CATH Classification

Domain Context

CATH Clusters

Superfamily Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal)
Functional Family Adenine DNA glycosylase

Enzyme Information
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 (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)

Escherichia coli K-12
Adenine DNA glycosylase

PDB Structure

External Links
Organism Escherichia
Primary Citation
Analysis of the E.coli MutY DNA glycosylase structure and function by site-directed mutagenesis
Gilboa, R., Kilshtein, A., Zharkov, D.O., Kycia, J.H., Gerchman, S.E., Grollman, A.P., Shoham, G.
To be Published