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

Generation of a Ni(II) binding site by introduction of a histidine cluster in the structure of human glutathione transferase A1-1.

Protein engineering - 1 Nov 1995

Yilmaz S, Widersten M, Emahazion T, Mannervik B

Abstract excerpt

Two mutant forms of human glutathione transferase (GST) A1-1 with affinity for metal ions were constructed by introduction of His residues by site-directed mutagenesis. A mutant, 2-His, contained the mutations Lys84Gln, Asp85His and Glu88His, and another, 5-His, contained the mutations Tyr79His, Asn80His, Lys84His, Asp85His and Glu88His. The mutant proteins were obtained in good yields (40-150 mg per 3 l culture)...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Binding Sites
Share to Isoenzymes

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

Share to Models, Molecular

Share to Molecular Sequence Data

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Recombinant Proteins

Source

Identifiers

PMID: 8819982
DOI: 10.1093/protein/8.11.1163

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

Generation of a Ni(II) binding site by introduction of a histidine cluster in the structure of human glutathione transferase A1-1.PMID 8819982Read ↗

New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix.Semantic proximity Read ↗

Glutathione transferases with novel active sites isolated by phage display from a library of random mutants.Semantic proximity Read ↗

An approach to optimizing the active site in a glutathione transferase by evolution in vitro.Semantic proximity Read ↗

Orthogonal protein purification--expanding the repertoire of GST fusion systems.Semantic proximity Read ↗

Structural studies on human glutathione S-transferase pi. Substitution mutations to determine amino acids necessary for binding glutathione.Semantic proximity Read ↗

Stability of the domain interface contributes towards the catalytic function at the H-site of class alpha glutathione transferase A1-1.Semantic proximity Read ↗

Mutation T71R enhanced the structural stability and functional activity of wild type superoxide dismutase cloned from soil metagenome.Semantic proximity Read ↗

Optimized heterologous expression of the polymorphic human glutathione transferase M1-1 based on silent mutations in the corresponding cDNA.Semantic proximity Read ↗

Single-nucleotide polymorphic variants of human glutathione transferase T1-1 differ in stability and functional properties.Semantic proximity Read ↗

Investigating the influence of histidine residues on the metal ion binding ability of the wheat metallothionein γ-Ec-1 domain.Semantic proximity Read ↗

Characterization of the E26H Mutant Schistosoma japonicum Glutathione S-Transferase.Semantic proximity Read ↗

A structural role of histidine 15 in human glutathione transferase M1-1, an amino acid residue conserved in class Mu enzymes.Semantic proximity Read ↗

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