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Literature summary extracted from

  • Maroux, S.; Baratti, J.; Desnuelle, P.
    Purification and specificity of porcine enterokinase (1971), J. Biol. Chem., 246, 5031-5039.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.9 alpha-tosyl-lysine chloromethyl ketone
-
 Sus scrofa
3.4.21.9 diisopropylphosphorofluoridate
-
 Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.9 0.07
-
 Trypsinogen bovine trypsinogen Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.9 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.9
-
 Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.21.9 duodenum
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.9 benzoyl-Arg ethyl ester + H2O
-
 Sus scrofa benzoyl-Arg + ethanol
-
 ?
3.4.21.9 Tosyl-Arg methyl ester + H2O
-
 Sus scrofa Tosyl-Arg + methanol
-
 ?
3.4.21.9 trypsinogen + H2O the specificity site of enterokinase recognizes in trypsinogen not merely the basic residue of the -Lys6-/-Ile7-bond, which is split during activation of the zymogen but also recognizes the sequence -Asp4-Lys, residues 2 to 6, which is present in all of the trypsinogens so far studied Sus scrofa trypsin + ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.21.9 4.8
-
 Trypsinogen bovine trypsinogen Sus scrofa
3.4.21.9 8.1
-
 tosyl-Arg methyl ester
-
 Sus scrofa
3.4.21.9 28.4
-
 benzoyl-Arg ethyl ester
-
 Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.9 6 9 activity rises sharply between pH 5 and 6 and then remains maximal until pH 9 Sus scrofa