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Literature summary for 3.2.2.23 extracted from

  • Gilboa, R.; Zharkov, D.O.; Golan, G.; Fernandes, A.S.; Gerchman, S.E.; Matz, E.; Kycia, J.H.; Grollman, A.P.; Shoham, G.
    Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA (2002), J. Biol. Chem., 277, 19811-19816.
    View publication on PubMed
Search for more literature for 3.2.2.23

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of enzyme covalently complexed to DNA Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ possesses a zinc finger 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 + H2O Escherichia coli DNA base excision repair enzyme ?
-
 ?

Organism

Organism UniProt Comment Textmining
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 excises oxidized purines from damaged DNA, Schiff base intermediate, enzyme structure, bilobal protein with a wide, positive charged DNA-binding groove and a helix-2-turn-helix motif that participates in DNA binding, damage recognition, catalytic mechanism Escherichia coli ?
-
 ?
DNA + H2O removes oxidized purines from oxidatively damaged DNA Escherichia coli ?
-
 ?
DNA + H2O DNA base excision repair enzyme Escherichia coli ?
-
 ?