Biology:DNA-3-methyladenine glycosylase II

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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

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. "Adaptation to alkylation resistance involves the induction of a DNA glycosylase". Nature 296 (5859): 773–775. April 1982. doi:10.1038/296773a0. PMID 7040984. Bibcode1982Natur.296..773E. 
  2. "Induction of a DNA glycosylase for N-methylated purines is part of the adaptive response to alkylating agents". Nature 296 (5859): 770–773. April 1982. doi:10.1038/296770a0. PMID 7040983. Bibcode1982Natur.296..770K. 
  3. "Properties of 3-methyladenine-DNA glycosylase from Escherichia coli". Biochemistry 17 (11): 2110–2118. May 1978. doi:10.1021/bi00604a014. PMID 352392. 
  4. "Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine". Biochemistry 21 (6): 1162–1169. March 1982. doi:10.1021/bi00535a009. PMID 7041972. 
  5. "Base excision repair". Cold Spring Harbor Perspectives in Biology 5 (4): a012583. April 2013. doi:10.1101/cshperspect.a012583. PMID 23545420. 

External links