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abnormal prion protein PrP(Sc) + H2O
?
Bovine serum albumin + H2O
?
N-succinyl-AAPF-4-nitroanilide + H2O
N-succinyl-AAPF + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Leu-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Leu + 4-nitroaniline
24.3% compared to the activity with N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
pro-Tk-subtilisin + H2O
Tk-subtilisin + propeptide
autoactivation
-
-
?
proform pernisine + H2O
mature pernisine + signal sequence-N-terminal pro-region
the enzyme performs autoproteolytical cleavage of its N-terminal pro-region for activation
-
-
?
succinyl-Ala-Ala-Pro-Leu-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Leu + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
Tk-RNase H2 + H2O
?
ribonuclease H2 from Thermococcus kodakarensis, pulse proteolysis using the superstable subtilisin-like serine protease Tk-subtilisin in highly concentrated guanidine hydrochloride to unfold the highly stable substrate protein. The native state of Tk-RNase H2 is completely resistant to Tk-subtilisin, whereas the unfolded state (induced by 4 M GdnHCl) is degraded by Tk-subtilisin, identification of the cleavage sites. Structure analysis of unfolded substrate states
-
-
?
additional information
?
-
abnormal prion protein PrP(Sc) + H2O
?
-
the prion protein PrP(Sc) is a pathological prion protein PrP isoform. The proteolytic activity of pernisine does not depend on the species of origin of the PrP used (bovine, mouse, human)
-
-
?
abnormal prion protein PrP(Sc) + H2O
?
-
the prion protein PrP(Sc) is a pathological prion protein PrP isoform. The proteolytic activity of pernisine does not depend on the species of origin of the PrP used (bovine, mouse, human)
-
-
?
abnormal prion protein PrP(Sc) + H2O
?
-
-
-
?
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
-
-
?
abnormal prion protein PrP(Sc) + H2O
?
the abnormal prion protein (scrapie-associated prion protein, PrP(Sc)) is considered to be included in the group of infectious agents of transmissible spongiform encephalopathies. Although PrP(Sc) is known to be resistant toward proteolytic enzymes, Tk-subtilisin is able to degrade PrP(Sc) under extreme conditions
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
?
Bovine serum albumin + H2O
?
-
among the proteins tested, casein shows the highest degree of susceptibility with 100% of hydrolysis, while in the case of hemoglobin, ovalbumin, and bovine serum albumin it was about 50%
-
-
?
Bovine serum albumin + H2O
?
-
among the proteins tested, casein shows the highest degree of susceptibility with 100% of hydrolysis, while in the case of hemoglobin, ovalbumin, and bovine serum albumin it was about 50%
-
-
?
casein + H2O
?
-
-
-
?
casein + H2O
?
-
among the proteins tested, casein shows the highest degree of susceptibility with 100% of hydrolysis, while in the case of hemoglobin, ovalbumin, and bovine serum albumin it was about 50%
-
-
?
casein + H2O
?
-
among the proteins tested, casein shows the highest degree of susceptibility with 100% of hydrolysis, while in the case of hemoglobin, ovalbumin, and bovine serum albumin it was about 50%
-
-
?
Hemoglobin + H2O
?
-
among the proteins tested, casein shows the highest degree of susceptibility with 100% of hydrolysis, while in the case of hemoglobin, ovalbumin, and bovine serum albumin it was about 50%
-
-
?
Hemoglobin + H2O
?
-
among the proteins tested, casein shows the highest degree of susceptibility with 100% of hydrolysis, while in the case of hemoglobin, ovalbumin, and bovine serum albumin it was about 50%
-
-
?
ovalbumin + H2O
?
-
among the proteins tested, casein shows the highest degree of susceptibility with 100% of hydrolysis, while in the case of hemoglobin, ovalbumin, and bovine serum albumin it was about 50%
-
-
?
ovalbumin + H2O
?
-
among the proteins tested, casein shows the highest degree of susceptibility with 100% of hydrolysis, while in the case of hemoglobin, ovalbumin, and bovine serum albumin it was about 50%
-
-
?
additional information
?
