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Literature summary extracted from

  • Lu, D.; Futterer, K.; Korolev, S.; Zheng, X.; Tan, K.; Waksman, G.; Sadler, J.E.
    Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide (1999), J. Mol. Biol., 292, 361-373.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.21.9 crystal structure of the enteropeptidase catalytic domain to 2.3 A resolution in complex with the inhibitor Val-(Asp)4-Lys-chloromethane Bos taurus

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.9 K99A no cleavage of trypsinogen or Gly-(Asp)4-Lys-beta-naphthylamide and reduced rate of inhibition by Val-(Asp)4-Lys-chloromethane Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.9 Val-(Asp)4-Lys-chloromethane
-
 Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.9 0.05
-
 thiobenzyl benzyloxycarbonyl-L-lysinate mutant enzyme R99A Bos taurus
3.4.21.9 0.1
-
 thiobenzyl benzyloxycarbonyl-L-lysinate mutant enzyme K96A Bos taurus
3.4.21.9 0.12
-
 thiobenzyl benzyloxycarbonyl-L-lysinate
-
 Bos taurus
3.4.21.9 0.12
-
 thiobenzyl benzyloxycarbonyl-L-lysinate mutant enzyme R97A Bos taurus
3.4.21.9 0.14
-
 thiobenzyl benzyloxycarbonyl-L-lysinate mutant enzyme R98A Bos taurus
3.4.21.9 0.61
-
 Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
 Bos taurus
3.4.21.9 0.66
-
 Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide mutant enzyme K97A Bos taurus
3.4.21.9 0.77
-
 Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide mutant enzyme K98A Bos taurus
3.4.21.9 1.25
-
 Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide mutant enzyme K96A Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.9 membrane bound Bos taurus 16020
-

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 Bos taurus initiates activation of pancreatic hydrolases by cleaving and activating trypsinogen ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.9 Bos taurus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.9 additional information cleaves after Lys residues of peptidyl substrates that resemble trypsinogen activation peptides such as Val-(Asp)4-Lys Bos taurus ?
-
 ?
3.4.21.9 thiobenzyl benzyloxycarbonyl-L-lysinate + H2O
-
 Bos taurus ?
-
 ?
3.4.21.9 Trypsinogen + H2O initiates activation of pancreatic hydrolases by cleaving and activating trypsinogen Bos taurus ?
-
 ?
3.4.21.9 Val-Asp-Asp-Asp-Asp-Lys-2-naphthylamide + H2O
-
 Bos taurus ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.21.9 4.27
-
 Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
 Bos taurus
3.4.21.9 17.1
-
 Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide mutant enzyme K96A Bos taurus
3.4.21.9 25.5
-
 Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide mutant enzyme K97A Bos taurus
3.4.21.9 39.1
-
 Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide mutant enzyme K98A Bos taurus
3.4.21.9 108
-
 thiobenzyl benzyloxycarbonyl-L-lysinate mutant enzyme K96A Bos taurus
3.4.21.9 120
-
 thiobenzyl benzyloxycarbonyl-L-lysinate mutant enzyme R99A Bos taurus
3.4.21.9 128
-
 thiobenzyl benzyloxycarbonyl-L-lysinate mutant enzyme R97A Bos taurus
3.4.21.9 128
-
 thiobenzyl benzyloxycarbonyl-L-lysinate mutant enzyme R98A Bos taurus
3.4.21.9 129
-
 thiobenzyl benzyloxycarbonyl-L-lysinate
-
 Bos taurus