Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli strain K12 JM109 | Bacillus thermoproteolyticus |
Protein Variants | Comment | Organism |
---|---|---|
D150E | the mutation increases the activity of thermolysin | Bacillus thermoproteolyticus |
G8C/N60C/S65P | the mutation increases the stability of thermolysin | Bacillus thermoproteolyticus |
G8C/N60C/S65P | the triple mutation increases the stability of thermolysin as high as the individual mutations do | Bacillus thermoproteolyticus |
G8C/N60C/S65P/L144S | the mutant is more active and stable than wild type thermolysin | Bacillus thermoproteolyticus |
I168A | the mutation increases the activity of thermolysin and shows about 90% casein-hydrolytic activity compared to the wild type enzyme | Bacillus thermoproteolyticus |
L144S | the mutation increases the activity of thermolysin and shows about 30% casein-hydrolytic activity compared to the wild type enzyme | Bacillus thermoproteolyticus |
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 |
L144S/D150E/I168A/S53D/L155A/G8C/N60C/S65P | inactive | Bacillus thermoproteolyticus |
L144S/D150E/L155A | inactive | Bacillus thermoproteolyticus |
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 |
L144S/D150E/S53D/L155A | inactive | Bacillus thermoproteolyticus |
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 |
L155A | the mutation increases the stability of thermolysin and shows about 60% casein-hydrolytic activity compared to the wild type enzyme | Bacillus thermoproteolyticus |
L155A/G8C/N60C/S65P | the mutant shows about 80% casein-hydrolytic activity compared to the wild type enzyme | Bacillus thermoproteolyticus |
S53D | the mutation increases the stability of thermolysin | Bacillus thermoproteolyticus |
S53D/G8C/N60C/S65P | the mutant shows about 110% casein-hydrolytic activity compared to the wild type enzyme | Bacillus thermoproteolyticus |
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 |
S53D/L155A/G8C/N60C/S65P | the mutant shows about 70% casein-hydrolytic activity compared to the wild type enzyme | Bacillus thermoproteolyticus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | Comment | Organism | Structure |
---|---|---|---|
Na+ | 4 M Na+ stimulates the hydrolytic activity of wild type thermolysin about 13fold | Bacillus thermoproteolyticus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus thermoproteolyticus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Bacillus thermoproteolyticus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
3.5 | - |
purified mutant enzyme L144S/D150E, using casein as substrate, at pH 7.5 and 25°C | Bacillus thermoproteolyticus |
3.6 | - |
purified mutant enzyme L144S, using casein as substrate, at pH 7.5 and 25°C | Bacillus thermoproteolyticus |
6.7 | - |
purified mutant enzyme L155A, using casein as substrate, at pH 7.5 and 25°C | Bacillus thermoproteolyticus |
7.5 | - |
purified mutant enzyme D150E/I168A, using casein as substrate, at pH 7.5 and 25°C | Bacillus thermoproteolyticus |
7.9 | - |
purified mutant enzyme S53D/L155A/G8C/N60C/S65P, using casein as substrate, at pH 7.5 and 25°C | Bacillus thermoproteolyticus |
8.1 | - |
purified mutant enzyme L155A/G8C/N60C/S65P, using casein as substrate, at pH 7.5 and 25°C | Bacillus thermoproteolyticus |
9.6 | - |
purified mutant enzyme I168A, using casein as substrate, at pH 7.5 and 25°C | Bacillus thermoproteolyticus |
10.2 | - |
purified mutant enzyme S53D/L155A, using casein as substrate, at pH 7.5 and 25°C | Bacillus thermoproteolyticus |
10.5 | - |
purified mutant enzyme D150E, using casein as substrate, at pH 7.5 and 25°C | Bacillus thermoproteolyticus |
10.8 | - |
purified mutant enzyme G8C/N60C/S65P, using casein as substrate, at pH 7.5 and 25°C | Bacillus thermoproteolyticus |
10.8 | - |
purified wild type enzyme, using casein as substrate, at pH 7.5 and 25°C | Bacillus thermoproteolyticus |
11.3 | - |
purified mutant enzyme S53D, using casein as substrate, at pH 7.5 and 25°C | Bacillus thermoproteolyticus |
11.9 | - |
purified mutant enzyme S53D/G8C/N60C/S65P, using casein as substrate, at pH 7.5 and 25°C | Bacillus thermoproteolyticus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
casein + H2O | - |
Bacillus thermoproteolyticus | ? | - |
? | |
N-carbobenzoxy-L-Asp-L-Phe methyl ester + H2O | - |
Bacillus thermoproteolyticus | ? | - |
? | |
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide + H2O | - |
Bacillus thermoproteolyticus | ? | - |
? |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
the rate constant (kobs) for thermal inactivation at 80°C is 84000 s-1 for the wild type enzyme | Bacillus thermoproteolyticus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | - |
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 | |
3.2 | - |
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 | |
3.3 | - |
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 | |
3.5 | - |
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 | |
3.8 | - |
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 | |
3.9 | - |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 |