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Article

Active-site residues governing high steroid isomerase activity in human glutathione transferase A3-3.

The Journal of biological chemistry - 10 May 2002

Johansson Ann-Sofie, Mannervik Bengt

Abstract excerpt

Glutathione transferase (GST) A3-3 is the most efficient human steroid double-bond isomerase known. The activity with Delta(5)-androstene-3,17-dione is highly dependent on the phenolic hydroxyl group of Tyr-9 and the thiolate of glutathione. Removal of these groups caused an 1.1 x 10(5)-fold decrease in k(cat); the Y9F mutant displayed a 150-fold lower isomerase activity in the presence of glutathione and a...

Topics

Binding Sites
Escherichia coli
Glutathione
Glutathione Transferase
Humans
Hydrogen-Ion Concentration
Kinetics
Models, Chemical
Mutagenesis, Site-Directed
Mutation
Phenylalanine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Steroid Isomerases

Substrate Specificity

Sulfhydryl Compounds

Tyrosine

Source

Identifiers

PMID: 11872752
DOI: 10.1074/jbc.M201062200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-11872752-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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