Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Catalytic contributions of key residues in the adenine glycosylase MutY revealed by pH-dependent kinetics and cellular repair assays.

Chemistry & biology - 24 Feb 2012

Brinkmeyer Megan K, Pope Mary Ann, David Sheila S

Abstract excerpt

MutY prevent DNA mutations associated with 8-oxoguanine (OG) by catalyzing the removal of adenines opposite OG. pH dependence of the adenine glycosylase activity establish that Asp 138 of MutY must be deprotonated for maximal activity consistent with its role in stabilizing the oxacarbenium ion transition state in an S(N)1 mechanism. A cellular OG:A repair assay allowed further validation of the critical role of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Substitution
Share to Base Pair Mismatch

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Biocatalysis

Share to DNA Glycosylases

Share to DNA Repair

Share to Guanine

Share to Hydrogen-Ion Concentration

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 22365610
DOI: 10.1016/j.chembiol.2011.11.011
PMCID: PMC3292766

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Catalytic contributions of key residues in the adenine glycosylase MutY revealed by pH-dependent kinetics and cellular repair assays.PMID 22365610Read ↗

Structural Basis for Avoidance of Promutagenic DNA Repair by MutY Adenine DNA Glycosylase.Semantic proximity Read ↗

Reaction intermediates in the catalytic mechanism of Escherichia coli MutY DNA glycosylase.Semantic proximity Read ↗

Repair of A/G and A/8-oxoG mismatches by MutY adenine DNA glycosylase.Semantic proximity Read ↗

Structural and biochemical analysis of DNA helix invasion by the bacterial 8-oxoguanine DNA glycosylase MutM.Semantic proximity Read ↗

MUTYH DNA glycosylase: the rationale for removing undamaged bases from the DNASemantic proximity Read ↗

Structural snapshots of base excision by the cancer-associated variant MutY N146S reveal a retaining mechanism.Semantic proximity Read ↗

Unnatural substrates reveal the importance of 8-oxoguanine for in vivo mismatch repair by MutYSemantic proximity Read ↗

Crystal structure of MutYX: a novel clusterless adenine DNA glycosylase with a distinct C-terminal domain and 8-oxoguanine recognition sphere.Semantic proximity Read ↗

Repair of 8-oxoG:A mismatches by the MUTYH glycosylase: Mechanism, metals and medicine.Semantic proximity Read ↗

Structure of human MUTYH and functional profiling of cancer-associated variants reveal an allosteric network between its [4Fe-4S] cluster cofactor and active site required for DNA repair.Semantic proximity Read ↗

The C-terminal domain of MutY glycosylase determines the 7,8-dihydro-8-oxo-guanine specificity and is crucial for mutation avoidance.Semantic proximity Read ↗

Structure of the mammalian adenine DNA glycosylase MUTYH: insights into the base excision repair pathway and cancer.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.