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

Tetramerization and cooperativity in Plasmodium falciparum glutathione S-transferase are mediated by atypic loop 113-119.

The Journal of biological chemistry - 14 Aug 2009

Liebau Eva, Dawood Kutayba F, Fabrini Raffaele, Fischer-Riepe Lena, Perbandt Markus, Stella Lorenzo, Pedersen Jens Z, Bocedi Alessio, Petrarca Patrizia, Federici Giorgio, Ricci Giorgio

Abstract excerpt

Glutathione S-transferase of Plasmodium falciparum (PfGST) displays a peculiar dimer to tetramer transition that causes full enzyme inactivation and loss of its ability to sequester parasitotoxic hemin. Furthermore, binding of hemin is modulated by a cooperative mechanism. Site-directed mutagenesis, steady-state kinetic experiments, and fluorescence anisotropy have been used to verify the possible involvement of...

Read the complete abstract on PubMed

Topics

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

Share to Dimerization
Share to Glutathione

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glutathione Transferase

Share to Molecular Conformation

Share to Mutagenesis, Site-Directed

Share to Oxidation-Reduction

Share to Plasmodium falciparum

Source

Open in PubMed Open full text

Identifiers

PMID: 19531494
DOI: 10.1074/jbc.M109.015198
PMCID: PMC2755937

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

Tetramerization and cooperativity in Plasmodium falciparum glutathione S-transferase are mediated by atypic loop 113-119.PMID 19531494Read ↗

Asn112 in Plasmodium falciparum glutathione S-transferase is essential for induced reversible tetramerization by phosphate or pyrophosphate.Semantic proximity Read ↗

Mutations of Gly to Ala in human glutathione transferase P1-1 affect helix 2 (G-site) and induce positive cooperativity in the binding of glutathione.Semantic proximity Read ↗

Catalytic and structural contributions for glutathione-binding residues in a Delta class glutathione S-transferase.Semantic proximity Read ↗

Structural effects of a dimer interface mutation on catalytic activity of triosephosphate isomerase. The role of conserved residues and complementary mutations.Semantic proximity Read ↗

Engineered dimer interface mutants of triosephosphate isomerase: the role of inter-subunit interactions in enzyme function and stability.Semantic proximity Read ↗

Functional analysis of genetic polymorphism in Wuchereria bancrofti glutathione S-transferase antioxidant gene: impact on protein structure and enzyme catalysis.Semantic proximity Read ↗

Glutamate-64, a newly identified residue of the functionally conserved electron-sharing network contributes to catalysis and structural integrity of glutathione transferases.Semantic proximity Read ↗

Key residues of loop 3 in the interaction with the interface residue at position 14 in triosephosphate isomerase from Trypanosoma brucei.Semantic proximity Read ↗

Tertiary interactions stabilise the C-terminal region of human glutathione transferase A1-1: a crystallographic and calorimetric study.Semantic proximity Read ↗

Cardiolipin drives the catalytic activity of GPX4 on membranes: Insights from the R152H mutant.Semantic proximity Read ↗

New insights of falcipain 2 structure from Plasmodium falciparum 3D7 strain.Semantic proximity Read ↗

Oligomeric interfaces as a tool in drug discovery: Specific interference with activity of malate dehydrogenase of Plasmodium falciparum in vitro.Semantic proximity Read ↗

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