DNA-3-methyladenine glycosylase II explained
| DNA-3-methyladenine glycosylase II |
| Ec Number: | 3.2.2.21 |
| Cas Number: | 89287-38-7 |
DNA-3-methyladenine glycosylase II 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 . The second, methylpurine-DNA glycosylase (MPG) 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)
Notes and References
- Evensen G, Seeberg E . Adaptation to alkylation resistance involves the induction of a DNA glycosylase . Nature . 296 . 5859 . 773–775 . April 1982 . 7040984 . 10.1038/296773a0 . 1982Natur.296..773E . 4318955 .
- Karran P, Hjelmgren T, Lindahl T . 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 . 7040983 . 10.1038/296770a0 . 1982Natur.296..770K . 4367726 .
- Riazuddin S, Lindahl T . Properties of 3-methyladenine-DNA glycosylase from Escherichia coli . Biochemistry . 17 . 11 . 2110–2118 . May 1978 . 352392 . 10.1021/bi00604a014 .
- Thomas L, Yang CH, Goldthwait DA . Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine . Biochemistry . 21 . 6 . 1162–1169 . March 1982 . 7041972 . 10.1021/bi00535a009 .
- Krokan HE, Bjørås M . Base excision repair . Cold Spring Harbor Perspectives in Biology . 5 . 4 . a012583 . April 2013 . 23545420 . 3683898 . 10.1101/cshperspect.a012583 .
