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Literature summary extracted from

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

KM Value [mM]

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

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.13 Cavia porcellus
-
-
-

Reaction

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.2.13 liver
-
 Cavia porcellus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.13 p-nitrophenyl trimethylacetate + H2O liver transglutaminase, ester hydrolysis in the presence of Ca2+ Cavia porcellus p-nitrophenol + trimethylacetate
-
 ?
2.3.2.13 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
-
 ?