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Literature summary extracted from

  • Matsushima, M.; Ichinose, M.; Yahagi, N.; Tsukada-Kato, S.; Miki, K.; Omata, M.; Kim, Y.T.; Ito, H.; Takahashi, T.; Sakurai, Y.; Tsuchiya, Y.; Athauda, S.B.P.; Inoue, H.; Takahashi, K.
    Purification and further characterization of enteropeptidase from porcine duodenum (1999), J. Biochem., 125, 947-951.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.9 antipain
-
 Sus scrofa
3.4.21.9 Aprotinin
-
 Sus scrofa
3.4.21.9 benzamidine
-
 Sus scrofa
3.4.21.9 diisopropylphosphorofluoridate
-
 Sus scrofa
3.4.21.9 trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
 Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.9 1.12
-
 Gly-Asp-ASp-Asp-Asp-2-naphthylamide
-
 Sus scrofa
3.4.21.9 1.24
-
 benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
-
 Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.9 membrane bound Sus scrofa 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.9 CoCl2 activates Sus scrofa
3.4.21.9 HgCl2 activates Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.9 Trypsinogen + H2O Sus scrofa
-
 ?
-
 ?

Organism

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

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.21.9 side-chain modification glycosylated mainly with N-linked carbohydrate chains of the triantennary and tetraantennary complex type 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 mucosa Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.9 benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl 7-amide + H2O
-
 Sus scrofa ?
-
 ?
3.4.21.9 Gly-Asp-ASp-Asp-Asp-2-naphthylamide + H2O
-
 Sus scrofa Gly-Asp-ASp-Asp-Asp + 2-naphthylamine
-
 ?
3.4.21.9 Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide + H2O
-
 Sus scrofa Gly-Asp-Asp-Asp-Asp-Lys + 2-naphthylamine
-
 ?
3.4.21.9 Lys-2-naphthylamide + H2O
-
 Sus scrofa Lys + 2-naphthylamine
-
 ?
3.4.21.9 additional information acidic residues at the P2, P3 and/or P4 position are especially favorable for maximal activity, but are not absolutely necessary Sus scrofa ?
-
 ?
3.4.21.9 tert-butoxycarbonyl-Gln-Ala-Arg-4-methylcoumarin 7-amide + H2O weak activity Sus scrofa ?
-
 ?
3.4.21.9 tert-butoxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumaryl 7-amide + H2O
-
 Sus scrofa ?
-
 ?
3.4.21.9 tert-butoxycarbonyl-Leu-Thr-Arg-4-methylcoumarin 7-amide + H2O weak activity Sus scrofa ?
-
 ?
3.4.21.9 tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin 7-amide + H2O weak activity Sus scrofa ?
-
 ?
3.4.21.9 tert-butoxycarbonyl-Val-Leu-Lys-4-methylcoumarin 7-amide + H2O weak activity Sus scrofa ?
-
 ?
3.4.21.9 Trypsinogen + H2O
-
 Sus scrofa ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.21.9 262
-
 benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
-
 Sus scrofa
3.4.21.9 520
-
 Gly-Asp-ASp-Asp-Asp-2-naphthylamide
-
 Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.9 8
-
 hydrolysis of Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide Sus scrofa

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.21.9 6.4 9 50% of maximal activity at pH 6.4 and at pH 9.0, hydrolysis of Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide Sus scrofa