Application | Comment | Organism |
---|---|---|
additional information | C-terminal pro sequence of the enzyme functions as an intramolecular chaperone that stabilizes the partially unfolded structure of the protease domain, and thereby facilitates its secretion | Thermus aquaticus |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli and Thermus thermophilus | Thermus aquaticus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
DFP | strongly inhibits | Thermus aquaticus | |
N-terminal propeptide of aqualisin I | potent inhibitor | Thermus aquaticus | |
Streptomyces subtilisin inhibitor | strongly inhibits | Thermus aquaticus | |
Z-Ala-Gly-Phe-CH2Cl | strongly inhibits | Thermus aquaticus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | stabilizes, at least two Ca2+-binding sites, i. e. stronger and weaker binding sites, weaker binding site essential for heat stability of the enzyme, Ca2+ bound to the stronger binding site is hardly removed with EDTA | Thermus aquaticus | |
La3+ | stabilizes | Thermus aquaticus | |
Nd3+ | stabilizes | Thermus aquaticus | |
Sr2+ | stabilizes | Thermus aquaticus | |
Tb3+ | stabilizes | Thermus aquaticus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
28350 | - |
calculated | Thermus aquaticus |
38000 | - |
precursor with a C-terminal pro sequence from the membrane fraction of Escherichia coli cells | Thermus aquaticus |
53910 | - |
synthesized as a large precursor, calculated | Thermus aquaticus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus aquaticus | - |
- |
- |
Thermus aquaticus YT-1 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli cells harboring an expression plasmid using the tac promoter by cation-exchange chromatography, larger scale production by using bacteriophage T7 RNA polymerase/promoter | Thermus aquaticus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
elastin-orcein + H2O | at 40°C, pH 7.5 | Thermus aquaticus | ? | - |
? | |
elastin-orcein + H2O | at 40°C, pH 7.5 | Thermus aquaticus YT-1 | ? | - |
? | |
Hammarsten casein + H2O | at 70°C, pH 7.5-10.4 | Thermus aquaticus | ? | - |
? | |
Hammarsten casein + H2O | at 70°C, pH 7.5-10.4 | Thermus aquaticus YT-1 | ? | - |
? | |
additional information | exhibits specificity toward ester of amino acids with small haydrophobic or aromatic residues in P1 | Thermus aquaticus | ? | - |
? | |
additional information | exhibits specificity toward ester of amino acids with small haydrophobic or aromatic residues in P1 | Thermus aquaticus YT-1 | ? | - |
? | |
oxidized insulin chain B + H2O | at 40°C, pH 7.5 | Thermus aquaticus | ? | - |
? | |
oxidized insulin chain B + H2O | at 40°C, pH 7.5 | Thermus aquaticus YT-1 | ? | - |
? | |
Suc-Ala-Ala-Pro-Phe-p-nitroanilide + H2O | at 40°C, pH 7.5 | Thermus aquaticus | Suc-Ala-Ala-Pro-Phe + p-nitroaniline | - |
? | |
Suc-Ala-Ala-Pro-Phe-p-nitroanilide + H2O | at 40°C, pH 7.5 | Thermus aquaticus YT-1 | Suc-Ala-Ala-Pro-Phe + p-nitroaniline | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
in the presence of 1 mM CaCl2, which stabilizes the enzyme | Thermus aquaticus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | 80 | - |
Thermus aquaticus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
10 | - |
- |
Thermus aquaticus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
7.5 | 10.4 | - |
Thermus aquaticus |