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
-
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
-
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
-
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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Activating Compound
Activating Compound on EC 3.4.21.B57 - pernisine
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destabilization of the hydrophobic core of Tk-propeptide by a nonpolar-to-polar amino acid substitution is an effective way to increase the activation rate of Pro-Tk-subtilisin
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additional information
the activities in the presence of 1% SANISOL C and AMPHITOL 20 N are higher than those at the concentration of 0.1%. This may relate to the critical micelle concentration of the surfactants. Improvement of the enzyme activity in the presence of nonionic surfactants might be due to the stimulation of conformational changes in Tk-SP or the substrate, leading to activity gain
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additional information
-
the activities in the presence of 1% SANISOL C and AMPHITOL 20 N are higher than those at the concentration of 0.1%. This may relate to the critical micelle concentration of the surfactants. Improvement of the enzyme activity in the presence of nonionic surfactants might be due to the stimulation of conformational changes in Tk-SP or the substrate, leading to activity gain
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