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

A glutathione-independent glyoxalase of the DJ-1 superfamily plays an important role in managing metabolically generated methylglyoxal in Candida albicans.

The Journal of biological chemistry - 17 Jan 2014

Hasim Sahar, Hussin Nur Ahmad, Alomar Fadhel, Bidasee Keshore R, Nickerson Kenneth W, Wilson Mark A

Abstract excerpt

Methylglyoxal is a cytotoxic reactive carbonyl compound produced by central metabolism. Dedicated glyoxalases convert methylglyoxal to d-lactate using multiple catalytic strategies. In this study, the DJ-1 superfamily member ORF 19.251/GLX3 from Candida albicans is shown to possess glyoxalase activity, making this the first demonstrated glutathione-independent glyoxalase in fungi. The crystal structure of Glx3p...

Read the complete abstract on PubMed

Topics

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

Share to Aldehyde Oxidoreductases
Share to Candida albicans

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genetic Loci

Share to Glycerol

Share to Heat-Shock Proteins

Share to Pyruvaldehyde

Share to Saccharomyces cerevisiae Proteins

Share to Stress, Physiological

Source

Open in PubMed Open full text

Identifiers

PMID: 24302734
DOI: 10.1074/jbc.M113.505784
PMCID: PMC3894345

Genes

GLO1

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

A glutathione-independent glyoxalase of the DJ-1 superfamily plays an important role in managing metabolically generated methylglyoxal in Candida albicans.PMID 24302734Read ↗

<i>Saccharomyces cerevisiae</i> DJ-1 paralogs maintain genome integrity through glycation repair of nucleic acids and proteinsSemantic proximity Read ↗

Presence of unique glyoxalase III proteins in plants indicates the existence of shorter route for methylglyoxal detoxification.Semantic proximity Read ↗

Glutathione biosynthesis in the yeast pathogens Candida glabrata and Candida albicans: essential in C. glabrata, and essential for virulence in C. albicans.Semantic proximity Read ↗

Robust glyoxalase activity of Hsp31, a ThiJ/DJ-1/PfpI family member protein, is critical for oxidative stress resistance in Saccharomyces cerevisiae.Semantic proximity Read ↗

The Saccharomyces cerevisiae aldose reductase is implied in the metabolism of methylglyoxal in response to stress conditions.Semantic proximity Read ↗

Glutathione peroxidase 3 of Saccharomyces cerevisiae regulates the activity of methionine sulfoxide reductase in a redox state-dependent way.Semantic proximity Read ↗

A family of glutathione peroxidases contributes to oxidative stress resistance in Candida albicansSemantic proximity Read ↗

Function of glutaredoxin 3 (Grx3) in oxidative stress response caused by iron homeostasis disorder in Candida albicans.Semantic proximity Read ↗

Bacterial Responses to Glyoxal and Methylglyoxal: Reactive Electrophilic SpeciesSemantic proximity Read ↗

Defense against Reactive Carbonyl Species Involves at Least Three Subcellular Compartments Where Individual Components of the System Respond to Cellular Sugar Status.Semantic proximity Read ↗

The glycolytic metabolite methylglyoxal activates Pap1 and Sty1 stress responses in Schizosaccharomyces pombe.Semantic proximity Read ↗

Sulphiredoxin plays peroxiredoxin‐dependent and ‐independent roles via the HOG signalling pathway in C ryptococcus neoformans and contributes to fungal virulenceSemantic proximity Read ↗

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