Crystallization (Comment) | Organism |
---|---|
hanging drop method, crystal structure determination of the native and two mutant structures (D524N and D524A) | Aeropyrum pernix |
Protein Variants | Comment | Organism |
---|---|---|
D524A | the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme | Aeropyrum pernix |
D524N | the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme | Aeropyrum pernix |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0117 | - |
4-nitrophenyl octanoate | pH 7.0, 70°C, mutant enzyme D524N | Aeropyrum pernix | |
0.0232 | - |
4-nitrophenyl octanoate | pH 7.0, 70°C, wild-type enzyme | Aeropyrum pernix | |
0.0266 | - |
4-nitrophenyl octanoate | pH 7.0, 70°C, mutant enzyme D524A | Aeropyrum pernix |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
63030 | - |
- |
Aeropyrum pernix |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aeropyrum pernix | Q9YBQ2 | - |
- |
Aeropyrum pernix DSM 11879 | Q9YBQ2 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-nitrophenyl octanoate + H2O | - |
Aeropyrum pernix | 4-nitrophenol + octanoate | - |
? | |
4-nitrophenyl octanoate + H2O | - |
Aeropyrum pernix DSM 11879 | 4-nitrophenol + octanoate | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | the monomer subunit is composed of one hydrolase and one propeller domain. In the homodimeric structures only one subunit displayed the closed form of the enzyme. The other subunit exhibits an open gate to the catalytic site, thus revealing the structural basis that controls the oligopeptidase activity | Aeropyrum pernix |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0313 | - |
4-nitrophenyl octanoate | pH 7.0, 70°C, mutant enzyme D524A | Aeropyrum pernix | |
0.032 | - |
4-nitrophenyl octanoate | pH 7.0, 70°C, mutant enzyme D524N | Aeropyrum pernix | |
8.67 | - |
4-nitrophenyl octanoate | pH 7.0, 70°C, wild-type enzyme | Aeropyrum pernix |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
wild-type enzyme | Aeropyrum pernix |
9 | - |
the rate constants for the D524A and D524N variants increase to about pH 9 | Aeropyrum pernix |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5.8 | 8.8 | pH 5.8: about% of maximal activity, pH 8.8: about% of maximal activity | Aeropyrum pernix |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.18 | - |
4-nitrophenyl octanoate | pH 7.0, 70°C, mutant enzyme D524A | Aeropyrum pernix | |
2.74 | - |
4-nitrophenyl octanoate | pH 7.0, 70°C, mutant enzyme D524N | Aeropyrum pernix | |
374 | - |
4-nitrophenyl octanoate | pH 7.0, 70°C, wild-type enzyme | Aeropyrum pernix |