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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...

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Identifiers

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

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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