Literature summary for 3.2.2.23 extracted from

Kuznetsov, N.A.; Koval, V.V.; Zharkov, D.O.; Vorobjev, Y.N.; Nevinsky, G.A.; Douglas, K.T.; Fedorova, O.S.
Pre-steady-state kinetic study of substrate specificity of Escherichia coli formamidopyrimidine--DNA glycosylase (2007), Biochemistry, 46, 424-435.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P05523	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
DNA containing ring-opened N7-methylguanine + H2O = deguanylated DNA + 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine	the damaged base is first destabilized by the enzyme binding and then everted from DNA, followed by insertion of several amino acid residues into DNA and isomerization of the enzyme into a pre-excision complex	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
DNA containing 8-oxoguanine opposite A + H2O	poor substrate, analysis of rate constants of conformational transitions	Escherichia coli	8-oxoguanine + DNA	-	?
DNA containing 8-oxoguanine opposite C + H2O	good substrate, analysis of rate constants of conformational transitions	Escherichia coli	8-oxoguanine + DNA	-	?
DNA containing 8-oxoguanine opposite G + H2O	analysis of rate constants of conformational transitions	Escherichia coli	8-oxoguanine + DNA	-	?
DNA containing 8-oxoguanine opposite T + H2O	analysis of rate constants of conformational transitions	Escherichia coli	8-oxoguanine + DNA	-	?
DNA containing dihydrouracil + H2O	-	Escherichia coli	8-oxoguanine + DNA	-	?

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Release 2023.1 (January 2023)