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Literature summary extracted from

  • Storozhenko, S.; Belles-Boix, E.; Babiychuk, E.; Herouart, D.; Davey, M.W.; Slooten, L.; Van Montagu, M.; Inze, D.; Kushnir, S.
    gamma-Glutamyl transpeptidase in transgenic tobacco plants. Cellular localization, processing, and biochemical properties (2002), Plant Physiol., 128, 1109-1119.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.2 overexpression as His-tagged protein in Escherichia coli JM109, DNA sequence analysis Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.2 additional information 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 Arabidopsis thaliana

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.2.2 4-nitroaniline strong, competitive against glutathione Arabidopsis thaliana

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.2.2 0.25
-
 glutathione
-
 Arabidopsis thaliana
2.3.2.2 0.8
-
 L-Glu-4-nitroanilide recombinant enzyme Arabidopsis thaliana

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.2.2 extracellular recombinant enzyme is extracellular in transgenic tabacco plants Arabidopsis thaliana
-
-
2.3.2.2 membrane membrane-bound Arabidopsis thaliana 16020
-
2.3.2.2 vacuole membrane-bound Arabidopsis thaliana 5773
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.2.2 additional information
-
 amino acid sequence alignment, enzyme gene family Arabidopsis thaliana
2.3.2.2 additional information
-
 amino acid sequence alignment, enzyme gene family Homo sapiens
2.3.2.2 additional information
-
 amino acid sequence alignment, enzyme gene family Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.2 glutathione + an amino acid Arabidopsis thaliana initial step of glutathione degradation L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
 ?
2.3.2.2 L-Glu-4-nitroanilide + glutathione Arabidopsis thaliana L-Glu-4-nitroanilide is a suicide substrate 4-nitroaniline + 5-L-glutamyl-glutathione
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.2 Arabidopsis thaliana
-
-
-
2.3.2.2 Arabidopsis thaliana O65652
-
-
2.3.2.2 Arabidopsis thaliana Q39078
-
-
2.3.2.2 Arabidopsis thaliana Q9M0G0
-
-
2.3.2.2 Homo sapiens P19440
-
-
2.3.2.2 Mus musculus Q60928
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.2 recombinant His-tagged enzyme from E. coli Arabidopsis thaliana

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.2 (5-L-glutamyl)-peptide + acceptor + H+
-
 Arabidopsis thaliana peptide + 5-L-glutamyl amino acid
-
 ?
2.3.2.2 5-D-glutamyl-4-nitroanilide + acceptor
-
 Arabidopsis thaliana 4-nitroaniline + 5-D-glutamyl-acceptor
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + glycylglycine
-
 Arabidopsis thaliana 4-nitroaniline + 5-L-glutamylglycylglycine
-
 ?
2.3.2.2 5-L-glutamyl-7-amido-4-methylcoumarin + acceptor
-
 Arabidopsis thaliana 7-amino-4-methylcoumarin + 5-L-glutamyl-acceptor
-
 ?
2.3.2.2 glutathione + an amino acid initial step of glutathione degradation Arabidopsis thaliana L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
 ?
2.3.2.2 L-Glu-4-nitroanilide + glutathione L-Glu-4-nitroanilide is a suicide substrate Arabidopsis thaliana 4-nitroaniline + 5-L-glutamyl-glutathione
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.3.2.2 0.25
-
 4-nitroaniline
-
 Arabidopsis thaliana