EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.4.24.27 | additional information | mechanism of salt-induced activation | Bacillus thermoproteolyticus |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.4.24.27 | gene npr, expression of wild-type and mutant enzymes in Escherichia coli K12 strain JM109 | Bacillus thermoproteolyticus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.4.24.27 | Q128A | site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme | Bacillus thermoproteolyticus |
3.4.24.27 | Q128E | site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme | Bacillus thermoproteolyticus |
3.4.24.27 | Q128K | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Bacillus thermoproteolyticus |
3.4.24.27 | Q225A | site-directed mutagenesis, the mutant shows altered pKa value and stimulation of activity by NaCl and reduced activity with the negatively charged substrate N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester substrate compared to the wild-type enzyme | Bacillus thermoproteolyticus |
3.4.24.27 | Q225D | site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme | Bacillus thermoproteolyticus |
3.4.24.27 | Q225E | site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme | Bacillus thermoproteolyticus |
3.4.24.27 | Q225K | site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme | Bacillus thermoproteolyticus |
3.4.24.27 | Q225R | site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme | Bacillus thermoproteolyticus |
3.4.24.27 | Q225V | site-directed mutagenesis, the mutant shows altered pKa value and stimulation of activity by NaCl and reduced activity with the negatively charged substrate N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester substrate compared to the wild-type enzyme | Bacillus thermoproteolyticus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.4.24.27 | 0.24 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant mutant Q225V | Bacillus thermoproteolyticus | |
3.4.24.27 | 0.28 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant mutant Q128A | Bacillus thermoproteolyticus | |
3.4.24.27 | 0.29 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant mutant Q225A | Bacillus thermoproteolyticus | |
3.4.24.27 | 0.3 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant mutants Q128K and Q225R | Bacillus thermoproteolyticus | |
3.4.24.27 | 0.33 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant mutant Q128E | Bacillus thermoproteolyticus | |
3.4.24.27 | 0.34 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant mutant Q225D | Bacillus thermoproteolyticus | |
3.4.24.27 | 0.39 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant mutant Q225K | Bacillus thermoproteolyticus | |
3.4.24.27 | 0.45 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant wild-type enzyme | Bacillus thermoproteolyticus | |
3.4.24.27 | 0.63 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant mutant Q225E | Bacillus thermoproteolyticus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.4.24.27 | K+ | activates, preference of monovalent cations in descending order: Na+, K+, Li+ | Bacillus thermoproteolyticus | |
3.4.24.27 | Li+ | activates, preference of monovalent cations in descending order: Na+, K+, Li+ | Bacillus thermoproteolyticus | |
3.4.24.27 | additional information | mechanism of salt-induced activation | Bacillus thermoproteolyticus | |
3.4.24.27 | Na+ | activates, preference of monovalent cations in descending order: Na+, K+, Li+, the bell-shaped pH dependence profile of the FAGLA-hydrolyzing activity of thermolysin is shifted from pH 5.4 to pH 6.7 by the addition of 4 M NaCl | Bacillus thermoproteolyticus | |
3.4.24.27 | Zn2+ | stereochemical relationships between Gln128, Glu143, Gln225, Asp226, His231 and active site Zn2+ of thermolysin, overview | Bacillus thermoproteolyticus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.24.27 | Bacillus thermoproteolyticus | - |
gene npr | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.4.24.27 | additional information | - |
catalytic efficiency of wild-type and mutant enzymes in absence or presence of 4 M NaCl, overview | Bacillus thermoproteolyticus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.24.27 | N-carbobenzoxy-L-Asp-L-Phe methyl ester + H2O | - |
Bacillus thermoproteolyticus | ? | - |
? | |
3.4.24.27 | N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide + H2O | i.e. FAGLA | Bacillus thermoproteolyticus | ? | - |
? |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.4.24.27 | 25 | - |
assay at | Bacillus thermoproteolyticus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.4.24.27 | 1.3 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant mutant Q225A | Bacillus thermoproteolyticus | |
3.4.24.27 | 1.6 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant mutant Q225V | Bacillus thermoproteolyticus | |
3.4.24.27 | 3.3 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant mutant Q225D | Bacillus thermoproteolyticus | |
3.4.24.27 | 3.6 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant mutant Q225R | Bacillus thermoproteolyticus | |
3.4.24.27 | 3.7 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant mutant Q128K | Bacillus thermoproteolyticus | |
3.4.24.27 | 3.8 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant mutant Q128A | Bacillus thermoproteolyticus | |
3.4.24.27 | 4.3 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant mutants Q128E and Q225E | Bacillus thermoproteolyticus | |
3.4.24.27 | 4.7 | - |
N-carbobenzoxy-L-Asp-L-Phe methyl ester | pH 7.5, 25°C, recombinant wild-type enzyme and mutant Q225K | Bacillus thermoproteolyticus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.4.24.27 | 7 | - |
- |
Bacillus thermoproteolyticus |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.4.24.27 | additional information | - |
bell-shaped pH-dependence with importance of surfacecharges of thermolysin, the bell-shaped pH dependence profile of the FAGLA-hydrolyzing activity of thermolysin is shifted from pH 5.4 to pH 6.7 by the addition of 4 M NaCl | Bacillus thermoproteolyticus |