Arginine 15 stabilizes an S(N)Ar reaction transition state and the binding of anionic ligands at the active site of human glutathione transferase A1-1.

doi:10.1016/j.bpc.2009.11.003

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Article

Arginine 15 stabilizes an S(N)Ar reaction transition state and the binding of anionic ligands at the active site of human glutathione transferase A1-1.

Biophysical chemistry - 1 Feb 2010

Gildenhuys Samantha, Dobreva Marina, Kinsley Nichole, Sayed Yasien, Burke Jonathan, Pelly Stephen, Gordon Graeme P, Sayed Muhammed, Sewell Trevor, Dirr Heini W

Abstract excerpt

Arg15, conserved in class Alpha GSTs (glutathione transferases), is located at the interface between the G- and H-sites of the active site where its cationic guanidinium group might play a role in catalysis and ligand binding. Arg15 in human GSTA1-1 was replaced with a leucine and crystallographi...

Topics

Amino Acid Substitution
Anilino Naphthalenesulfonates
Arginine
Biocatalysis
Crystallography, X-Ray
Dinitrochlorobenzene
Enzyme Stability
Glutathione
Glutathione Transferase
Humans
Isoenzymes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Ligands

Models, Molecular

Mutation

Oxidation-Reduction

Protein Binding

Protons

Spectrum Analysis

Source

Open in PubMed

Identifiers

PMID: 19959275
DOI: 10.1016/j.bpc.2009.11.003

Genes

GSTA1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-19959275-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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