Description
Fpg protein, a key enzyme in the DNA base excision repair pathway (BER), catalyses the excision of a broad spectrum of modified purines such as formamidopyrimidine (Fapy) and 8-oxoguanine (8-oxo-G). Fpg possess both DNA glycosylase activity that removes the mutated base and AP-lyase activity that releases ribose, leaving both 5'-and 3'-phosphorylated ends in the DNA. Several analytical methods based on Fpg protein activity in vitro were developed for detection and quantitation of oxidative damage to DNA mainly for FapyA, FapyG and 8-oxo-G. The fpg gene was cloned by Boiteux, et al. Fpg protein possess a zinc finger motif at its C-terminus (one zinc atom per molecule). This region is responsible for the DNA binding and AP-lyase activity. In addition, its N-terminal proline was found to act as a nucleophile to produce a Schiff base intermediate, which is essential for enzyme action.
Abbr
MutM, Recombinant (Escherichia coli)
Form
buffered aqueous glycerol solution; Solution in 50% glycerol containing 50 mM potassium HEPES, pH 7.5, 1 mM DTT, 1 mM EDTA, and 200 mM NaCl.
Enzyme Commission Number
EC 3.2.2.23
Activity
>20 ,000 units/mg protein
Molecular Weight
mol wt 30.2 kDa (269 amino acids, predicted from the nucleotide sequence)
Unit Definition
One unit will cleave 50% of 0.5 pmol of double-stranded DNA oligomer substrate (8-oxoguanine−mutated) in 10 min at 25°C.
Pathway
Base excision repair, organism-specific biosystem; Base excision repair, conserved biosystem; Base excision repair, organism-specific biosystem; Base excision repair, conserved biosystem
Synonyms
Fapy-DNA glycosylase; deoxyribonucleate glycosidase; 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase; 2,6-diamino-4-hydroxy-5 (N-methyl)formamidopyrimidine-DNA glycosylase; formamidopyrimidine-DNA glycosylase; DNA-formamidopyrimidine glycosidase; Fpg protein; DNA-formamidopyrimidine glycosylase; EC 3.2.2.23; 78783-53-6; MutM
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