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Literature summary for 3.4.22.8 extracted from

  • Kim, C.K.; Lee, S.Y.; Kwon, O.J.; Lee, S.M.; Nah, S.Y.; Jeong, S.M.
    Secretory expression of active clostripain in Escherichia coli (2007), J. Biotechnol., 131, 346-352.
    View publication on PubMed

Application

Application Comment Organism
synthesis recombinant clostripain might prove useful in the production of insulin from the proinsulin fusion protein Clostridium sp.

Cloned(Commentary)

Cloned (Comment) Organism
clostripain gene is modified and its signal sequence is replaced with that of penicillin G acylase. The core clostripain protein fused to the penicillin G acylase signal peptide is also prepared. With regard to the expression of the clostripain precursors, the majority of clostripain activity is observed in the culture media, thereby indicating that both the clostripain signal peptide and the penicillin G acylase signal peptide are recognized in the Escherichia coli secretion pathway, and the precursors successfully mature into the active form. The activity is rather low when the core protein is expressed, which indicates that the clostripain pro-peptide is important in the formation of the active enzyme in Escherichia coli Clostridium sp.

Organism

Organism UniProt Comment Textmining
Clostridium sp.
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
proinsulin fusion protein + H2O clostripain specifically cleaves the arginine residues in the leader peptide and in the C-peptide Clostridium sp. insulin + ?
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