Cloned (Comment) | Organism |
---|---|
- |
Aeropyrum pernix K1 |
Crystallization (Comment) | Organism |
---|---|
crystals of the H367A mutant grown at 20°C in hanging drops, to 2.2 A resolution. Belongs to space group P212121 | Aeropyrum pernix |
the crystal structure of the H367A variant of ApAAP is determined and refined to a resolution of 2.2 A | Aeropyrum pernix K1 |
Protein Variants | Comment | Organism |
---|---|---|
H367A | displays significantly reduced catalytic activity. Unlike the reaction of the wild-type, the reaction of the mutant displays completely linear temperature dependence. Its reaction is associated with unfavourable entropy of activation | Aeropyrum pernix |
H367A | mutant, displays significantly reduced catalytic activity | Aeropyrum pernix K1 |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ac-Phe-OH | product-like inhibitor | Aeropyrum pernix K1 | |
Acetyl-Phe | forms hydrogen bonds with both NH groups of the oxyanion binding site of AAP. In the mutant enzyme the NH bond of Gly369 points in a different direction | Aeropyrum pernix |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0082 | - |
N-acetyl-Phe-2-naphthylamide | wild-type enzyme | Aeropyrum pernix K1 | |
0.0082 | - |
acetyl-Phe-2-naphthylamide | wild-type | Aeropyrum pernix | |
0.1 | - |
acetyl-Phe-2-naphthylamide | mutant H367A | Aeropyrum pernix | |
0.1 | - |
N-acetyl-Phe-2-naphthylamide | mutant H367A, larger than 0.1 | Aeropyrum pernix K1 |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
126100 | - |
calculated, dimer | Aeropyrum pernix K1 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aeropyrum pernix | Q9YBQ2 | - |
- |
Aeropyrum pernix K1 | Q9YBQ2 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Aeropyrum pernix K1 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-Phe-2-naphthylamide + H2O | - |
Aeropyrum pernix | acetyl-Phe + 2-naphthylamine | - |
? | |
N-acetyl-Phe-2-naphthylamide + H2O | kinetic assay | Aeropyrum pernix K1 | N-acetyl-L-Phe + 2-naphthylamine | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | - |
Aeropyrum pernix K1 |
Synonyms | Comment | Organism |
---|---|---|
AAP | - |
Aeropyrum pernix K1 |
AAP | - |
Aeropyrum pernix |
acylaminoacyl peptidase | - |
Aeropyrum pernix K1 |
ApAAP | - |
Aeropyrum pernix K1 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
70 | - |
- |
Aeropyrum pernix K1 |
74 | - |
wild-type | Aeropyrum pernix |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
90 | - |
both the wild-type and the H367A mutant are stable up to 90°C but tend to denature at higher temperature, more readily with the mutant. At lower temperature the wild-type has more flexible structural elements, particularly at 25°C, but differences diminish with increase of temperature | Aeropyrum pernix |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
- |
Aeropyrum pernix K1 |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0105 | - |
Ac-Phe-OH | wild-type enzyme | Aeropyrum pernix K1 | |
0.0105 | - |
Acetyl-Phe | wild-type | Aeropyrum pernix | |
0.0178 | - |
Acetyl-Phe | mutant H367A | Aeropyrum pernix | |
0.0178 | - |
Ac-Phe-OH | mutant H367A | Aeropyrum pernix K1 |