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
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3.4.21.B57
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hyperthermophilic
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archaeon
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subtilisin-like
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pernix
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aeropyrum
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subtilisins
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thermococcus
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prion
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medicine
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kodakaraensis
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proregion
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mesophilic
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autoprocessed
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detergents
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edta
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codon-optimised
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far-uv
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tk-subtilisin
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high-temperature
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cacl2
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n-propeptide
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roll
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hyperthermostable
- 3.4.21.B57
-
hyperthermophilic
- archaeon
-
subtilisin-like
- pernix
-
aeropyrum
- subtilisins
-
thermococcus
- prion
- medicine
- kodakaraensis
-
proregion
-
mesophilic
-
autoprocessed
- detergents
- edta
-
codon-optimised
-
far-uv
- tk-subtilisin
-
high-temperature
- cacl2
- n-propeptide
-
roll
-
hyperthermostable
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
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Cloned
Cloned on EC 3.4.21.B57 - pernisine
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expression in Escherichia coli
expression in Escherichia coli of pernisine, lacking the leader sequence a fusion protein with glutathione-S-transferase
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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