Methylpurine-DNA glycosylase is a base excision-repair protein. It is responsible for the hydrolysis of the deoxyribose N-glycosidic bond, excising 3-methyladenine and 3-methylguanine from damaged DNA [1]. Its action is induced by alkylating chemotherapeutics, as well as deaminated and lipid peroxidation-induced purine adducts [2]. MPG without an N-terminal extension excises hypoxanthine with one-third of the efficiency of full-length MPG under similar conditions, suggesting that is function may largely be attributable to the N-terminal extension [3].

1. Expression, purification and characterization of codon-optimized human N-methylpurine-DNA glycosylase from Escherichia coli. Protein Expr. Purif. 58, 257-62
2. Discrimination of lesion removal of N-methylpurine-DNA glycosylase revealed by a potent neutralizing monoclonal antibody. DNA Repair (Amst.) 7, 31-9
3. N-terminal extension of N-methylpurine DNA glycosylase is required for turnover in hypoxanthine excision reaction. J. Biol. Chem. 282, 30078-84

Methylpurine-DNA glycosylase is a base excision-repair protein. It is responsible for the hydroly
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