The mammlian enzyme is part of the cell antioxidant defense mechanism. It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels. The protein also has EC 3.4.19.13 (glutathione hydrolase) activity [3-4]. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions [3-4].
The mammlian enzyme is part of the cell antioxidant defense mechanism. It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels. The protein also has EC 3.4.19.13 (glutathione hydrolase) activity [3-4]. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions [3-4].
in the standard GGT assay with gamma-glutamyl p-nitroanilide as substrate, GGT1 accounts for 80% to 99% of the activity in all tissues except seeds where GGT2 is 50% of the activity
in the ggt1-1/ggt4-1/oxp1-1 triple mutant with no GGT activity in any organs except young siliques, the 5-oxoproline concentration in leaves is not different from that in oxp1-1 suggesting that GGTs are not major contributors to 5OP production in Arabidopsis
in the ggt1-1/ggt4-1/oxp1-1 triple mutant with no GGT activity in any organs except young siliques, the 5-oxoproline concentration in leaves is not different from that in oxp1-1 suggesting that GGTs are not major contributors to 5OP production in Arabidopsis
gamma-glutamyl transpeptidase 4 catalyzes the first step of vacuolar degradation of glutathione conjugates. Hydrolysis of glutathione S-bimane is blocked in ggt4 null mutants of Arabidopsis thaliana. Accumulation of glutathione S-bimane in mutants and in wild-type plants treated with the high affinity GGT inhibitor acivicin shows that GGT4 is required to initiate the two step hydrolysis sequence
gamma-glutamyl transpeptidase 4 catalyzes the first step of vacuolar degradation of glutathione conjugates. Hydrolysis of glutathione S-bimane is blocked in ggt4 null mutants of Arabidopsis thaliana. Accumulation of glutathione S-bimane in mutants and in wild-type plants treated with the high affinity GGT inhibitor acivicin shows that GGT4 is required to initiate the two step hydrolysis sequence
in the ggt1-1/ggt4-1/oxp1-1 triple mutant with no GGT activity in any organs except young siliques, the 5-oxoproline concentration in leaves is not different from that in oxp1-1 suggesting that GGTs are not major contributors to 5OP production in Arabidopsis
in the ggt1-1/ggt4-1/oxp1-1 triple mutant with no GGT activity in any organs except young siliques, the 5-oxoproline concentration in leaves is not different from that in oxp1-1 suggesting that GGTs are not major contributors to 5OP production in Arabidopsis
in the ggt1-1/ggt4-1/oxp1-1 triple mutant with no GGT activity in any organs except young siliques, the 5-oxoproline concentration in leaves is not different from that in oxp1-1 suggesting that GGTs are not major contributors to 5OP production in Arabidopsis
in the ggt1-1/ggt4-1/oxp1-1 triple mutant with no GGT activity in any organs except young siliques, the 5-oxoproline concentration in leaves is not different from that in oxp1-1 suggesting that GGTs are not major contributors to 5OP production in Arabidopsis
gamma-glutamyl transpeptidase 4 catalyzes the first step of vacuolar degradation of glutathione conjugates. Hydrolysis of glutathione S-bimane is blocked in ggt4 null mutants of Arabidopsis thaliana. Accumulation of glutathione S-bimane in mutants and in wild-type plants treated with the high affinity GGT inhibitor acivicin shows that GGT4 is required to initiate the two step hydrolysis sequence
gamma-glutamyl transpeptidase 4 catalyzes the first step of vacuolar degradation of glutathione conjugates. Hydrolysis of glutathione S-bimane is blocked in ggt4 null mutants of Arabidopsis thaliana. Accumulation of glutathione S-bimane in mutants and in wild-type plants treated with the high affinity GGT inhibitor acivicin shows that GGT4 is required to initiate the two step hydrolysis sequence
in the ggt1-1/ggt4-1/oxp1-1 triple mutant with no GGT activity in any organs except young siliques, the 5-oxoproline concentration in leaves is not different from that in oxp1-1 suggesting that GGTs are not major contributors to 5OP production in Arabidopsis
in the ggt1-1/ggt4-1/oxp1-1 triple mutant with no GGT activity in any organs except young siliques, the 5-oxoproline concentration in leaves is not different from that in oxp1-1 suggesting that GGTs are not major contributors to 5OP production in Arabidopsis
construction of transgenic Nicotiana tabacum plants via Agrobacterium tumefaciens transformation, functional extracellular overexpression of the Arabidopsis thaliana enzyme in leaves, transgenic and control plants show the same amount of glutathione degradation
construction of transgenic Nicotiana tabacum plants via Agrobacterium tumefaciens transformation, functional extracellular overexpression of the Arabidopsis thaliana enzyme in leaves, transgenic and control plants show the same amount of glutathione degradation
construction of transgenic Nicotiana tabacum plants via Agrobacterium tumefaciens transformation, functional extracellular overexpression of the Arabidopsis thaliana enzyme in leaves, transgenic and control plants show the same amount of glutathione degradation
construction of transgenic Nicotiana tabacum plants via Agrobacterium tumefaciens transformation, functional extracellular overexpression of the Arabidopsis thaliana enzyme in leaves, transgenic and control plants show the same amount of glutathione degradation
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform GGT2 expression is enhanced in ggt1 knockout mutants, suggesting a compensatory effect to restore enzyme activity in the root apoplast. Supplementation with 0.1 mM glutathione results in the 4fold up-regulation of isoform GGT2 gene expression