-
-
pernisine has no activity on N-alpha-benzoyl-D-Arg-4-nitroanilide, N-alpha-benzoyl-D-Tyr-4-nitroanilide, and N-succinyl-Ala-Ala-Ala-4-nitroanilide used to detect trypsin, chymotrypsin, and elastase activity, respectively. Aminopeptidase activity is not detected
-
-
?
additional information
?
-
enzymatic degradation of protein aggregates by pernisine, such as for infective prions (PrPSc) from different origins (i.e., mouse, bovine, deer, human)
-
-
?
additional information
?
-
-
pernisine has no activity on N-alpha-benzoyl-D-Arg-4-nitroanilide, N-alpha-benzoyl-D-Tyr-4-nitroanilide, and N-succinyl-Ala-Ala-Ala-4-nitroanilide used to detect trypsin, chymotrypsin, and elastase activity, respectively. Aminopeptidase activity is not detected
-
-
?
additional information
?
-
broad substrate specificity, with a slight preference for aromatic or large nonpolar P1 substrate residues
-
-
?
additional information
?
-
the propeptide is effectively degraded by the mature enzyme only at high temperatures, because it is too stable to be degraded at moderate temperatures
-
-
?
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proteolytic modification
-
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
-
the purified pernisine has a proregion that is autocleaved during maturation
-
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
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S355A
site-directed mutagenesis, catalytically inactive active site mutant
Pro-Tk-S359C
construction of an enzyme derivative with the mutation of the active-site serine residue to Cys (Pro-Tk-S359C). Pro-Tk-S359C is purified mostly in an autoprocessed form in which the N-propeptide is autoprocessed but the isolated N-propeptide (ProN) forms a stable complex with ProC-Tk-S359C, indicating that the N-propeptide is autoprocessed first
ProC-Tk-S359C
construction of an enzyme derivative lacking the N-propeptide (ProC-Tk-S359C). The C-propeptide is autoprocessed and degraded when ProC-Tk-S359C is incubated at 80 °C in the absence of Ca2+. However, it is not autoprocessed in the presence of Ca2+. The enzymatic activity of ProC-Tk-S359C is higher than (but comparable to) that of Tk-S359C, an enzyme derivatives lacking both propeptides, suggesting that the C-propeptide is not important for activity. The Tm value of ProC-Tk-S359C is higher than that of Tk-S359C by 25.9°C in the absence of Ca2+ and 7.5 °C in the presence of Ca2+, indicating that the C-propeptide contributes to the stabilization of ProC-Tk-S359C
S255A
active-site mutant enzyme
S324C
site-directed mutagenesis, structure comparison of the mutant pro-enzyme with the wild-type pro-enzyme
S359C
S359C is more stable than S359A. Tm value of is 58.0°C in the presence of 2.5 M GdnHCl and the absence of Ca2+ and 80.1°C in the presence of 6 m GdnHCl and 10 mm CaCl2
Tk-S359C
construction of an enzyme derivative lacking both propeptides (Tk-S359C). The enzymatic activity of ProC-Tk-S359C, an enzyme derivatives lacking the N-propeptide is higher than (but comparable to) that of Tk-S359C, suggesting that the C-propeptide is not important for activity. The Tm value of ProC-Tk-S359C is higher than that of Tk-S359C by 25.9°C in the absence of Ca2+ and 7.5 °C in the presence of Ca2+, indicating that the C-propeptide contributes to the stabilization of ProC-Tk-S359C
S324A
the crystal structure of the active site mutant of Tk-subtilisin (S324A-subtilisin), which is refolded in the presence of Ca2+ and absence of Tk-propeptide, is determined at 2.16 A resolution. This structure is the same as that of Tk-subtilisin matured from Pro-Tk-subtilisin. The counting of amino acids refers to the enzyme protein without the signal peptide (amino acid 1-24) and the propeptide (amino acid 25-106)
