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Literature summary for 2.5.1.18 extracted from

  • Dourado, D.F.; Fernandes, P.A.; Ramos, M.J.
    Glutathione transferase classes alpha, pi, and mu: GSH activation mechanism (2010), J. Phys. Chem. B, 114, 12972-12980.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Homo sapiens
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isozymes GSTA1-1, GSTM1-1, and GSTP1-1
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Source Tissue

Source Tissue Comment Organism Textmining
liver GSTM1-1 is a major liver GST, but 50% of the population are hGSTM1-null Homo sapiens
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liver cancer cell GSTP1-1 is overexpressed in liver cancer cells Homo sapiens
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Synonyms

Synonyms Comment Organism
GSTM1-1
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Homo sapiens
GSTP1-1
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Homo sapiens

General Information

General Information Comment Organism
evolution glutathione transferase classes alpha, pi, and mu and their GSH activation mechanism, overview Homo sapiens
additional information structure of G-site active center amino acids of GSTM1-1, GSTP1-1, and GSTA1-1, mechanism comparison of isozymes, overview. Analysis of the GSH activation mechanism of GSTP1-1 and GSTM1-1 isoenzymes, overview. For the GSTP1-1 enzyme, a water molecule, after an initial conformational rearrangement of GSH, can assist a proton transfer between the GSH cysteine thiol and the GSH glutamate alpha carboxylate groups. The GSTM1-1 enzyme shows a completely different behavior from isoenzyme GSTP1-1, here two water molecules, positioned between the GSH-SH and the zeta N atom of His107, working like a bridge, are able to promote the proton transfer between these two active groups Homo sapiens