Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Horiuchi, S.; Inoue, M.; Morino, Y.
    Latent active site in rat-kidney gamma-glutamyl transpeptidase. The refolding process of the large subunit and characterization of the renatured enzyme (1980), Eur. J. Biochem., 105, 93-102.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.2.2 6-diazo-5-oxo-L-norleucine inactivation of kidney enzyme Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.2.2 additional information
-
 additional information kinetic study of renatured large subunit Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.2.2 20000
-
 1 * 48000 + 1 * 20000, about, gel filtration of denatured and native enzyme Rattus norvegicus
2.3.2.2 48000
-
 1 * 48000 + 1 * 20000, about, gel filtration of denatured and native enzyme Rattus norvegicus
2.3.2.2 68000
-
 gel filtration Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.2 Rattus norvegicus
-
 Wistar
-
2.3.2.2 Rattus norvegicus Wistar
-
 Wistar
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid structure Rattus norvegicus
a
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid active site on small subunit Rattus norvegicus
a

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.3.2.2 renaturation as catalytically active enzyme after inactivation with 6-diazo-5-oxo-L-norleucine, requires glutathione or S-methyl derivative as a substrate ligand, circular dichroic spectra Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.2.2 kidney
-
 Rattus norvegicus
-

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+ donor: GSH S-substituted derivatives Rattus norvegicus peptide + 5-L-glutamyl amino acid
-
 ?
2.3.2.2 (5-L-glutamyl)-peptide + acceptor + H+ Glu-donor is 5-L-Glu-4-nitroanilide Rattus norvegicus peptide + 5-L-glutamyl amino acid
-
 ?
2.3.2.2 (5-L-glutamyl)-peptide + acceptor + H+ Glu-donor is GSH Rattus norvegicus peptide + 5-L-glutamyl amino acid
-
 ?
2.3.2.2 (5-L-glutamyl)-peptide + acceptor + H+ donor: GSH S-substituted derivatives Rattus norvegicus Wistar peptide + 5-L-glutamyl amino acid
-
 ?
2.3.2.2 (5-L-glutamyl)-peptide + acceptor + H+ Glu-donor is 5-L-Glu-4-nitroanilide Rattus norvegicus Wistar peptide + 5-L-glutamyl amino acid
-
 ?
2.3.2.2 (5-L-glutamyl)-peptide + acceptor + H+ Glu-donor is GSH Rattus norvegicus Wistar peptide + 5-L-glutamyl amino acid
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + glycylglycine
-
 Rattus norvegicus 4-nitroaniline + 5-L-glutamylglycylglycine
-
 ?
2.3.2.2 5-L-glutamyl-4-nitroanilide + glycylglycine
-
 Rattus norvegicus Wistar 4-nitroaniline + 5-L-glutamylglycylglycine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.2.2 dimer 1 * 48000 + 1 * 20000, about, gel filtration of denatured and native enzyme Rattus norvegicus
2.3.2.2 More the active site resides on the small subunit Rattus norvegicus
2.3.2.2 More the enzyme is composed of two non-identical catalytically active subunits Rattus norvegicus

Temperature Optimum [°C]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.2 8.5
-
 assay at Rattus norvegicus