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

Characterization of an Escherichia coli mutant MutY with a cysteine to alanine mutation at the iron-sulfur cluster domain.

Biochemistry - 8 Apr 2003

Lu A-Lien, Wright Patrick M

Abstract excerpt

Escherichia coli MutY is an adenine and a weak guanine DNA glycosylase involved in reducing mutagenic effects of 7,8-dihydro-8-oxoguanine (8-oxoG). The [4Fe-4S] cluster of MutY is ligated by four conserved cysteine residues and has been shown to be important in substrate recognition. Here, we show that the C199A mutant MutY is very insoluble and can be denatured and renatured to regain activity only if iron and...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Cysteine
Share to DNA Glycosylases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Activation

Share to Enzyme Stability

Share to Iron-Sulfur Proteins

Share to N-Glycosyl Hydrolases

Share to Protein Denaturation

Source

Identifiers

PMID: 12667065
DOI: 10.1021/bi0269198

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Characterization of an Escherichia coli mutant MutY with a cysteine to alanine mutation at the iron-sulfur cluster domain.PMID 12667065Read ↗

The C-terminal domain of Escherichia coli MutY is involved in DNA binding and glycosylase activities.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 ↗

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

An Escherichia coli MutY mutant without the six-helix barrel domain is a dimer in solution and assembles cooperatively into multisubunit complexes with DNA.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 ↗

Molecular cloning and functional analysis of the MutY homolog of Deinococcus radiodurans.Semantic proximity Read ↗

Cellular Assays for Studying the Fe-S Cluster Containing Base Excision Repair Glycosylase MUTYH and Homologs.Semantic proximity Read ↗

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

Escherichia coli MutY protein has a guanine-DNA glycosylase that acts on 7,8-dihydro-8-oxoguanine:guanine mispair to prevent spontaneous G:C-->C:G transversions.Semantic proximity Read ↗

The Zinc Linchpin Motif in the DNA Repair Glycosylase MUTYH: Identifying the Zn2+ Ligands and Roles in Damage Recognition and Repair.Semantic proximity Read ↗

Adenine Glycosylase MutY of Corynebacterium pseudotuberculosis presents the antimutator phenotype and evidences of glycosylase/AP lyase activity in vitro.Semantic proximity Read ↗

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