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DNA-3-methyladenine glycosylase
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DNA-3-methyladenine glycosylase : ウィキペディア英語版
DNA-3-methyladenine glycosylase

DNA-3-methyladenine glycosylase also known as 3-alkyladenine DNA glycosylase (AAG) or N-methylpurine DNA glycosylase (MPG) is an enzyme that in humans is encoded by the ''MPG'' gene.〔(【引用サイトリンク】 url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4350 )
Alkyladenine DNA glycosylase is an specific type of DNA glycosylase. This subfamily of monofunctional glycosylases is involved in the recognition of a variety of base lesions, including alkylated and deaminated purines, and initiating their repair via the base excision repair pathway. To date, the human AAG (hAAG) is the only glycosylase identified that excises alkylation-damaged purine bases.
== Function ==

DNA bases are subject to a large number of anomalies: spontaneous alkylation or oxidative deamination. It is estimated that 104 mutations appear in a typical human cell per day. Albeit it seems to be an insignificant amount considering the extension of the DNA (1010 nucleotides), these mutations lead to changes in the structure and coding potential of the DNA, affecting processes of replication and transcription.
3-Methyladenine DNA glycosilases are able to initiate the base excision repair (BER) of a wide range of substrate bases that, due to their chemical reactivity, suffer inevitable modifications resulting in different biological outcomes. DNA repair mechanisms take on a vital roll in maintainning the genomic integrity of cells from different organisms, in particular 3-Methyladenine DNA glycosilases are found in bacteria, yeast, plants, rodents and humans. Therefore, there are different subfamilies of this enzime, such as the Human Alkyladenine DNA Glycosylase (hAAG), that act on other damaged DNA bases apart from 3-MeA

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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