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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Posttranslational Modification
Posttranslational Modification on EC 3.4.21.B57 - pernisine
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proteolytic modification
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the purified pernisine has a proregion that is autocleaved during maturation
proteolytic modification
the enzyme needs to be heat-activated for 1 h at 90°C in activation buffer containing 10 mM HEPES, 1 mM CaCl2, pH 8.0, through autoproteolytical cleavage of its N-terminal pro-region from the 55 kDa inactive proform to the 36 kDa active form. The cleavage site of the proregion appears to be between Gln92 and Ala93
proteolytic modification
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the purified pernisine has a proregion that is autocleaved during maturation
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proteolytic modification
pro-subtilisin is inactive in the absence of Ca2+ but is activated upon autoprocessing and degradation of propeptide in the presence of Ca2+ at 80°C. This maturation process is completed within 30 min at 80°C but is bound at an intermediate stage, in which the propeptide is autoprocessed from the mature domain (mat-subtilisin) but forms an inactive complex with mat-subtilisin*, at lower temperatures. At 80°C, approximately 30% of the pro-subtilisin is autoprocessed into propeptide and mat-subtilisin, and the other 70% is completely degraded to small fragments. mat-Subtilisin is inactive in the absence of Ca2+ but is activated upon incubation with Ca2+ at 80°C
proteolytic modification
produced from its inactive precursor, Pro-Tk-subtilisin (Gly1-Gly398), by autoprocessing and degradation of the propeptide (Tk-propeptide, Gly1-Leu69). This activation process is extremely slow at moderate temperatures owing to the high stability of Tk-propeptide. The refolding rate of Pro-F17H/S324A and autoprocessing rate of Pro-F17H/S324C are nearly identical to those of their parent proteins (Pro-S324A and Pro-S324C). The activation rate of Pro-F17H greatly increases when compared with that of Pro-Tk-subtilisin, such that Pro-F17H is efficiently activated even at 40°C
proteolytic modification
the enzyme is autoprocessed from its precursor with N- and C-propeptides
proteolytic modification
the enzyme matures from the inactive precursor, Pro-Tk-subtilisin (Pro-TKS), upon autoprocessing and degradation of the propeptide (Tkpro)
proteolytic modification
the N-propeptide is autoprocessed first in the maturation process of Pro-Tk-S359C (an enzyme derivative with the mutation of the active-site serine residue to Cys), although the C-propeptide is subsequently autoprocessed and degraded only in the absence of Ca2+. The C-propeptide is not autoprocessed in the presence of Ca2+, suggesting that Pro-Tk-SP derivative lacking N-propeptide (Val114-Gly640) (ProC-Tk-SP) is not an intermediate form but is the mature form of the enzyme. It is shown that the C-propeptide contributes to the stabilization of ProC-Tk-S359C
proteolytic modification
Tk-subtilisin (the mature domain of Pro-Tk-subtilisin in active form (Gly70-Gly398)) is matured from Pro-Tk-subtilisin (pro form (Gly1-Gly398)) upon autoprocessing and degradation of propeptide. Extremely slow maturation at mild temperatures. Maturation rate is greatly increased by a single Gly56/Ser mutation in the propeptide region
proteolytic modification
Tk-subtilisin is matured from Pro-Tk-subtilisin upon autoprocessing and degradation of Tk-propeptide. Tk-subtilisin does not require Tk-propeptide for folding but requires it for acceleration of folding
proteolytic modification
Tk-subtilisin, a subtilisin homologue (Gly70-Gly398) from Thermococcus kodakarensis, is matured from its precursor, Pro-Tk-subtilisin (Tk-subtilisin in a pro form (Gly1-Gly398)), by autoprocessing and degradation of propeptide (Tk-propeptide, a propeptide of Tk-subtilisin (Gly1-Leu69)). The scissile peptide bond between Leu69 and Gly70 of Pro-Tk-subtilisin is first self-cleaved to produce an inactive Tk-propeptide:Tk-subtilisin complex, in which the C-terminal region of Tk-propeptide binds to the active-site cleft of Tk-subtilisin. Tk-propeptide is then dissociated from Tk-subtilisin and degraded by Tk-subtilisin to release active Tk-subtilisin
proteolytic modification
autocatalytic processing, pro-Tk-subtilisin from Thermococcus kodakarensis is fully folded, because it does not require the structural rearrangement upon autoprocessing for the formation of the Ca2+-binding Ca1 site due to the presence of the insertion sequence IS1 between the propeptide and subtilisin domains
proteolytic modification
prepro-Tk-subtilisin (Prepro-TKS), which consists of the signal sequence [Met (-24)-Ala(-1)], propeptide (Gly1-Leu69), and mature domain (Tk-subtilisin, Gly70-Gly398). Tk-subtilisin matures from Pro-Tk-subtilisin upon autoprocessing and degradation of propeptide. The pro-enzyme form contains the insertion sequence, IS1, at the N-terminus of the mature domain which is required not only for hyperstabilization of Pro-Tk-subtilisin but also for its rapid maturation, Most part of IS1 (Gly70-Gly78) is autocatalytically removed when Pro-TKS matures to Tk-subtilisin, structure and mechanism, overview