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Literature summary extracted from

  • Castellano, I.; Merlino, A.; Rossi, M.; La Cara, F.
    Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: An enzyme specialized in hydrolase activity (2010), Biochimie, 92, 464-474.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.2 expression in Escherichia coli Geobacillus thermodenitrificans
3.4.19.9 expressed as a fusion protein containing a C-terminal His-tag in Escherichia coli Geobacillus thermodenitrificans
3.4.19.9 expression in Escherichia coli Geobacillus thermodenitrificans

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.2 T353A mutation of the N-terminal residue of the 21 kDa subunit, abolishes the post-translational cleavage of the pro-enzyme, but does not completely block the hydrolytic action Geobacillus thermodenitrificans
3.4.19.9 T353A mutation of the N-terminal residue of the 21 kDa subunit, abolishes the post-translational cleavage of the pro-enzyme, but does not completely block the hydrolytic action Geobacillus thermodenitrificans
3.4.19.9 T353A mutation abolishes the post-translational cleavage of the pro-enzyme, but does not completely block the hydrolytic action Geobacillus thermodenitrificans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.19.9 0.0076
-
 5-L-glutamyl-4-nitroanilide pH 7.8, 52°C Geobacillus thermodenitrificans
3.4.19.9 0.0076
-
 L-glutamic acid gamma-(4-nitroanilide) Vmax: 0.36 micromol/min/mg Geobacillus thermodenitrificans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.2.2 21000
-
 2 * 40000 + 2 * 21000, SDS-PAGE. The unprocessed enzyme forms an already active homotetramer, whereas the mature enzyme is a fully active compact alpha2beta2-heterotetramer Geobacillus thermodenitrificans
2.3.2.2 40000
-
 2 * 40000 + 2 * 21000, SDS-PAGE. The unprocessed enzyme forms an already active homotetramer, whereas the mature enzyme is a fully active compact alpha2beta2-heterotetramer Geobacillus thermodenitrificans
2.3.2.2 103000
-
 gel filtration Geobacillus thermodenitrificans
3.4.19.9 21000
-
 SDS-PAGE, shorter subunit after post-translational modification Geobacillus thermodenitrificans
3.4.19.9 40000
-
 SDS-PAGE, shorter subunit after post-translational modification Geobacillus thermodenitrificans
3.4.19.9 44000
-
 gel filtration Geobacillus thermodenitrificans
3.4.19.9 61000
-
 SDS-PAGE, precursor homotetrameric protein of 61000 Da per subunit Geobacillus thermodenitrificans
3.4.19.9 103000
-
 gel filtration Geobacillus thermodenitrificans
3.4.19.9 222000
-
 gel filtration Geobacillus thermodenitrificans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.19.9 glutathione + H2O Geobacillus thermodenitrificans enzyme hydrolyses the physiological antioxidant glutathione, suggesting an involvement of the enzyme in the cellular defense mechanism against oxidative stress ?
-
 ?
3.4.19.9 glutathione + H2O Geobacillus thermodenitrificans NG80-2 enzyme hydrolyses the physiological antioxidant glutathione, suggesting an involvement of the enzyme in the cellular defense mechanism against oxidative stress ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.2 Geobacillus thermodenitrificans
-
-
-
2.3.2.2 Geobacillus thermodenitrificans NG80-2
-
-
-
3.4.19.9 Geobacillus thermodenitrificans
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.3.2.2 proteolytic modification the enzyme is synthesized as a precursor homotetrameric protein of 60-kDa per subunit, and undergoes an internal post-translational cleavage of the 60 kDa monomer into 40- and 21-kDa shorter subunits, which are then assembled into an active heterotetramer composed of two 40- and two 21-kDa subunits Geobacillus thermodenitrificans
3.4.19.9 proteolytic modification the enzyme is synthesized as a precursor homotetrameric protein of 60 kDa per subunit, and undergoes an internal post-translational cleavage of the 60 kDa monomer into 40 kDa and 21 kDa shorter subunits, which are then assembled into an active heterotetramer composed of two 40 kDa and two 21 kDa subunits Geobacillus thermodenitrificans
3.4.19.9 proteolytic modification precursor homotetrameric protein of 61000 Da per subunit undergoes an internal post-translational cleavage into 40 and 21 kDa shorter subunits, which are then assembled into an active heterotetramer composed of two 40 and two 21 kDa subunits Geobacillus thermodenitrificans

