CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.10 | Orthogonal Bundle | |
1.10.1670 | Endonuclease Iii, domain 2 | |
1.10.1670.10 | Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal) |
Domain Context
CATH Clusters
Superfamily | Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal) |
Functional Family | Adenine DNA glycosylase |
Enzyme Information
3.2.2.31 |
Adenine glycosylase.
based on mapping to UniProt P17802
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)
P17802 |
MUTY_ECOLI
Escherichia coli K-12
Adenine DNA glycosylase
|
PDB Structure
PDB | 1WEI |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Reaction intermediates in the catalytic mechanism of Escherichia coli MutY DNA glycosylase
J.Biol.Chem.
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