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Literature summary for 2.3.2.2 extracted from

  • Dvorakova, L.; Krusek, J.; Stastny, F.; Lisy, V.
    Relationship between kinetic properties of gamma-glutamyl transpeptidase and the structure of its saccharide moiety (1996), Biochim. Biophys. Acta, 1292, 163-167.
    View publication on PubMed
Search for more literature for 2.3.2.2

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic study Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-bound Rattus norvegicus 16020
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
 Wistar, female
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein heterogenous, tissue-dependent glycosylation pattern Rattus norvegicus
glycoprotein binding of concanavalin A Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
partial Rattus norvegicus
Triton X-100 Rattus norvegicus

Reaction

Reaction Comment Organism Reaction ID
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid kinetic study Rattus norvegicus
a

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Rattus norvegicus
-
kidney
-
 Rattus norvegicus
-
pancreas
-
 Rattus norvegicus
-
spleen
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(5-L-glutamyl)-peptide + acceptor + H+
-
 Rattus norvegicus peptide + 5-L-glutamyl amino acid
-
 ?

Synonyms

Synonyms Comment Organism
GGT
-
 Rattus norvegicus