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Literature summary for 3.2.2.23 extracted from

  • Sidorkina, O.M.; Laval, J.
    Role of the N-terminal proline residue in the catalytic activities of the Escherichia coli Fpg protein (2000), J. Biol. Chem., 275, 9924-9929.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
P2E, P2T and P2G mutant Fpg are cloned and expressed in Escherichia coli BH20(fpg-) Escherichia coli

Protein Variants

Protein Variants Comment Organism
P2E completely inactive mutant: no 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine DNA/7,8-dihydro-8-oxoguanine-DNA glycosylase activity or cleavage of DNA containing AP sites Escherichia coli
P2G mutant with 10% of wild-type 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine DNA glycosylase activity and barely detectable 7,8-dihydro-8-oxoguanine-DNA glycosylase activity, no cleavage of DNA containing AP sites Escherichia coli
P2T mutant with 10% of wild-type 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine DNA glycosylase activity and barely detectable 7,8-dihydro-8-oxoguanine-DNA glycosylase activity, no cleavage of DNA containing AP sites Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ possesses a zinc finger Escherichia coli
Zn2+ contains one zinc per enzyme molecule Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30200
-
1 * 30200, globular monomer Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
DNA + H2O Escherichia coli removes oxidized purines from oxidatively damaged DNA ?
-
?
DNA containing 8-hydroxyguanine residues + H2O Escherichia coli dublex, primary physiological substrate is 7,8-dihydro-8-oxoguanine-DNA, DNA repair 8-hydroxyguanine + DNA
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type, P2G, P2E and P2T mutant Fpg 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 catalytic mechanism Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Escherichia coli

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 removes oxidized purines from oxidatively damaged DNA Escherichia coli ?
-
?
DNA + H2O catalytic mechanism involves formation of Schiff base intermediate between DNA containing an oxidized residue and the N-terminal Pro-2 of Fpg, mendatory role of P-2 in 7,8-dihydro-8-oxoguanine-DNA glycosylase and AP lyase activity, but less in 2,6-diamino-4-hydroxy-5-N-methyl-formamidopyrimidine-DNA glycosylase activity Escherichia coli ?
-
?
DNA + H2O enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity Escherichia coli ?
-
?
DNA containing 8-hydroxyguanine residues + H2O mendatory role of P-2 in 7,8-dihydro-8-oxoguanine-DNA glycosylase activity 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 dublex, primary physiological substrate is 7,8-dihydro-8-oxoguanine-DNA, DNA repair Escherichia coli 8-hydroxyguanine + DNA
-
?
DNA containing ring-opened N7-methylguanine residues + H2O less mendatory role of P-2 in 2,6-diamino-4-hydroxy-5-N-methyl-formamidopyrimidine-DNA glycosylase activity Escherichia coli 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
-
?
additional information not: dublex DNA containing a single tetrahydrofuran residue Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 30200, globular monomer Escherichia coli

pI Value

Organism Comment pI Value Maximum pI Value
Escherichia coli
-
-
8.6