23 extracted from

  • Minetti, C.A.S.A.; Remeta, D.P.; Zharkov, D.O.; Plum, G.E.; Johnson, F.; Grollman, A.P.; Breslauer, K.J.
    Energetics of lesion recognition by a DNA repair protein: Thermodynamic characterization of formamidopyrimidine-glycosylase (Fpg) interactions with damaged DNA duplexes (2003), J. Mol. Biol., 328, 1047-1060.
    View publication on PubMed
Search for more literature for 3.2.2.23

Inhibitors

Inhibitors Comment Organism Structure
tetrahydrofuran-containing DNA dublex
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information thermodynamic characterization of Fpg binding to lesion-containing 13mer DNA dublexes, binding affinity Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Na+ maximal efficiency at 100 mM NaCl Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
DNA + H2O Escherichia coli bifunctional base excision repair enzyme: DNA glycosylase/AP lyase ?
-
 ?
DNA + H2O Escherichia coli B834 (DE3) bifunctional base excision repair enzyme: DNA glycosylase/AP lyase ?
-
 ?
DNA containing 8-hydroxyguanine residues + H2O Escherichia coli natural substrate: 7,8-dihydro-8-oxo-dG, DNA base excision repair 8-hydroxyguanine + DNA
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 harboring PET13a-fpg plasmid
-
Escherichia coli B834 (DE3)
-
 harboring PET13a-fpg plasmid
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
DNA containing ring-opened N7-methylguanine + H2O = deguanylated DNA + 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine mechanism Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA + H2O with apurinic/apyrimidinic lyase activity, catalyzes beta and delta elimination reactions Escherichia coli ?
-
 ?
DNA + H2O FpG-DNA interactions establish contacts with DNA ligands, which span no more than 9 base-pairs, structural studies of Fpg-DNA complexes Escherichia coli ?
-
 ?
DNA + H2O enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity Escherichia coli ?
-
 ?
DNA + H2O bifunctional base excision repair enzyme: DNA glycosylase/AP lyase Escherichia coli ?
-
 ?
DNA + H2O with apurinic/apyrimidinic lyase activity, catalyzes beta and delta elimination reactions Escherichia coli B834 (DE3) ?
-
 ?
DNA + H2O FpG-DNA interactions establish contacts with DNA ligands, which span no more than 9 base-pairs, structural studies of Fpg-DNA complexes Escherichia coli B834 (DE3) ?
-
 ?
DNA + H2O enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity Escherichia coli B834 (DE3) ?
-
 ?
DNA + H2O bifunctional base excision repair enzyme: DNA glycosylase/AP lyase Escherichia coli B834 (DE3) ?
-
 ?
DNA containing 8-hydroxyguanine residues + H2O DNA glycosylase/AP lyase activity Escherichia coli 8-hydroxyguanine + DNA
-
 ?
DNA containing 8-hydroxyguanine residues + H2O 7,8-dihydro-8-oxo-2’-deoxyguanosine, natural substrate, substrate recognition, mechanism Escherichia coli 8-hydroxyguanine + DNA
-
 ?
DNA containing 8-hydroxyguanine residues + H2O 7,8-dihydro-8-oxoguanine-DNA Escherichia coli 8-hydroxyguanine + DNA
-
 ?
DNA containing 8-hydroxyguanine residues + H2O natural substrate: 7,8-dihydro-8-oxo-dG, DNA base excision repair Escherichia coli 8-hydroxyguanine + DNA
-
 ?
additional information not: carbocyclic substrate analog of 8-oxo-7,8-dihydro-2’-deoxyguanosine Escherichia coli ?
-
 ?
additional information not: carbocyclic substrate analog of 8-oxo-7,8-dihydro-2’-deoxyguanosine Escherichia coli B834 (DE3) ?
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
 free protein undergoes irreversible thermal unfolding with a Tm of about 65°C Escherichia coli