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Literature summary for 2.3.2.13 extracted from

  • Folk, J.E.
    The trimethylacetyl-transglutaminase complex (1982), Methods Enzymol., 87, 36-42.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic mechanism Cavia porcellus

Organism

Organism UniProt Comment Textmining
Cavia porcellus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 mechanism and structure Cavia porcellus
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 modified double displacement mechanism i.e. modified ping pong reaction Cavia porcellus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Cavia porcellus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
p-nitrophenyl trimethylacetate + H2O liver transglutaminase, ester hydrolysis in the presence of Ca2+ Cavia porcellus p-nitrophenol + trimethylacetate
-
?
protein-bound gamma-glutamine + alkylamine hydrolysis and aminolysis of certain aliphatic amides and active esters e.g. p-nitrophenyl esters and thiolesters Cavia porcellus protein N5-alkylglutamine + NH3
-
?