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.19.9 using Ni-NTA chromatography Geobacillus thermodenitrificans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.2 glutathione + H2O L-glutamate is transferred to H2O, c.f. EC 3.4.19.9 Geobacillus thermodenitrificans L-cysteinylglycine + L-glutamate
-
 ?
2.3.2.2 glutathione + H2O L-glutamate is transferred to H2O, c.f. EC 3.4.19.9 Geobacillus thermodenitrificans NG80-2 L-cysteinylglycine + L-glutamate
-
 ?
2.3.2.2 additional information enzyme does not show any transpeptidase activity Geobacillus thermodenitrificans ?
-
 ?
2.3.2.2 additional information enzyme does not show any transpeptidase activity Geobacillus thermodenitrificans NG80-2 ?
-
 ?
3.4.19.9 5-L-glutamyl-4-nitroanilide + H2O
-
 Geobacillus thermodenitrificans L-glutamic acid + 4-nitroaniline
-
 ?
3.4.19.9 glutathione + H2O
-
 Geobacillus thermodenitrificans ?
-
 ?
3.4.19.9 glutathione + H2O enzyme hydrolyses the physiological antioxidant glutathione, suggesting an involvement of the enzyme in the cellular defense mechanism against oxidative stress Geobacillus thermodenitrificans ?
-
 ?
3.4.19.9 glutathione + H2O
-
 Geobacillus thermodenitrificans NG80-2 ?
-
 ?
3.4.19.9 glutathione + H2O enzyme hydrolyses the physiological antioxidant glutathione, suggesting an involvement of the enzyme in the cellular defense mechanism against oxidative stress Geobacillus thermodenitrificans NG80-2 ?
-
 ?
3.4.19.9 L-glutamic acid gamma-(4-nitroanilide) + H2O
-
 Geobacillus thermodenitrificans L-glutamic acid + 4-nitroaniline
-
 ?
3.4.19.9 additional information enzyme does not show any transpeptidase activity Geobacillus thermodenitrificans ?
-
 ?
3.4.19.9 additional information enzyme does not show any transpeptidase activity Geobacillus thermodenitrificans NG80-2 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.2.2 tetramer 2 * 40000 + 2 * 21000, SDS-PAGE. The unprocessed enzyme forms an already active homotetramer, whereas the mature enzyme is a fully active compact alpha2beta2-heterotetramer Geobacillus thermodenitrificans
3.4.19.9 heterotetramer 2 * 21000, 2 * 40000, SDS-PAGE Geobacillus thermodenitrificans
3.4.19.9 homotetramer 4 * 61000 Da, SDS-PAGE Geobacillus thermodenitrificans
3.4.19.9 tetramer 2 * 40000 + 2 * 21000, SDS-PAGE. The unprocessed enzyme forms an already active homotetramer, whereas the mature enzyme is a fully active compact alpha2beta2-heterotetramer Geobacillus thermodenitrificans

Synonyms

EC Number Synonyms Comment Organism
3.4.19.9 gamma-glutamyl hydrolase
-
 Geobacillus thermodenitrificans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.2 52
-
-
 Geobacillus thermodenitrificans
3.4.19.9 52
-
-
 Geobacillus thermodenitrificans

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.2.2 45
-
 24 h, 83% residual activity Geobacillus thermodenitrificans
3.4.19.9 45
-
 24 h, 83% residual activity Geobacillus thermodenitrificans
3.4.19.9 45
-
 pH 7.8, GthGT retains 83% of the activity after 24 h incubation Geobacillus thermodenitrificans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.2 7.8
-
-
 Geobacillus thermodenitrificans
3.4.19.9 7.8
-
-
 Geobacillus thermodenitrificans