DNA-3-methyladenine glycosylase II

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
DNA-3-methyladenine glycosylase II
Identifiers
EC number3.2.2.21
CAS number89287-38-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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

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)

References

  1. Evensen G, Seeberg E (Apr 1982). "Adaptation to alkylation resistance involves the induction of a DNA glycosylase". Nature. 296 (5859): 773–5. doi:10.1038/296773a0. PMID 7040984.
  2. Karran P, Hjelmgren T, Lindahl T (Apr 1982). "Induction of a DNA glycosylase for N-methylated purines is part of the adaptive response to alkylating agents". Nature. 296 (5859): 770–3. doi:10.1038/296770a0. PMID 7040983.
  3. Riazuddin S, Lindahl T (May 1978). "Properties of 3-methyladenine-DNA glycosylase from Escherichia coli". Biochemistry. 17 (11): 2110–8. doi:10.1021/bi00604a014. PMID 352392.
  4. Thomas L, Yang CH, Goldthwait DA (Mar 1982). "Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine". Biochemistry. 21 (6): 1162–9. doi:10.1021/bi00535a009. PMID 7041972.
  5. Krokan HE, Bjørås M (2013). "Base excision repair". Cold Spring Harb Perspect Biol. 5 (4): a012583. doi:10.1101/cshperspect.a012583. PMC 3683898. PMID 23545420.


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