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Literature summary for 2.3.2.2 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)

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

Protein Variants

Protein Variants Comment Organism
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

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

KM Value [mM]

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

Localization

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Ki Value [mM]

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