BRENDA - Enzyme Database

Characterization of gamma-glutamyl transpeptidase from the Rathke's gland secretions of Kemp's ridley sea turtles (Lepidochelys kempi)

Krishna, R.G.; Chin, C.C.Q.; Weldon, P.J.; Wold, F.; Comp. Biochem. Physiol. B 111, 257-264 (1995) View publication on PubMed

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
2.3.2.2
Maleate
-
Lepidochelys kempii
Inhibitors
EC Number
Inhibitors
Commentary
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
Commentary
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]
Commentary
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
Commentary
Textmining
2.3.2.2
Lepidochelys kempii
-
Kemp's ridley sea-turtle
-
Purification (Commentary)
EC Number
Purification (Commentary)
Organism
2.3.2.2
from secretion
Lepidochelys kempii
Source Tissue
EC Number
Source Tissue
Commentary
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]
Commentary
Organism
2.3.2.2
2213
-
purified enzyme
Lepidochelys kempii
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
2.3.2.2
(5-L-glutamyl)-peptide + acceptor + H+
concurrent reaction: hydrolase reaction with H2O as acceptor
487959
Lepidochelys kempii
peptide + 5-L-glutamyl amino acid
-
487959
Lepidochelys kempii
?
2.3.2.2
(5-L-glutamyl)-peptide + acceptor + H+
best acceptors: free amino acids
487959
Lepidochelys kempii
peptide + 5-L-glutamyl amino acid
-
487959
Lepidochelys kempii
?
2.3.2.2
(5-L-glutamyl)-peptide + acceptor + H+
acceptor specificity, overview
487959
Lepidochelys kempii
peptide + 5-L-glutamyl amino acid
-
487959
Lepidochelys kempii
?
2.3.2.2
(5-L-glutamyl)-peptide + acceptor + H+
donor specificity, overview
487959
Lepidochelys kempii
peptide + 5-L-glutamyl amino acid
-
487959
Lepidochelys kempii
?
2.3.2.2
5-L-glutamyl-L-alanine + 5-L-glutamyl-L-alanine
shows also hydrolase activity with this substrate
487959
Lepidochelys kempii
L-glutamine + 5-L-glutamyl-L-glutamyl-L-alanine
-
487959
Lepidochelys kempii
?
2.3.2.2
5-L-glutamyl-L-lysine + acceptor
shows also hydrolase activity with this substrate
487959
Lepidochelys kempii
L-lysine + 5-L-glutamyl-acceptor
-
487959
Lepidochelys kempii
?
2.3.2.2
glutathione + acceptor
-
487959
Lepidochelys kempii
cysteinylglycine + 5-L-glutamyl-acceptor
-
-
-
?
2.3.2.2
S-methylglutathione + acceptor
shows also hydrolase activity with this substrate
487959
Lepidochelys kempii
S-methyl-L-cysteinylglycine + 5-L-glutamyl-acceptor
-
487959
Lepidochelys kempii
?
Subunits
EC Number
Subunits
Commentary
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]
Commentary
Organism
2.3.2.2
37
-
assay at
Lepidochelys kempii
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.3.2.2
8.5
-
assay at
Lepidochelys kempii
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
2.3.2.2
Maleate
-
Lepidochelys kempii
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
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 (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.3.2.2
extracellular
secretion of Rathke's gland
Lepidochelys kempii
-
-
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
2.3.2.2
from secretion
Lepidochelys kempii
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
2.3.2.2
gland
secretions of Rathke's gland
Lepidochelys kempii
-
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.3.2.2
2213
-
purified enzyme
Lepidochelys kempii
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
2.3.2.2
(5-L-glutamyl)-peptide + acceptor + H+
concurrent reaction: hydrolase reaction with H2O as acceptor
487959
Lepidochelys kempii
peptide + 5-L-glutamyl amino acid
-
487959
Lepidochelys kempii
?
2.3.2.2
(5-L-glutamyl)-peptide + acceptor + H+
best acceptors: free amino acids
487959
Lepidochelys kempii
peptide + 5-L-glutamyl amino acid
-
487959
Lepidochelys kempii
?
2.3.2.2
(5-L-glutamyl)-peptide + acceptor + H+
acceptor specificity, overview
487959
Lepidochelys kempii
peptide + 5-L-glutamyl amino acid
-
487959
Lepidochelys kempii
?
2.3.2.2
(5-L-glutamyl)-peptide + acceptor + H+
donor specificity, overview
487959
Lepidochelys kempii
peptide + 5-L-glutamyl amino acid
-
487959
Lepidochelys kempii
?
2.3.2.2
5-L-glutamyl-L-alanine + 5-L-glutamyl-L-alanine
shows also hydrolase activity with this substrate
487959
Lepidochelys kempii
L-glutamine + 5-L-glutamyl-L-glutamyl-L-alanine
-
487959
Lepidochelys kempii
?
2.3.2.2
5-L-glutamyl-L-lysine + acceptor
shows also hydrolase activity with this substrate
487959
Lepidochelys kempii
L-lysine + 5-L-glutamyl-acceptor
-
487959
Lepidochelys kempii
?
2.3.2.2
glutathione + acceptor
-
487959
Lepidochelys kempii
cysteinylglycine + 5-L-glutamyl-acceptor
-
-
-
?
2.3.2.2
S-methylglutathione + acceptor
shows also hydrolase activity with this substrate
487959
Lepidochelys kempii
S-methyl-L-cysteinylglycine + 5-L-glutamyl-acceptor
-
487959
Lepidochelys kempii
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
2.3.2.2
?
x * 54000 + x * 21000, SDS-PAGE
Lepidochelys kempii
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
2.3.2.2
37
-
assay at
Lepidochelys kempii
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.3.2.2
8.5
-
assay at
Lepidochelys kempii