Search results for GGT1

Showing 16 results out of 19

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Protein (5 results from a total of 8)

Identifier: R-HSA-1247889
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: GGT1: P19440
Identifier: R-HSA-5602869
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: GGT1: P19440
Identifier: R-HSA-8943263
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: P19440
Identifier: R-HSA-5602961
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: P19440
Identifier: R-HSA-1247924
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: P19440

Complex (1 results from a total of 1)

Identifier: R-HSA-1247898
Species: Homo sapiens
Compartment: plasma membrane

Set (2 results from a total of 2)

Identifier: R-HSA-5602933
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-2162130
Species: Homo sapiens
Compartment: plasma membrane

Pathway (2 results from a total of 2)

Identifier: R-HSA-5579022
Species: Homo sapiens
To be excreted in urine, glutathione conjugates undergo several hydrolysis steps to form mercapturic acids which are readily excreted. The first step is the hydrolysis of a gamma-glutamyl residue from the conjugate catalysed by gamma-glutamyltransferases (GGTs). These are membrane-bound, heterodimeric enzymes composed of light and heavy peptide chains. Extracellular glutathione (GSH) or its conjugates can be hydrolysed to give cysteinylglycine (CG, or CG conjugates) and free glutamate (L-Glu). Hydrolysis of GSH provides cells with a local cysteine supply and contributes to intracellular GSH levels (Heisterkamp et al. 2008). Defects in GGT1 can cause glutathionuria (GLUTH; MIM:231950), an autosomal recessive disorder characterised by increased GSH concentration in the plasma and urine. Mutations that cause GLUTH can occur in both chains of the GGT1 dimer (Heisterkamp et al. 2008, Aoyama & Nakaki 2013).
Identifier: R-HSA-9035968
Species: Homo sapiens
To be excreted in urine, glutathione conjugates undergo several hydrolysis steps to form mercapturic acids which are readily excreted. The first step is the hydrolysis of a gamma-glutamyl residue from the conjugate catalysed by gamma-glutamyltransferases (GGTs). These are membrane-bound, heterodimeric enzymes composed of light and heavy peptide chains. Extracellular glutathione (GSH) or its conjugates can be hydrolysed to give cysteinylglycine (CG, or CG conjugates) and free glutamate (L-Glu). Hydrolysis of GSH provides cells with a local cysteine supply and contributes to intracellular GSH levels (Heisterkamp et al. 2008). Defects in GGT1 can cause glutathionuria (GLUTH; MIM:231950), an autosomal recessive disorder characterised by increased GSH concentration in the plasma and urine. Mutations that cause GLUTH can occur in both chains of the GGT1 dimer (Heisterkamp et al. 2008, Aoyama & Nakaki 2013).

Reaction (5 results from a total of 5)

Identifier: R-HSA-9035966
Species: Homo sapiens
Compartment: plasma membrane, extracellular region
To be excreted in urine, glutathione conjugates undergo several hydrolysis steps to form mercapturic acids which are readily excreted. The first step is the hydrolysis of a gamma-glutamyl residue from the conjugate catalysed by gamma-glutamyltransferases (GGTs). These are membrane-bound, heterodimeric enzymes composed of light and heavy peptide chains. Extracellular glutathione (GSH) or its conjugates can be hydrolysed to produce cysteinylglycine (CG, or CG conjugates) and free glutamate (L-Glu). Defects in GGT1 can cause glutathionuria (GLUTH; MIM:231950), an autosomal recessive disorder characterised by increased GSH concentration in the plasma and urine. Mutations that cause GLUTH can occur in both chains of the GGT1 dimer. R107H and R107Q in the heavy chain play a significant role in substrate binding rather than catalysis (Ikeda et al. 1993). S451A, S452A, D423A and D423E mutations in the light, catalytic chain of GGT1 completely or almost completely result in loss of function of the enzyme (Ikeda et al. 1995, Ikeda et al. 1995b).
Identifier: R-HSA-5602984
Species: Homo sapiens
Compartment: plasma membrane, extracellular region
To be excreted in urine, glutathione conjugates undergo several hydrolysis steps to form mercapturic acids which are readily excreted. The first step is the hydrolysis of a gamma-glutamyl residue from the conjugate catalysed by gamma-glutamyltransferases (GGTs). These are membrane-bound, heterodimeric enzymes composed of light and heavy peptide chains. Aflatoxin conjugates (AFXBO-SG, AFNBO-SG) can be hydrolysed in this way. Defects in GGT1 can cause glutathionuria (GLUTH; MIM:231950), an autosomal recessive disorder characterised by increased GSH concentration in the plasma and urine. Mutations that cause GLUTH can occur in both chains of the GGT1 dimer. R107H and R107Q in the heavy chain play a significant role in substrate binding rather than catalysis (Ikeda et al. 1993). S451A, S452A, D423A and D423E mutations in the light, catalytic chain of GGT1 completely or almost completely result in loss of function of the enzyme (Ikeda et al. 1995, Ikeda et al. 1995b).
Identifier: R-HSA-266046
Species: Homo sapiens
Compartment: plasma membrane, extracellular region
The reversible conversion of leukotriene C4 (LTC4) to leukotriene D4 (LTD4) is catalysed by gamma-glutamyl transferases 1 (GGT1) and 5 (GGT5). GGTs are present on the outer surface of plasma membranes and are a heterodimer of a heavy and a light chain. Its action involves the hydrolysis of the gamma-glutamyl peptide bond of glutathione and glutathione conjugates, releasing glutamate. In this example, LTC4 is a glutathione conjugate that is hydrolysed to LTD4 (Anderson et al. 1982, Wickham et al. 2011).
Identifier: R-HSA-5433072
Species: Homo sapiens
Compartment: extracellular region, plasma membrane
To be excreted in urine, glutathione conjugates undergo several hydrolysis steps to form mercapturic acids which are readily excreted. The first step is the hydrolysis of a gamma-glutamyl residue from the conjugate catalysed by gamma-glutamyltransferases (GGTs). These are membrane-bound, heterodimeric enzymes composed of light and heavy peptide chains. GGT1 and 2 are well characterised while GGT3P, 5, 6 and 7 are putative transferases. Extracellular glutathione or its conjugates can be hydrolysed to give cysteinylglycine (CG, or CG conjugates) and free glutamate (L-Glu) (Heisterkamp et al. 2008, Tate & Ross 1977, Pawlak et al. 1989).
Identifier: R-HSA-8943279
Species: Homo sapiens
Compartment: plasma membrane, extracellular region
GGT (gamma-glutamyl transpeptidase) dimers associated with the plasma membrane (Hanigan & Frierson 1996) hydrolyze extracellular glutathione (GSH) to form cysteinylglycine (CysGly) and glutamate (L-Glu). GGT1 has been extensively characterized. The active dimeric form of the enzyme is generated by autohydrolysis (West et al. 2011) and in vitro can catalyze both the reaction of GSH with water annotated here, and the reaction of GSH with a free amino acid or dipeptide to generate a gamma-glutamyl-amino acid and cysteinylglycine (Castonguay et al. 2007; Pawlak et al. 1989; Tate & Ross 1977; Thompson & Meister 1976). Based on amino acid sequence similarity, Heisterkamp et al. (2008) identified five additional dimeric proteins, GGT2, 3P, 5, 6, and 7, likely to catalyze the same reactions. West et al. (2013), however, found that GGT2 had no catalytic activity in vitro.

Interactor (1 results from a total of 1)

Identifier: P19440-3
Species: Homo sapiens
Primary external reference: UniProt: P19440-3
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