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Literature summary for 3.2.2.23 extracted from

  • Tchou, J.; Grollman, A.P.
    The catalytic mechanism of Fpg protein. Evidence for a Schiff base intermediate and amino terminus localization of the catalytic site (1995), J. Biol. Chem., 270, 11671-11677.
    View publication on PubMed
Search for more literature for 3.2.2.23

Protein Variants

Protein Variants Comment Organism
additional information mutant Fpg protein with NH2-terminal modifications Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ contains a single zinc finger motif near the C-terminus Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34400
-
 x * 34400, SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
DNA + H2O Escherichia coli DNA base excision repair enzyme ?
-
 ?
DNA + H2O Escherichia coli JM109 DNA base excision repair enzyme ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli JM109
-
-
-

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 catalytic mechanism Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA + H2O enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity Escherichia coli ?
-
 ?
DNA + H2O DNA base excision repair enzyme Escherichia coli ?
-
 ?
DNA + H2O enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity Escherichia coli JM109 ?
-
 ?
DNA + H2O DNA base excision repair enzyme Escherichia coli JM109 ?
-
 ?
DNA containing 7-hydro-8-oxoguanine residues + H2O mechanism involving protonation at O-6 of 8-oxodeoxyguanine Escherichia coli DNA + 7-hydro-8-oxoguanine
-
 ?
DNA containing 7-hydro-8-oxoguanine residues + H2O dublex 20-oligomer, catalytic mechanism with enzyme-substrate Schiff base intermediate, amino terminal localization of the catalytic site, C-8 keto group of 8-oxodeoxyguanine plays a critical role in binding enzyme Escherichia coli DNA + 7-hydro-8-oxoguanine
-
 ?
DNA containing 7-hydro-8-oxoguanine residues + H2O mechanism involving protonation at O-6 of 8-oxodeoxyguanine Escherichia coli JM109 DNA + 7-hydro-8-oxoguanine
-
 ?
DNA containing 7-hydro-8-oxoguanine residues + H2O dublex 20-oligomer, catalytic mechanism with enzyme-substrate Schiff base intermediate, amino terminal localization of the catalytic site, C-8 keto group of 8-oxodeoxyguanine plays a critical role in binding enzyme Escherichia coli JM109 DNA + 7-hydro-8-oxoguanine
-
 ?
DNA containing ring-opened N7-methylguanine residues + H2O amino terminal localization of the catalytic site Escherichia coli 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
-
 ?
DNA containing ring-opened N7-methylguanine residues + H2O amino terminal localization of the catalytic site Escherichia coli JM109 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine + DNA
-
 ?

Subunits

Subunits Comment Organism
? x * 34400, SDS-PAGE Escherichia coli