CATH Classification

Domain Context

CATH Clusters

Superfamily Nucleoside Triphosphate Pyrophosphohydrolase
Functional Family Adenine DNA glycosylase

Enzyme Information

3.2.2.31
Adenine glycosylase.
based on mapping to UniProt Q9UIF7
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)

Q9UIF7
MUTYH_HUMAN
Homo sapiens
Adenine DNA glycosylase

PDB Structure

PDB 1X51
External Links
Method SOLUTION NMR
Organism
Primary Citation
Solution structure of the NUDIX domain from human A/G-specific adenine DNA glycosylase alpha-3 splice isoform
Tomizawa, T., Kigawa, T., Koshiba, S., Inoue, M., Yokoyama, S.
To be Published