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Literature summary 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

EC Number Activating Compound Comment Organism Structure
2.3.2.2 Maleate
-
Lepidochelys kempii

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.2.2 5,5'-dithiobis(2-nitrobenzoate) no inhibition Lepidochelys kempii
2.3.2.2 N-ethylmaleimide no inhibition Lepidochelys kempii
2.3.2.2 p-chloromercuribenzoate no inhibition Lepidochelys kempii
2.3.2.2 tosyl fluoride inhibition by tosyl fluoride only in presence of maleate Lepidochelys kempii

Localization

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.2.2 21000
-
x * 54000 + x * 21000, SDS-PAGE Lepidochelys kempii
2.3.2.2 54000
-
x * 54000 + x * 21000, SDS-PAGE Lepidochelys kempii
2.3.2.2 200000
-
gel filtration Lepidochelys kempii

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.2 from secretion Lepidochelys kempii

Source Tissue

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.2.2 2213
-
purified enzyme Lepidochelys kempii

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+ concurrent reaction: hydrolase reaction with H2O as acceptor Lepidochelys kempii peptide + 5-L-glutamyl amino acid
-
?
2.3.2.2 (5-L-glutamyl)-peptide + acceptor + H+ best acceptors: free amino acids Lepidochelys kempii peptide + 5-L-glutamyl amino acid
-
?
2.3.2.2 (5-L-glutamyl)-peptide + acceptor + H+ acceptor specificity, overview Lepidochelys kempii peptide + 5-L-glutamyl amino acid
-
?
2.3.2.2 (5-L-glutamyl)-peptide + acceptor + H+ donor specificity, overview Lepidochelys kempii peptide + 5-L-glutamyl amino acid
-
?
2.3.2.2 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
-
?
2.3.2.2 5-L-glutamyl-L-lysine + acceptor shows also hydrolase activity with this substrate Lepidochelys kempii L-lysine + 5-L-glutamyl-acceptor
-
?
2.3.2.2 glutathione + acceptor
-
Lepidochelys kempii cysteinylglycine + 5-L-glutamyl-acceptor
-
?
2.3.2.2 S-methylglutathione + acceptor shows also hydrolase activity with this substrate Lepidochelys kempii S-methyl-L-cysteinylglycine + 5-L-glutamyl-acceptor
-
?

Subunits

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.2 37
-
assay at Lepidochelys kempii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.2 8.5
-
assay at Lepidochelys kempii