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

doi:10.1016/j.bbapap.2010.09.003

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Article

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

Biochimica et biophysica acta - 1 Dec 2010

Balchin David, Fanucchi Sylvia, Achilonu Ikechukwu, Adamson Roslin J, Burke Jonathan, Fernandes Manuel, Gildenhuys Samantha, Dirr Heini W

Abstract excerpt

Cytosolic glutathione transferases (GSTs) are major detoxification enzymes in aerobes. Each subunit has two distinct domains and an active site consisting of a G-site for binding GSH and an H-site for an electrophilic substrate. While the active site is located at the domain interface, the role of the stability of this interface in the catalytic function of GSTs is poorly understood. Domain 1 of class alpha GSTs...

Topics

Amino Acid Sequence
Binding Sites
Biocatalysis
Catalytic Domain
Circular Dichroism
Crystallography, X-Ray
Dinitrochlorobenzene
Enzyme Stability
Glutathione
Glutathione Transferase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Humans

Isoenzymes

Kinetics

Models, Molecular

Mutation

Protein Binding

Protein Denaturation

Protein Structure, Tertiary

Source

Open in PubMed

Identifiers

PMID: 20833278
DOI: 10.1016/j.bbapap.2010.09.003

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-20833278-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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