Literature summary for 3.2.2.23 extracted from

Popov, A.V.; Endutkin, A.V.; Vorobjev, Y.N.; Zharkov, D.O.
Molecular dynamics simulation of the opposite-base preference and interactions in the active site of formamidopyrimidine-DNA glycosylase (2017), BMC Struct. Biol., 17, 005 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
dynamic simulation of the pre-catalytic complex of Fpg with DNA containing oxoG opposite C or A, the latter in either syn or anti conformation. Only one transition is observed in the experimental reaction rate pH dependence plots, and Glu2 keeps the same set of interactions regardless of its protonation state. The adenine base opposite oxoG is highly distorting for the adjacent nucleotides. The side chains of Arg109 and Phe111 that Fpg inserts into DNA to maintain its kinked conformation tend to withdraw from their positions if A is opposite to the lesion	Lactococcus lactis

Crystallization (Comment)

Organism

dynamic simulation of the pre-catalytic complex of Fpg with DNA containing oxoG opposite C or A, the latter in either syn or anti conformation. Only one transition is observed in the experimental reaction rate pH dependence plots, and Glu2 keeps the same set of interactions regardless of its protonation state. The adenine base opposite oxoG is highly distorting for the adjacent nucleotides. The side chains of Arg109 and Phe111 that Fpg inserts into DNA to maintain its kinked conformation tend to withdraw from their positions if A is opposite to the lesion

Lactococcus lactis

Organism

Organism	UniProt	Comment	Textmining
Lactococcus lactis	P42371	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
DNA containing oxoG opposite C or A + H2O	-	Lactococcus lactis	2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA	-	?

Synonyms

Synonyms	Comment	Organism
FPG	-	Lactococcus lactis
MutM	-	Lactococcus lactis

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Release 2023.1 (January 2023)