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Literature summary for 3.2.2.23 extracted from

  • Koval, V.V.; Kuznetsov, N.A.; Ishchenko, A.A.; Saparbaev, M.K.; Fedorova, O.S.
    Real-time studies of conformational dynamics of the repair enzyme E. coli formamidopyrimidine-DNA glycosylase and its DNA complexes during catalytic cycle (2010), Mutat. Res., 685, 3-10.
    View publication on PubMed
Search for more literature for 3.2.2.23

Protein Variants

Protein Variants Comment Organism
F110A the mutation affects the enzyme activity, especially in the case of oxoG/C substrate, in the second and third reaction steps Escherichia coli
F110W the mutation affects the enzyme activity, especially in the case of oxoG/C substrate, in the second and third reaction steps Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information transient kinetics of Fpg Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli FPG excises oxidatively damaged purines in the base excision repair pathway, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 gene fpg
-

Reaction

Reaction Comment Organism Reaction ID
DNA containing ring-opened N7-methylguanine + H2O = deguanylated DNA + 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine chemical reaction mechanism, overview. For the catalysis to occur, the damaged base must be extruded from the DNA helix and placed in the active site of enzyme, this is achieved in Fpg by kinking DNA at the lesion point. The reaction mechanism involves coupled conformational changes in the enzyme and DNA, which proceed sequentially and assemble the catalytic groups in the active site Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information FPG excises oxidatively damaged purines in the base excision repair pathway, overview Escherichia coli ?
-
 ?
additional information FPG excises oxidatively damaged purines in the base excision repair pathway, it acts on DNA containing 5,6-dihydrouracil, 8-oxo-7,8-dihydroguanine, or on apurinic/apyrimidinic DNA base pairs, analysis of conformational dynamics of Fpg protein and DNA substrates, rate constants of conformational transitions, and intrinsic mechanism of recognition and excision of damaged bases in DNA, overview Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
More Fpg consists of two domains connected by a hinge polypeptide. The N-terminal domain contains a beta-sandwich core and a long alpha-helix with an N-terminal catalytic dyad, proline-glutamate. The C-terminal domain is mostly alpha-helical, containing two motifs almost universally conserved in Fpg proteins: a helix-two turn-helix motif and a beta-hairpin Cys4 zinc finger. The protein molecule possesses a positively charged cleft where damaged DNA is bound Escherichia coli

Synonyms

Synonyms Comment Organism
formamidopyrimidine-DNA glycosylase
-
 Escherichia coli
FPG
-
 Escherichia coli
More Fpg belongs to the class of DNA glycosylases/abasic site lyases Escherichia coli

General Information

General Information Comment Organism
metabolism DNA glycosylases play a key role in the base excision repair pathway, Fpg belongs to the class of DNA glycosylases/abasic site lyases excising several oxidatively damaged purines in the base excision repair pathway Escherichia coli