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3.4.21.B57: pernisine

This is an abbreviated version!
For detailed information about pernisine, go to the full flat file.

Word Map on EC 3.4.21.B57

Reaction

the enzyme can digest the pathological prion protein isoform (PrPSc) from different species, e.g. human, bovine, deer and mouse =

Synonyms

pernisine, subtilase, Tk-SP, Tk-subtilisin, TKS

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.B57 pernisine

Cloned

Cloned on EC 3.4.21.B57 - pernisine

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli BL21(DE3)
expression in Escherichia coli of pernisine, lacking the leader sequence a fusion protein with glutathione-S-transferase
-
expression of wid-type and mutant enzymes in Escherichia coli strain BL21(DE3)
overproduced in Escherichia coli in a form with a putative prosequence in inclusion bodies, solubilized in the presence of 8 M urea, and refolded and converted to an active molecule. The enzyme is refolded in a form with a putative prosequence
overproduction in Escherichia coli of an enzyme derivative with the mutation of the active-site serine residue to Cys (Pro-Tk-S359C), its derivatives lacking the N-propeptide (ProC-Tk-S359C) and both propeptides (Tk-S359C), and a His-tagged form of the C-propeptide (ProC*)
overproduction of pro-S255A in Escherichia coli BL21-Codon-Plus(DE3)
recombinant overexpression of and His-tagged wild-type (pernisinewt), codon-optimised (pernisineco), and codon-optimised S355A active site mutant (pernisineS355Aco), with or without additional GST-tag or maltose-binding-protein-tag, in Escherichia coli strain BL21(DE3) requires codon preference optimisation and de-novo DNA synthesis. Undetectable expression level of unmodified wild-type enzyme, method evaluation
the propeptide and mature domain are independently overproduced in Escherichia coli
Tk-S359A without N- and C-propeptides is overproduced in Escherichia coli in a soluble form