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Article

Regio- and enantioselectivities in epoxide conjugations are modulated by residue 210 in Mu class glutathione transferases.

Protein engineering, design & selection : PEDS - 1 Dec 2005

Ivarsson Ylva, Mannervik Bengt

Abstract excerpt

The homologous human glutathione transferases (GSTs) M1-1 and M2-2 have similar catalytic activities with many electrophilic substrates, but differ strikingly in their conjugation of epoxides with glutathione. Residue 210, Thr in GST M2-2 and Ser in GST M1-1, is a key active-site component in determining the activity profile with epoxide substrates. This residue is hypervariable in Mu class GSTs, suggesting that...

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Identifiers

PMID: 16251220
DOI: 10.1093/protein/gzi064

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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