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DNA-3-methyladenine glycosylase II

From Wikipedia, the free encyclopedia

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DNA-3-methyladenine glycosylase II (EC 3.2.2.21) is an enzyme[1][2][3][4] that catalyses the following chemical reaction:

Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine, and 7-methyladenine

Involved in the removal of alkylated bases from DNA in Escherichia coli.

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Evolution

Through the process of convergent evolution, there are at least two unrelated protein folds that share the same DNA-3-methyladenine glycosylase activity. The first, the AlkA N-terminal domain, is found in bacteria Pfam PF06029. The second, methylpurine-DNA glycosylase (MPG) Pfam PF02245 is found in vertebrates including humans.[5]

Nomenclature

DNA-3-methyladenine glycosylase II is also known as

  • deoxyribonucleate 3-methyladenine glycosides II
  • 3-methyladenine DNA glycosylase II
  • DNA-3-methyladenine glycosides II
  • AlkA
  • alkylated-DNA glycohydrolase (releasing methyladenine and methylguanine)

See also

  • MAG1 (DNA-3-methyladenine glycosylase)

References

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