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Literature summary extracted from

  • Kusano, M.; Yasukawa, K.; Inouye, K.
    Effects of the mutational combinations on the activity and stability of thermolysin (2010), J. Biotechnol., 147, 7-16.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.27 expressed in Escherichia coli strain K12 JM109 Bacillus thermoproteolyticus

Protein Variants

EC Number Protein Variants Comment Organism
3.4.24.27 D150E the mutation increases the activity of thermolysin Bacillus thermoproteolyticus
3.4.24.27 G8C/N60C/S65P the mutation increases the stability of thermolysin Bacillus thermoproteolyticus
3.4.24.27 G8C/N60C/S65P the triple mutation increases the stability of thermolysin as high as the individual mutations do Bacillus thermoproteolyticus
3.4.24.27 G8C/N60C/S65P/L144S the mutant is more active and stable than wild type thermolysin Bacillus thermoproteolyticus
3.4.24.27 I168A the mutation increases the activity of thermolysin and shows about 90% casein-hydrolytic activity compared to the wild type enzyme Bacillus thermoproteolyticus
3.4.24.27 L144S the mutation increases the activity of thermolysin and shows about 30% casein-hydrolytic activity compared to the wild type enzyme Bacillus thermoproteolyticus
3.4.24.27 L144S/D150E the mutation yields the most significant increase in the hydrolytic activities for N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide and N-carbobenzoxy-L-Asp-L-Phe methyl ester and shows about 30% casein-hydrolytic activity compared to the wild type enzyme Bacillus thermoproteolyticus
3.4.24.27 L144S/D150E/I168A/S53D/L155A/G8C/N60C/S65P inactive Bacillus thermoproteolyticus
3.4.24.27 L144S/D150E/L155A inactive Bacillus thermoproteolyticus
3.4.24.27 L144S/D150E/S53D the triple mutant shows improved activity and stability with about 30% casein-hydrolytic activity compared to the wild type enzyme Bacillus thermoproteolyticus
3.4.24.27 L144S/D150E/S53D/L155A inactive Bacillus thermoproteolyticus
3.4.24.27 L144S/I168A the mutation abolishes the hydrolytic activities for N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide and N-carbobenzoxy-L-Asp-L-Phe methyl ester Bacillus thermoproteolyticus
3.4.24.27 L155A the mutation increases the stability of thermolysin and shows about 60% casein-hydrolytic activity compared to the wild type enzyme Bacillus thermoproteolyticus
3.4.24.27 L155A/G8C/N60C/S65P the mutant shows about 80% casein-hydrolytic activity compared to the wild type enzyme Bacillus thermoproteolyticus
3.4.24.27 S53D the mutation increases the stability of thermolysin Bacillus thermoproteolyticus
3.4.24.27 S53D/G8C/N60C/S65P the mutant shows about 110% casein-hydrolytic activity compared to the wild type enzyme Bacillus thermoproteolyticus
3.4.24.27 S53D/L155A the mutation yields the greatest increase in the thermal stability and shows about 90% casein-hydrolytic activity compared to the wild type enzyme Bacillus thermoproteolyticus
3.4.24.27 S53D/L155A/G8C/N60C/S65P the mutant shows about 70% casein-hydrolytic activity compared to the wild type enzyme Bacillus thermoproteolyticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.24.27 0.16
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme L144S/D150E/S53D, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.17
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme L144S/D150E, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.18
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme D150E/I168A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.19
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme L144S, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.46
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme I168A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.5
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme D150E, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.54
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.55
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme S53D/L155A/G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.63
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester wild type enzyme, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.69
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme S53D/L155A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.77
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme S53D, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.83
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme L155A/G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.94
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme S53D/G8C/N60C/S65P, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 1.29
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme L155A, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.27 Na+ 4 M Na+ stimulates the hydrolytic activity of wild type thermolysin about 13fold Bacillus thermoproteolyticus

