Literature summary for 3.2.2.21 extracted from

Adhikari, S.; Toretsky, J.A.; Yuan, L.; Roy, R.
Magnesium, essential for base excision repair enzymes, inhibits substrate binding of N-methylpurine-DNA glycosylase (2006), J. Biol. Chem., 281, 29525-29532.

Search for more literature for 3.2.2.21

Inhibitors

Inhibitors	Comment	Organism	Structure
Mg2+	significant inhibition depending on its concentration, but independent of substrate type. Mg2+ at high but physiologic concentrations decreases the amount of active enzyme. Inhibition affects the Km value, but not Vmax, and is due to inhibition in substrate binding and can be reversed by EDTA. At low concentration, Mg2+ stimulates enzyme activity with substrate hypoxanthine, but not with ethenoadenine	Mus musculus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0000354	-	duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine	37°C, pH 7.9	Mus musculus
0.0000448	-	duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine	37°C, pH 7.9, presence of 250 mM Mg2+	Mus musculus
0.0000548	-	duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine	37°C, pH 7.9, presence of 500 mM Mg2+	Mus musculus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	at low concentration, Mg2+ stimulates enzyme activity with substrate hypoxanthine, but not with ethenoadenine. At high concentrations, inhibitory	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	-	recombinant enzyme	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine + H2O	-	Mus musculus	ethenoadenine + hypoxanthine + oligonucleotide	-	?

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Release 2023.1 (January 2023)