DNA-3-methyladenine glycosylase II
| DNA-3-methyladenine glycosylase II | |||||||||
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| Identifiers | |||||||||
ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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DNA-3-methyladenine glycosylase II (EC 3.2.2.21) is an enzyme[1][2][3][4] that catalyses the following chemical reaction:
- 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
External links
- DNA-3-methyladenine+glycosylase+II at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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