CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.79 | Nucleoside Triphosphate Pyrophosphohydrolase |
|
3.90.79.10 | Nucleoside Triphosphate Pyrophosphohydrolase |
Domain Context
CATH Clusters
| Superfamily | Nucleoside Triphosphate Pyrophosphohydrolase |
| Functional Family |
Enzyme Information
| 3.2.2.31 |
Adenine glycosylase.
based on mapping to UniProt P83847
Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
-!- The enzyme serves as a mismatch repair enzyme that works to correct 7,8-dihydro-8-oxoguanine:adenine mispairs that arise in DNA when error-prone synthesis occurs past 7,8-dihydro-8-oxoguanine (GO) lesions in DNA. -!- The enzyme excises the adenine of the mispair, producing an apurinic site sensitive to AP endonuclease activity. -!- After removing the undamaged adenine the enzyme remains bound to the site to prevent EC 3.2.2.23 (MutM) from removing the GO lesion, which could lead to a double strand break. -!- In vitro the enzyme is also active with adenine:guanine, adenine:cytosine, and adenine:7,8-dihydro-8-oxoadenine (AO) mispairs, removing the adenine in all cases.
|
UniProtKB Entries (1)
| P83847 |
MUTY_GEOSE
Geobacillus stearothermophilus
Adenine DNA glycosylase
|
PDB Structure
| PDB | 3G0Q |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Atomic substitution reveals the structural basis for substrate adenine recognition and removal by adenine DNA glycosylase.
Proc.Natl.Acad.Sci.Usa
|
