DNA-3-methyladenine glycosylase II
Identifiers
EC no.3.2.2.21
CAS no.89287-38-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
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NCBIproteins

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.

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

  1. Evensen G, Seeberg E (April 1982). "Adaptation to alkylation resistance involves the induction of a DNA glycosylase". Nature. 296 (5859): 773–775. Bibcode:1982Natur.296..773E. doi:10.1038/296773a0. PMID 7040984. S2CID 4318955.
  2. Karran P, Hjelmgren T, Lindahl T (April 1982). "Induction of a DNA glycosylase for N-methylated purines is part of the adaptive response to alkylating agents". Nature. 296 (5859): 770–773. Bibcode:1982Natur.296..770K. doi:10.1038/296770a0. PMID 7040983. S2CID 4367726.
  3. Riazuddin S, Lindahl T (May 1978). "Properties of 3-methyladenine-DNA glycosylase from Escherichia coli". Biochemistry. 17 (11): 2110–2118. doi:10.1021/bi00604a014. PMID 352392.
  4. Thomas L, Yang CH, Goldthwait DA (March 1982). "Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine". Biochemistry. 21 (6): 1162–1169. doi:10.1021/bi00535a009. PMID 7041972.
  5. Krokan HE, Bjørås M (April 2013). "Base excision repair". Cold Spring Harbor Perspectives in Biology. 5 (4): a012583. doi:10.1101/cshperspect.a012583. PMC 3683898. PMID 23545420.


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