S324A
site-directed mutagenesis, structure comparison of the mutant pro-enzyme with the wild-type pro-enzyme
additional information
construction of a series of active-site mutants of with (Tk-S359A/C) and without (Tk-S359A/CDeltaJ) beta-jelly roll domain. Both Tk-S359C and Tk-S359CDeltaJ exhibit protease activities, indicating that the beta-jelly roll domain is not required for folding or activity. The Tm value of Tk-S359ADeltaJ determined by far-UV CD spectroscopy in the presence of 10-mM CaCl2 is lower than that of Tk-S359A by 29.4°C. The Tm value of Tk-S359A is decreased by 29.5 °C by the treatment with 10 mM ethylenediaminetetraacetic acid, indicating that the beta-jelly roll domain contributes to the stabilization of Tk-S359A only in a Ca2+-bound form
additional information
-
construction of a series of active-site mutants of with (Tk-S359A/C) and without (Tk-S359A/CDeltaJ) beta-jelly roll domain. Both Tk-S359C and Tk-S359CDeltaJ exhibit protease activities, indicating that the beta-jelly roll domain is not required for folding or activity. The Tm value of Tk-S359ADeltaJ determined by far-UV CD spectroscopy in the presence of 10-mM CaCl2 is lower than that of Tk-S359A by 29.4°C. The Tm value of Tk-S359A is decreased by 29.5 °C by the treatment with 10 mM ethylenediaminetetraacetic acid, indicating that the beta-jelly roll domain contributes to the stabilization of Tk-S359A only in a Ca2+-bound form
additional information
construction of enzyme derivatives with the mutation of the active-site serine residue to Cys (Pro-Tk-S359C), Pro-Tk-S359C derivative lacking the N-propeptide (ProC-Tk-S359C) and both propeptides (Tk-S359C), and a His-tagged form of the isolated C-propeptide (ProC*). Comparison of the susceptibility of ProC* to proteolytic degradation in the presence and absence of Ca2+ suggests that the C-propeptide becomes highly resistant to proteolytic degradation in the presence of Ca2+
additional information
-
construction of enzyme derivatives with the mutation of the active-site serine residue to Cys (Pro-Tk-S359C), Pro-Tk-S359C derivative lacking the N-propeptide (ProC-Tk-S359C) and both propeptides (Tk-S359C), and a His-tagged form of the isolated C-propeptide (ProC*). Comparison of the susceptibility of ProC* to proteolytic degradation in the presence and absence of Ca2+ suggests that the C-propeptide becomes highly resistant to proteolytic degradation in the presence of Ca2+
additional information
Pro-Tk-subtilisin variants with complete amino acid substitutions at Gly56 are constructed. Pro-G56W, Pro-G56E and Pro-G56S are overproduced, purified, and characterized. Their maturation rates increase in the order wild-type enzyme or = G56W-propeptide > G56S-propeptide > G56E-propeptide, indicating that they are inversely correlated with the maturation rates of Pro7-Tk-subtilisin and its derivatives
additional information
the Leu69Pro mutation in the propeptide accelerates the maturation of Pro-Tk-subtilisin by reducing the binding ability of Tk-propeptide to Tk-subtilisin
additional information
the Pro-Tk-subtilisin derivative with the F17His mutation (Pro-F17H), Tk-propeptide derivative with the same mutation (F17H-propeptide), and two active-site mutants of Pro-F17H (Pro-F17H/S324A and Pro-F17H/S324C) are constructed
additional information
to analyze the role of the Ca2+-binding loop, three mutant proteins, Deltaloop-Tk-subtilisin (Ca2+-binding loop is removed), DeltaCa2-Pro-S324A (Ca2+-binding site Ca2 is removed), and DeltaCa3-Pro-S324A (Ca2+-binding site Ca3 is removed), are constructed. The structures of DeltaCa2-Pro-S324A (Ca2+-binding site Ca 2 is removed) and DeltaCa3-Pro-S324A (Ca2+-binding site Ca3 is removed) are identical to that of Pro-S324A, except that they lack the Ca2 and Ca3 sites, respectively, and the structure of the Ca2+-binding loop is destabilized. These proteins are slightly more stable than Pro-S324A
