Diuretic drug binding to human glutathione transferase P1-1: potential role of Cys-101 revealed in the double mutant C47S/Y108V.

doi:10.1002/jmr.1040

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Article

Diuretic drug binding to human glutathione transferase P1-1: potential role of Cys-101 revealed in the double mutant C47S/Y108V.

Journal of molecular recognition : JMR - 1 Jan 2000

Quesada-Soriano Indalecio, Parker Lorien J, Primavera Alessandra, Wielens Jerome, Holien Jessica K, Casas-Solvas Juan M, Vargas-Berenguel Antonio, Aguilera Ana M, Nuccetelli Marzia, Mazzetti Anna P, Lo Bello Mario, Parker Michael W, García-Fuentes Luis

Abstract excerpt

The diuretic drug ethacrynic acid (EA), both an inhibitor and substrate of pi class glutathione S-transferase (GST P1-1), has been tested in clinical trials as an adjuvant in chemotherapy. We recently studied the role of the active site residue Tyr-108 in binding EA to the enzyme and found that t...

Topics

Amino Acid Substitution
Calorimetry
Crystallography, X-Ray
Cysteine
Diuretics
Enzyme Activation
Ethacrynic Acid
Glutathione
Glutathione S-Transferase pi
Humans
Hydrogen-Ion Concentration
Kinetics
Models, Molecular

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutant Proteins

Mutation

Protein Multimerization

Structure-Activity Relationship

Substrate Specificity

Source

Open in PubMed

Identifiers

PMID: 20540076
DOI: 10.1002/jmr.1040

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-20540076-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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