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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Temperature Stability
Temperature Stability on EC 3.4.21.B57 - pernisine
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100
110
120
40
purified recombinant activated enzyme, 50 mMTris-HCl, pH 8.0 with 1 mM CaCl2, 4 h, completely stable
58
Tm-value of Tk-S359C in absence of CaCl2. The Tm value of ProC-Tk-S359C is higher than that of Tk-S359C by 25.9°C in the absence of CaCl2 and 7.5°C in the presence of 10 mM CaCl2, indicating that the C-propeptide of ProC-Tk-S359C contributes to the stabilization of the protein by 25.9°C in Tm in the absence of Ca2+ and 7.5°C in Tm in the presence of Ca2+
58.9
Tm value of a mutant enzyme without beta-jelly roll domain (Tk-S359A/CDeltaJ), 10 mM CaCl2
70
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20 min, stable in presence of CaCls, about 60% loss of activity in absence of CaCl2
80
80.1
Tm-value of Tk-S359C in presence of 10 mM CaCl2. The Tm value of ProC-Tk-S359C is higher than that of Tk-S359C by 25.9°C in the absence of CaCl2 and 7.5°C in the presence of 10 mM CaCl2, indicating that the C-propeptide of ProC-Tk-S359C contributes to the stabilization of the protein by 25.9°C in Tm in the absence of Ca2+ and 7.5°C in Tm in the presence of Ca2+
83.9
Tm-value of ProC-Tk-S359C in absence of CaCl2. The Tm value of ProC-Tk-S359C is higher than that of Tk-S359C by 25.9°C in the absence of CaCl2 and 7.5°C in the presence of 10 mM CaCl2, indicating that the C-propeptide of ProC-Tk-S359C contributes to the stabilization of the protein by 25.9°C in Tm in the absence of Ca2+ and 7.5°C in Tm in the presence of Ca2+
87.6
Tm-value of ProC-Tk-S359C in presence of 10 mM CaCl2. The Tm value of ProC-Tk-S359C is higher than that of Tk-S359C by 25.9°C in the absence of CaCl2 and 7.5°C in the presence of 10 mM CaCl2, indicating that the C-propeptide of ProC-Tk-S359C contributes to the stabilization of the protein by 25.9°C in Tm in the absence of Ca2+ and 7.5°C in Tm in the presence of Ca2+
90
additional information
110
purified recombinant activated enzyme, 50 mMTris-HCl, pH 8.0 with 1 mM CaCl2, 4 h, loss of 30% activity
120
purified recombinant activated enzyme, 50 mMTris-HCl, pH 8.0 with 1 mM CaCl2, 4 h, loss of 50% activity
purified recombinant activated enzyme, 50 mMTris-HCl, pH 8.0 with 1 mM CaCl2, 4 h, loss of 20% activity
80
half life: more than 60 min, in the presence of 50 mM CaCl2
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20 min, stable in presence of CaCl2, about 80% loss of activity in absence of CaCl2
attachment of a beta-jelly roll domain to the C-terminus is one of the strategies of the proteins from hyperthermophiles to adapt to high-temperature environment
additional information
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attachment of a beta-jelly roll domain to the C-terminus is one of the strategies of the proteins from hyperthermophiles to adapt to high-temperature environment