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Literature summary for 3.4.21.9 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
Search for more literature for 3.4.21.9

Inhibitors

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
duodenum
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzoyl-Arg ethyl ester + H2O
-
 Sus scrofa benzoyl-Arg + ethanol
-
 ?
Tosyl-Arg methyl ester + H2O
-
 Sus scrofa Tosyl-Arg + methanol
-
 ?
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]

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

pH Optimum

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