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.27 Bacillus thermoproteolyticus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.27
-
 Bacillus thermoproteolyticus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.24.27 3.5
-
 purified mutant enzyme L144S/D150E, using casein as substrate, at pH 7.5 and 25°C Bacillus thermoproteolyticus
3.4.24.27 3.6
-
 purified mutant enzyme L144S, using casein as substrate, at pH 7.5 and 25°C Bacillus thermoproteolyticus
3.4.24.27 6.7
-
 purified mutant enzyme L155A, using casein as substrate, at pH 7.5 and 25°C Bacillus thermoproteolyticus
3.4.24.27 7.5
-
 purified mutant enzyme D150E/I168A, using casein as substrate, at pH 7.5 and 25°C Bacillus thermoproteolyticus
3.4.24.27 7.9
-
 purified mutant enzyme S53D/L155A/G8C/N60C/S65P, using casein as substrate, at pH 7.5 and 25°C Bacillus thermoproteolyticus
3.4.24.27 8.1
-
 purified mutant enzyme L155A/G8C/N60C/S65P, using casein as substrate, at pH 7.5 and 25°C Bacillus thermoproteolyticus
3.4.24.27 9.6
-
 purified mutant enzyme I168A, using casein as substrate, at pH 7.5 and 25°C Bacillus thermoproteolyticus
3.4.24.27 10.2
-
 purified mutant enzyme S53D/L155A, using casein as substrate, at pH 7.5 and 25°C Bacillus thermoproteolyticus
3.4.24.27 10.5
-
 purified mutant enzyme D150E, using casein as substrate, at pH 7.5 and 25°C Bacillus thermoproteolyticus
3.4.24.27 10.8
-
 purified mutant enzyme G8C/N60C/S65P, using casein as substrate, at pH 7.5 and 25°C Bacillus thermoproteolyticus
3.4.24.27 10.8
-
 purified wild type enzyme, using casein as substrate, at pH 7.5 and 25°C Bacillus thermoproteolyticus
3.4.24.27 11.3
-
 purified mutant enzyme S53D, using casein as substrate, at pH 7.5 and 25°C Bacillus thermoproteolyticus
3.4.24.27 11.9
-
 purified mutant enzyme S53D/G8C/N60C/S65P, using casein as substrate, at pH 7.5 and 25°C Bacillus thermoproteolyticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.27 casein + H2O
-
 Bacillus thermoproteolyticus ?
-
 ?
3.4.24.27 N-carbobenzoxy-L-Asp-L-Phe methyl ester + H2O
-
 Bacillus thermoproteolyticus ?
-
 ?
3.4.24.27 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide + H2O
-
 Bacillus thermoproteolyticus ?
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.24.27 80
-
 the rate constant (kobs) for thermal inactivation at 80°C is 84000 s-1 for the wild type enzyme Bacillus thermoproteolyticus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.24.27 3.3
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme S53D/L155A/G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 5.4
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 5.9
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester wild type enzyme, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 6.3
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme L155A/G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 6.4
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme S53D/L155A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 6.9
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme S53D, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 7.4
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme S53D/G8C/N60C/S65P, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 7.7
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme I168A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 8.7
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme L155A, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 9.4
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme L144S, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 15.5
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme D150E/I168A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 15.6
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme L144S/D150E/S53D, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 16.5
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme D150E, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 17
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme L144S/D150E, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.4.24.27 0.23
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme S53D/L155A/G8C/N60C/S65P, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.26
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme L155A, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.29
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme G8C/N60C/S65P, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.29
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide wild type enzyme, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.31
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme S53D/G8C/N60C/S65P, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.32
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme S53D, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.33
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme S53D/L155A, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.34
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme L155A/G8C/N60C/S65P, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.62
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme I168A, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 0.79
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme D150E, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 1.82
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme L144S, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 2.04
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme L144S/D150E, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 2.1
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme L155A, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 2.49
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme L144S/D150E/S53D, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 3
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme I168A, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 3.2
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme S53D/L155A, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 3.3
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme S53D/L155A/G8C/N60C/S65P, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 3.5
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme G8C/N60C/S65P, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 3.8
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide wild type enzyme, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 3.9
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme S53D, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 4
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme D150E, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 4
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme S53D/G8C/N60C/S65P, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 4.3
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme L155A/G8C/N60C/S65P, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 6
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme L144S/D150E, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 6
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme S53D/L155A/G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 6.6
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme L144S, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 6.7
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme L155A, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 7.5
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme L155A/G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 7.9
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme S53D/G8C/N60C/S65P, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 9
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme S53D, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 9.2
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme S53D/L155A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 9.4
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester wild type enzyme, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 10
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 11.7
-
 N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide mutant enzyme L144S/D150E/S53D, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 16.8
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme I168A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 33.1
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme D150E, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 49.7
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme L144S, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 96.2
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme L144S/D150E/S53D, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus
3.4.24.27 99
-
 N-carbobenzoxy-L-Asp-L-Phe methyl ester mutant enzyme L144S/D150E, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C Bacillus thermoproteolyticus