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Literature summary for 2.3.2.2 extracted from

  • Krishna, R.G.; Chin, C.C.Q.; Weldon, P.J.; Wold, F.
    Characterization of gamma-glutamyl transpeptidase from the Rathke's gland secretions of Kemp's ridley sea turtles (Lepidochelys kempi) (1995), Comp. Biochem. Physiol. B, 111, 257-264.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Maleate
-
Lepidochelys kempii

Inhibitors

Inhibitors Comment Organism Structure
5,5'-dithiobis(2-nitrobenzoate) no inhibition Lepidochelys kempii
N-ethylmaleimide no inhibition Lepidochelys kempii
p-chloromercuribenzoate no inhibition Lepidochelys kempii
tosyl fluoride inhibition by tosyl fluoride only in presence of maleate Lepidochelys kempii

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular secretion of Rathke's gland Lepidochelys kempii
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
21000
-
x * 54000 + x * 21000, SDS-PAGE Lepidochelys kempii
54000
-
x * 54000 + x * 21000, SDS-PAGE Lepidochelys kempii
200000
-
gel filtration Lepidochelys kempii

Organism

Organism UniProt Comment Textmining
Lepidochelys kempii
-
Kemp's ridley sea-turtle
-

Purification (Commentary)

Purification (Comment) Organism
from secretion Lepidochelys kempii

Source Tissue

Source Tissue Comment Organism Textmining
gland secretions of Rathke's gland Lepidochelys kempii
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2213
-
purified enzyme Lepidochelys kempii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(5-L-glutamyl)-peptide + acceptor + H+ concurrent reaction: hydrolase reaction with H2O as acceptor Lepidochelys kempii peptide + 5-L-glutamyl amino acid
-
?
(5-L-glutamyl)-peptide + acceptor + H+ best acceptors: free amino acids Lepidochelys kempii peptide + 5-L-glutamyl amino acid
-
?
(5-L-glutamyl)-peptide + acceptor + H+ acceptor specificity, overview Lepidochelys kempii peptide + 5-L-glutamyl amino acid
-
?
(5-L-glutamyl)-peptide + acceptor + H+ donor specificity, overview Lepidochelys kempii peptide + 5-L-glutamyl amino acid
-
?
5-L-glutamyl-L-alanine + 5-L-glutamyl-L-alanine shows also hydrolase activity with this substrate Lepidochelys kempii L-glutamine + 5-L-glutamyl-L-glutamyl-L-alanine
-
?
5-L-glutamyl-L-lysine + acceptor shows also hydrolase activity with this substrate Lepidochelys kempii L-lysine + 5-L-glutamyl-acceptor
-
?
glutathione + acceptor
-
Lepidochelys kempii cysteinylglycine + 5-L-glutamyl-acceptor
-
?
S-methylglutathione + acceptor shows also hydrolase activity with this substrate Lepidochelys kempii S-methyl-L-cysteinylglycine + 5-L-glutamyl-acceptor
-
?

Subunits

Subunits Comment Organism
? x * 54000 + x * 21000, SDS-PAGE Lepidochelys kempii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Lepidochelys kempii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Lepidochelys kempii