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Literature summary for 2.3.2.2 extracted from

  • Castonguay, R.; Lherbet, C.; Keillor, J.W.
    Mapping of the active site of rat kidney gamma-glutamyl transpeptidase using activated esters and their amide derivatives (2002), Bioorg. Med. Chem., 10, 4185-4191.
    View publication on PubMed
Search for more literature for 2.3.2.2

Inhibitors

Inhibitors Comment Organism Structure
4-aminobutyramide
-
 Rattus norvegicus
4-carboxybutyramide and derivatives Rattus norvegicus
additional information inhibition mechanism Rattus norvegicus
N-acetyl-L-glutamine poor inhibitor, competitive Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Rattus norvegicus

Reaction

Reaction Comment Organism Reaction ID
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid active site Rattus norvegicus
a
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid almost the entire glutamyl moiety is necessary for recognition in the binding site of the donor substrate Rattus norvegicus
a

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(5-L-glutamyl)-peptide + acceptor + H+ Glu-donor is 5-L-Glu-4-nitroanilide Rattus norvegicus peptide + 5-L-glutamyl amino acid
-
 ?
additional information ester and amide derivatives of L-Glu-4-nitroanilide are no substrates, overview Rattus norvegicus ?
-
 ?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information Ki-values for derivatives of 4-acrboxybutyramide, overview Rattus norvegicus
12.6
-
 4-carboxybutyramide
-
 Rattus norvegicus
23.2
-
 4-aminobutyramide
-
 Rattus norvegicus