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Literature summary extracted from

  • Hirata, A.; Hori, Y.; Koga, Y.; Okada, J.; Sakudo, A.; Ikuta, K.; Kanaya, S.; Takano, K.
    Enzymatic activity of a subtilisin homolog, Tk-SP, from Thermococcus kodakarensis in detergents and its ability to degrade the abnormal prion protein (2013), BMC Biotechnol., 13, 19.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.21.B57 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 Thermococcus kodakarensis

Application

EC Number Application Comment Organism
3.4.21.B57 medicine potential application for the inactivation of abnormal prion protein PrPSc, a protease-resistant isoform of normal prion protein. PrPSc is largely unaffected by standard methods of sterilization, thus, contaminated neurosurgical instruments are the major cause of human transmissible spongiform encephalopathies Thermococcus kodakarensis
3.4.21.B57 medicine the enzyme may have potential application as a detergent additive to decrease the infectivity of abnormal prion protein PrPSc Thermococcus kodakarensis
3.4.21.B57 medicine Tk-SP-containing detergents can be developed to decrease the secondary infection risks of transmissible spongiform encephalopathies Thermococcus kodakarensis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.B57 expression in Escherichia coli Thermococcus kodakarensis

General Stability

EC Number General Stability Organism
3.4.21.B57 in the presence of 0.05% (w/v) nonionic surfactants, such as EMULGEN LS-114 or RHEODOL Tw-0120 V, and 0.01% (w/v) EDTA, Tk-SP retains almost its entire initial activity Thermococcus kodakarensis
3.4.21.B57 in the presence of anionic surfactants, the enzyme is unstable, losing up to 80% of its activity Thermococcus kodakarensis
3.4.21.B57 in the presence of anionic surfactants, Tk-SP is unstable, losing up to 80% of its activity Thermococcus kodakarensis
3.4.21.B57 less stable in the presence of QUARTAMIN 60 W Thermococcus kodakarensis
3.4.21.B57 stable in the presence of 0.1% (w/v) AMPHITOL 20Y-B Thermococcus kodakarensis
3.4.21.B57 the enzyme is highly stable in the presence of 0.05% (w/v) nonionic surfactants and 0.01% (w/v) EDTA, retaining up to 80% of its activity Thermococcus kodakarensis
3.4.21.B57 the enzyme is highly stable in the presence of both 0.1 and 1% (w/v) nonionic surfactants Thermococcus kodakarensis
3.4.21.B57 the enzyme retains its activity in the presence of surfactants tested at 80°C and 90°C Thermococcus kodakarensis
3.4.21.B57 the enzyme retains more than 100% of its activity in the presence of four of the nonionic surfactants, namely, EMULGEN 147, EMULGEN LS-114, EMULGEN PP-290, and RHEODOL Tw-0120 V. It is less stable in the presence of QUARTAMIN 60 W Thermococcus kodakarensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.B57 AMPHITOL 20Y-B presence of 1% (w/v) AMPHITOL 20Y-B causes strong inhibitions, resulting in an enzyme retaining only 50% of its activity Thermococcus kodakarensis
3.4.21.B57 EDTA about 20% loss of activity in the presence of 0.01% (w/v) at 80°C, about 60% loss of activity in the presence of 1% (w/v) at 80°C; activity decreases with the increasing concentration of EDTA from 0.01 to 1% (w/v) Thermococcus kodakarensis

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.B57 Thermococcus kodakarensis P58502 sequence including singnal peptide (amino acid 1-24) and propeptide (amino acid 25-106)
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.B57 abnormal prion protein PrP(Sc) + H2O
-
Thermococcus kodakarensis ?
-
?
3.4.21.B57 abnormal prion protein PrP(Sc) + H2O prion protein PrP(Sc) is a pathological prion protein PrP isoform. The enzyme can disrupt PrPSc to a level undetectable by Western-blot analysis Thermococcus kodakarensis ?
-
?
3.4.21.B57 azocasein + H2O
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Thermococcus kodakarensis ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.4.21.B57 Tk-SP
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Thermococcus kodakarensis
3.4.21.B57 Tk-subtilisin
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Thermococcus kodakarensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.B57 80
-
assay at Thermococcus kodakarensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.B57 7.5
-
assay at Thermococcus kodakarensis