CATH Classification

Domain Context

CATH Clusters

Superfamily Hypothetical protein; domain 2
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 1MUN
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily.
Guan, Y., Manuel, R.C., Arvai, A.S., Parikh, S.S., Mol, C.D., Miller, J.H., Lloyd, S., Tainer, J.A.
Nat.Struct.Biol.