Literature summary for 3.2.2.21 extracted from

Lenz, S.A.P.; Wetmore, S.D.
QM/MM study of the reaction catalyzed by alkyladenine DNA glycosylase examination of the substrate specificity of a DNA repair enzyme (2017), J. Phys. Chem. B, 121, 11096-11108 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
quantum mechanis study of alkyladenine DNA glycosylase AAG bound to DNA containing hypoxanthine, guanine or 7-methylguanine. Subtle differences in protein-DNA contacts upon binding different substrates within the flexible AAG active site can significantly affect the deglycosylation reaction. AAG excises hypoxanthine in a concerted mechanism that is facilitated through correct alignment of the E125 general base due to hydrogen bonding with a neighboring aromatic amino acid Y127. Hypoxanthine departure is further stabilized by pi-pi interactions with aromatic amino acids and hydrogen bonds with active site water. Guanine is not excised since the additional exocyclic amino group leads to misalignment of the general base due to disruption of the key E125-Y127 hydrogen bond, the catalytically unfavorable placement of water within the active site, and weakened pi-contacts between aromatic amino acids and the nucleobase. 7-methylguanine does not occupy the same position within the AAG active site as guanine due to steric clashes with the additional N7 methyl group	Homo sapiens

Crystallization (Comment)

Organism

quantum mechanis study of alkyladenine DNA glycosylase AAG bound to DNA containing hypoxanthine, guanine or 7-methylguanine. Subtle differences in protein-DNA contacts upon binding different substrates within the flexible AAG active site can significantly affect the deglycosylation reaction. AAG excises hypoxanthine in a concerted mechanism that is facilitated through correct alignment of the E125 general base due to hydrogen bonding with a neighboring aromatic amino acid Y127. Hypoxanthine departure is further stabilized by pi-pi interactions with aromatic amino acids and hydrogen bonds with active site water. Guanine is not excised since the additional exocyclic amino group leads to misalignment of the general base due to disruption of the key E125-Y127 hydrogen bond, the catalytically unfavorable placement of water within the active site, and weakened pi-contacts between aromatic amino acids and the nucleobase. 7-methylguanine does not occupy the same position within the AAG active site as guanine due to steric clashes with the additional N7 methyl group

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P29372	-	-

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Release 2023.1 (January 2023)