additional information
generation of IS1-deletion mutants of S324A and S324C enzyme variants
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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
-
20 min, stable in presence of CaCls, about 60% loss of activity in absence of CaCl2
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+
88.3
Tm value of mutant enzyme S359A, 10 mM CaCl2
100
-
half life: 60 min, in absence of Ca2+
100
half life: 7 min, in the presence of 50 mM CaCl2
100
the enzyme loses half of its activity in 50 min
110
-
half life: 40 min, in absence of Ca2+
110
purified recombinant activated enzyme, 50 mMTris-HCl, pH 8.0 with 1 mM CaCl2, 4 h, loss of 30% activity
120
-
half life: 30 min, in absence of Ca2+
120
purified recombinant activated enzyme, 50 mMTris-HCl, pH 8.0 with 1 mM CaCl2, 4 h, loss of 50% activity
80
purified recombinant activated enzyme, 50 mMTris-HCl, pH 8.0 with 1 mM CaCl2, 4 h, loss of 20% activity
80
stable for at least 3 h
80
half life: more than 60 min, in the presence of 50 mM CaCl2
90
-
20 min, stable in presence of CaCl2, about 80% loss of activity in absence of CaCl2
90
-
4 h, no loss of activity, in absence of Ca2+
90
half life: 20 min, in the presence of 50 mM CaCl2
90
the enzyme loses half of its activity in 9 h
additional information
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
-
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
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Tanaka, S.; Saito, K.; Chon, H.; Matsumura, H.; Koga, Y.; Takano, K.; Kanaya, S.
Crystallization and preliminary X-ray diffraction study of an active-site mutant of pro-Tk-subtilisin from a hyperthermophilic archaeon
Acta Crystallogr. Sect. F
62
902-905
2006
Thermococcus kodakarensis (P58502)
brenda
Pulido, M.A.; Tanaka, S.; Sringiew, C.; You, D.J.; Matsumura, H.; Koga, Y.; Takano, K.; Kanaya, S.
Requirement of left-handed glycine residue for high stability of the Tk-subtilisin propeptide as revealed by mutational and crystallographic analyses
J. Mol. Biol.
374
1359-1373
2007
Thermococcus kodakarensis (P58502)
brenda
Takeuchi, Y.; Tanaka, S.; Matsumura, H.; Koga, Y.; Takano, K.; Kanaya, S.
Requirement of a unique Ca(2+)-binding loop for folding of Tk-subtilisin from a hyperthermophilic archaeon
Biochemistry
48
10637-10643
2009
Thermococcus kodakarensis (P58502)
brenda
Kannan, Y.; Koga, Y.; Inoue, Y.; Haruki, M.; Takagi, M.; Imanaka, T.; Morikawa, M.; Kanaya, S.
Active subtilisin-like protease from a hyperthermophilic archaeon in a form with a putative prosequence
Appl. Environ. Microbiol.
67
2445-2452
2001
Thermococcus kodakarensis (P58502)
brenda
Pulido, M.; Saito, K.; Tanaka, S.; Koga, Y.; Morikawa, M.; Takano, K.; Kanaya, S.
Ca2+-dependent maturation of subtilisin from a hyperthermophilic archaeon, Thermococcus kodakaraensis: the propeptide is a potent inhibitor of the mature domain but is not required for its folding
Appl. Environ. Microbiol.
72
4154-4162
2006
Thermococcus kodakarensis (P58502)
brenda
Koga, Y.; Tanaka, S.; Sakudo, A.; Tobiume, M.; Aranishi, M.; Hirata, A.; Takano, K.; Ikuta, K.; Kanaya, S.
Proteolysis of abnormal prion protein with a thermostable protease from Thermococcus kodakarensis KOD1
Appl. Microbiol. Biotechnol.
98
2113-2120
2013
Thermococcus kodakarensis (P58502)
brenda
Uehara, R.; Takeuchi, Y.; Tanaka, S.; Takano, K.; Koga, Y.; Kanaya, S.
Requirement of Ca(2+) ions for the hyperthermostability of Tk-subtilisin from Thermococcus kodakarensis
Biochemistry
51
5369-5378
2012
Thermococcus kodakarensis (P58502)
brenda
Tanaka, S.; Koga, Y.; Takano, K.; Kanaya, S.
