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Literature summary for 3.4.21.9 extracted from

  • Vozza, L.A.; Wittwer, L.; Higgins, D.R.; Purcell, T.J.; Bergseid, M.; Collins-Racie, L.A.; LaVallie, E.R.; Hoeffler, J.P.
    Production of a recombinant bovine enterokinase catalytic subunit in the methylotrophic yeast Pichia pastoris (1996), Biotechnology, 14, 77-81.
    View publication on PubMed

Application

Application Comment Organism
synthesis the cleavage immediately after the carboxyl-terminal residue of the (Asp)4-Lys recognition sequence allows regeneration of native amino-terminal residues of recombinant proteins, e.g. removal of the thioredoxin and polyhistidine fusion partners from proteins of intrest Bos taurus

Cloned(Commentary)

Cloned (Comment) Organism
expression of a 26300 Da protein containing the catalytic domain of bovine enterokinase, expression in methylotrophic yeast Pichia pastoris Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
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Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the highly specific protease cleaves immediately after the carboxyl-terminal residue of the (Asp)4-Lys recognition sequence Bos taurus ?
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?