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DraconiticBiochemistryBiomolecules · Catabolism · Biosynthesis · MetabolismMap

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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.

GGT dimers hydrolyse GSH

GSH + H2O → CysGly + L-Glu

Reactome: R-HSA-8943279
Compartment: plasma membrane · extracellular region
Rhea: RHEA:28808

Inputs

GSHCHEBI:16856, C10H17N3O6S, extracellular region
H2OCHEBI:15377, H2O, extracellular region

Outputs

CysGlyCHEBI:61694, C5H10N2O3S, extracellular region
L-GluCHEBI:29985, C5H8NO4, extracellular region

Catalysed by

glutathione gamma-glutamate hydrolase activity of GGT dimers [plasma membrane]EC 3.4.19.13

Literature

Kinetic characterization and identification of the acylation and glycosylation sites of recombinant human gamma-glutamyltranspeptidase Biochemistry, 2007
Immunohistochemical detection of gamma-glutamyl transpeptidase in normal human tissue J. Histochem. Cytochem., 1996
The human gamma-glutamyltransferase gene family Hum Genet, 2008
Different gamma-glutamyl transpeptidase mRNAs are expressed in human liver and kidney Biochem Biophys Res Commun, 1989
Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit J Biol Chem, 1977
Hydrolysis and transfer reactions catalyzed by gamma-glutamyl transpeptidase; evidence for separate substrate sites and for high affinity of L-cystine Biochem. Biophys. Res. Commun., 1976