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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...

Topics

Amino Acid Substitution
Catalysis
Epoxy Compounds
Glutathione
Glutathione Transferase
Humans
Kinetics
Models, Molecular
Mutation
Serine
Stereoisomerism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Substrate Specificity

Threonine

Source

Identifiers

PMID: 16251220
DOI: 10.1093/protein/gzi064

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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