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Literature summary for 3.4.21.9 extracted from

  • Yuan, L.D.; Hua, Z.C.
    Expression, purification, and characterization of a biologically active bovine enterokinase catalytic subunit in Escherichia coli (2002), Protein Expr. Purif., 25, 300-304.
    View publication on PubMed

Application

Application Comment Organism
synthesis useful tool for in vitro cleavage of fusion proteins Bos taurus

Cloned(Commentary)

Cloned (Comment) Organism
catalytic subunit is expressed in escherichia coli BL21 Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.17
-
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide pH 8.0, 25°C Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant catalytic subunit Bos taurus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
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
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
20.8
-
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide pH 8.0, 25°C Bos taurus