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:

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
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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

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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

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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

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  • MAG1 (DNA-3-methyladenine glycosylase)

References

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  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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