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DraconiticBiochemistryBiomolecules · Catabolism · Biosynthesis · MetabolismMap

Data

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Human metabolism

Reactome's human metabolism drawn as one network. Each molecule has one home node; widely shared molecules also appear as dashed copies in other territories, linked from their details. .

Territories

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Metabolite; its structure appears as you zoom in
Reaction, arrow toward the product
Cofactors and co-substrates are written beside the reaction when you zoom in
Dashed ring: a copy of a widely shared molecule or cofactor in another territory or pathway
Compartment transfer of the molecule it is linked to
Binding, release or complex event; its proteins are named in its details
Outline: reactions mostly in the mitochondrion

Arrows follow Reactome's curated reaction direction.

GST dimers conjugate GSH with cytosolic substrates

GSH + Electrophilic substrate → electrophilic substrate:SG

Reactome: R-HSA-176054
Compartment: cytosol
Rhea: None recorded

Inputs

GSHCHEBI:57925, C10H16N3O6S, cytosol
Electrophilic substrateR-ALL-176070, cytosol

Outputs

electrophilic substrate:SGR-ALL-176049, cytosol

Catalysed by

glutathione transferase activity of GST dimers [cytosol]EC 2.5.1.18

Literature

Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes J. Mol. Biol., 1993
1.3-A resolution structure of human glutathione S-transferase with S-hexyl glutathione bound reveals possible extended ligandin binding site Proteins, 2002
Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver Biochim. Biophys. Acta, 1993
Purification and characterization of a novel alpha-class glutathione transferase from human liver Int. J. Biochem. Cell Biol., 1998
Structural basis for featuring of steroid isomerase activity in alpha class glutathione transferases J. Mol. Biol., 2010
Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products J. Mol. Biol., 1999