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Literature summary for 3.4.21.9 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)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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

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

KM Value [mM]

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

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Trypsinogen + H2O Bos taurus initiates activation of pancreatic hydrolases by cleaving and activating trypsinogen ?
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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