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Literature summary for extracted from

  • Schwartz, M.; Didierjean, C.; Hecker, A.; Girardet, J.M.; Morel-Rouhier, M.; Gelhaye, E.; Favier, F.
    Crystal structure of Saccharomyces cerevisiae ECM4, a Xi-class glutathione transferase that reacts with glutathionyl-(hydro)quinones (2016), PLoS ONE, 11, e0164678.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
isoform ECM4 shows extensions including a huge loop which contributes to the quaternary assembly. Soaking of ECM4 crystals with glutathionyl-menadione results in a structure where glutathione forms a mixed disulfide bond with the cysteine 46. Residues H345 and H350, F228, Y224 and W48 could play crucial roles in binding of glutathionyl-(hydro)quinones, and in assisting C46 during catalysis Saccharomyces cerevisiae


Organism UniProt Comment Textmining
Saccharomyces cerevisiae P36156 cf. EC, EC

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione + 2-(glutathione-S-yl)-menadione
Saccharomyces cerevisiae glutathione disulfide + menadione


Synonyms Comment Organism
Saccharomyces cerevisiae