Inhibition of chymotrypsin- and subtilisin-like serine proteases with Tk-serpin from hyperthermophilic archaeon Thermococcus kodakaraensis
Biochim. Biophys. Acta
1814
299-307
2010
Thermococcus kodakarensis (P58502)
brenda
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
BMC Biotechnol.
13
19
2013
Thermococcus kodakarensis (P58502), Thermococcus kodakarensis
brenda
Catara, G.; Ruggiero, G.; La Cara, F.; Digilio, F.A.; Capasso, A.; Rossi, M.
A novel extracellular subtilisin-like protease from the hyperthermophile Aeropyrum pernix K1: biochemical properties, cloning, and expression
Extremophiles
7
391-399
2003
Aeropyrum pernix, Aeropyrum pernix DSM 11879
brenda
Sinsereekul, N.; Foophow, T.; Yamanouchi, M.; Koga, Y.; Takano, K.; Kanaya, S.
An alternative mature form of subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis identified in the presence of Ca2+
FEBS J.
278
1901-1911
2011
Thermococcus kodakarensis (P58502), Thermococcus kodakarensis
brenda
Uehara, R.; Ueda, Y.; You, D.J.; Koga, Y.; Kanaya, S.
Accelerated maturation of Tk-subtilisin by a Leu->Pro mutation at the C-terminus of the propeptide, which reduces the binding of the propeptide to Tk-subtilisin
FEBS J.
280
994-1006
2013
Thermococcus kodakarensis (P58502)
brenda
Tanaka, S.; Takeuchi, Y.; Matsumura, H.; Koga, Y.; Takano, K.; Kanaya, S.
Crystal structure of Tk-subtilisin folded without propeptide: requirement of propeptide for acceleration of folding
FEBS Lett.
582
3875-3878
2008
Thermococcus kodakarensis (P58502)
brenda
Foophow, T.; Tanaka, S.; Angkawidjaja, C.; Koga, Y.; Takano, K.; Kanaya, S.
Crystal structure of a subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis: requirement of a C-terminal beta-jelly roll domain for hyperstability
J. Mol. Biol.
400
865-877
2010
Thermococcus kodakarensis (P58502), Thermococcus kodakarensis
brenda
Snajder, M.; Vilfan, T.; Cernilec, M.; Rupreht, R.; Popovic, M.; Juntes, P.; Serbec, V.C., Ulrih, N.P.
Enzymatic degradation of PrPSc by a protease secreted from Aeropyrum pernix K1
PLoS One
7
e39548
2012
Aeropyrum pernix, Aeropyrum pernix DSM 11879
brenda
Yuzaki, K.; Sanda, Y.; You, D.J.; Uehara, R.; Koga, Y.; Kanaya, S.
Increase in activation rate of Pro-Tk-subtilisin by a single nonpolar-to-polar amino acid substitution at the hydrophobic core of the propeptide domain
Protein Sci.
22
1711-1721
2013
Thermococcus kodakarensis (P58502)
brenda
Okada, J.; Koga, Y.; Takano, K.; Kanaya, S.
Slow unfolding pathway of hyperthermophilic Tk-RNase H2 examined by pulse proteolysis using the stable protease Tk-subtilisin
Biochemistry
51
9178-9191
2012
Thermococcus kodakarensis (P58502)
brenda
Uehara, R.; Angkawidjaja, C.; Koga, Y.; Kanaya, S.
Formation of the high-affinity calcium binding site in pro-subtilisin E with the insertion sequence IS1 of pro-Tk-subtilisin
Biochemistry
52
9080-9088
2013
Thermococcus kodakarensis (P58502)
brenda
Uehara, R.; Tanaka, S.; Takano, K.; Koga, Y.; Kanaya, S.
Requirement of insertion sequence IS1 for thermal adaptation of Pro-Tk-subtilisin from hyperthermophilic archaeon
Extremophiles
16
841-851
2012
Thermococcus kodakarensis (P58502)
brenda
Snajder, M.; Mihelic, M.; Turk, D.; Ulrih, N.P.
Codon optimisation is key for pernisine expression in Escherichia coli
PLoS ONE
10
e0123288
2015
Aeropyrum pernix (Q9YFI3)
brenda