Literature summary for 1.8.5.7 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.

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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

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P36156	cf. EC 1.8.5.1, EC 2.5.1.18	-

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

Synonyms	Comment	Organism
ECM4	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)