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Literature summary for 3.4.21.9 extracted from

  • Chun, H.; Joo, K.; Lee, J.; Shin, H.C.
    Design and efficient production of bovine enterokinase light chain with higher specificity in E. coli (2011), Biotechnol. Lett., 33, 1227-1232.
    View publication on PubMed
Search for more literature for 3.4.21.9

Application

Application Comment Organism
additional information utility of enterokinase light chain as a site-specific cleavage enzyme is hampered by sporadic cleavage at other sites than the canonical D4K recognition sequence Bos taurus

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enterokinase light chain in Escherichia coli strain Rosetta (DE3) Bos taurus

Protein Variants

Protein Variants Comment Organism
additional information in order to produce more site-specific enterokinase light chain, EKL, several mutants are generated with substitutions at Tyr174 and Lys99 using the protein disulfide isomerase fusion system. Substitution of Tyr174 by basic residues confers higher specificity on EKL. Mutant enzyme substrate specificity and modeling, overview Bos taurus
Y174K site-directed mutagenesis, Bos taurus
Y174K/K99M site-directed mutagenesis, the mutant does not form the active structure Bos taurus
Y174K/K99Q site-directed mutagenesis, the mutantion results in a more site-specific enterokinase light chain Bos taurus
Y174R site-directed mutagenesis, Bos taurus
Y174R/K99M site-directed mutagenesis, the mutant does not form the active structure Bos taurus
Y174R/K99Q site-directed mutagenesis, the mutant does not form the active structure Bos taurus

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bos taurus enterokinase light chain is a serine protease that recognizes Asp-Asp-Asp-Asp-Lys, D4K, sequence and cleaves the C-terminal peptide bond of the lysine residue ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
duodenum mucosa Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide + H2O
-
 Bos taurus Gly-Asp-Asp-Asp-Asp-Lys + 2-naphthylamine
-
 ?
Gly-Asp-Asp-Asp-Asp-Lys-Ile-Val-Gly-Gly + H2O
-
 Bos taurus Gly-Asp-Asp-Asp-Asp-Lys + Ile-Val-Gly-Gly
-
 ?
Gly-Gly-Asp-Asp-Asp-Lys-Ile-Val-Gly-Gly + H2O
-
 Bos taurus Gly-Gly-Asp-Asp-Asp-Lys + Ile-Val-Gly-Gly
-
 ?
Gly-Gly-Gly-Asp-Asp-Lys-Ile-Val-Gly-Gly + H2O
-
 Bos taurus Gly-Gly-Gly-Asp-Asp-Lys + Ile-Val-Gly-Gly
-
 ?
Gly-Gly-Gly-Gly-Asp-Lys-Ile-Val-Gly-Gly + H2O
-
 Bos taurus Gly-Gly-Gly-Gly-Asp-Lys + Ile-Val-Gly-Gly
-
 ?
additional information enterokinase light chain is a serine protease that recognizes Asp-Asp-Asp-Asp-Lys, D4K, sequence and cleaves the C-terminal peptide bond of the lysine residue Bos taurus ?
-
 ?

Synonyms

Synonyms Comment Organism
enterokinase
-
 Bos taurus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Bos taurus

General Information

General Information Comment Organism
additional information enterokinase shows no strict cleavage site specificity because of sporadic cleavage at other sites, which consist of acidic and basic residues Bos taurus