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

Tyr115, gln165 and trp209 contribute to the 1, 2-epoxy-3-(p-nitrophenoxy)propane-conjugating activity of glutathione S-transferase cGSTM1-1.

Journal of molecular biology - 28 Jul 2000

Chern M K, Wu T C, Hsieh C H, Chou C C, Liu L F, Kuan I C, Yeh Y H, Hsiao C D, Tam M F

Abstract excerpt

We investigated the epoxidase activity of a class mu glutathione S-transferase (cGSTM1-1), using 1,2-epoxy-3-(p-nitrophenoxy)propane (EPNP) as substrate. Trp209 on the C-terminal tail, Arg107 on the alpha4 helix, Asp161 and Gln165 on the alpha6 helix of cGSTM1-1 were selected for mutagenesis and kinetic studies. A hydrophobic side-chain at residue 209 is needed for the epoxidase activity of cGSTM1-1. Replacing...

Read the complete abstract on PubMed

Topics

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

Share to Deuterium
Share to Epoxy Compounds

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Glutamine

Share to Glutathione

Share to Hydrogen Bonding

Share to Nitrophenols

Share to Protons

Share to Tryptophan

Source

Identifiers

PMID: 10903867
DOI: 10.1006/jmbi.2000.3904

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Tyr115, gln165 and trp209 contribute to the 1, 2-epoxy-3-(p-nitrophenoxy)propane-conjugating activity of glutathione S-transferase cGSTM1-1.PMID 10903867Read ↗

Loss of the oxidative stress sensor NPGPx compromises GRP78 chaperone activity and induces systemic disease.Semantic proximity Read ↗

Allelic variants of glutathione S-transferase P1-1 differentially mediate the peroxidase function of peroxiredoxin VI and alter membrane lipid peroxidation.Semantic proximity Read ↗

The identification and structural characterization of C7orf24 as gamma-glutamyl cyclotransferase. An essential enzyme in the gamma-glutamyl cycle.Semantic proximity Read ↗

Pleiotropic functions of glutathione S-transferase P.Semantic proximity Read ↗

Computational Structural Biology of S-nitrosylation of Cancer TargetsSemantic proximity Read ↗

PEGylation and antioxidant effects of a human glutathione peroxidase 1 mutant.Semantic proximity Read ↗

The role of active site residues in the oxidant specificity of the Orp1 thiol peroxidase.Semantic proximity Read ↗

Regulation of Glutathione S-Transferase Omega 1 Mediated by Cysteine Residues Sensing the Redox Environment.Semantic proximity Read ↗

The catalytic site of glutathione peroxidases.Semantic proximity Read ↗

A High-Performance Genetically Encoded Fluorescent Biosensor for Imaging Physiological PeroxynitriteSemantic proximity Read ↗

Protein disulfide isomerase and glutathione are alternative substrates in the one Cys catalytic cycle of glutathione peroxidase 7.Semantic proximity Read ↗

The enhanced affinity for thiolate anion and activation of enzyme-bound glutathione is governed by an arginine residue of human Mu class glutathione S-transferases.Semantic proximity Read ↗

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