Crystallization (Comment) | Organism |
---|---|
the structure of G91A mutant enzyme is determined by x-ray crystallography at 2.4 A resolution, and it is superimposable with the structure of wild-type enzyme | Pyrococcus horikoshii |
Protein Variants | Comment | Organism |
---|---|---|
G91A | at 10°C the mutant enzyme G91A lacking the salt-bridge retains a significantly greater kcat value than the wild-type enzyme | Pyrococcus horikoshii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | P84142 | - |
- |
Pyrococcus horikoshii OT-3 | P84142 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
benzoyl phosphate + H2O | - |
Pyrococcus horikoshii | benzoate + phosphate | - |
? | |
benzoyl phosphate + H2O | - |
Pyrococcus horikoshii OT-3 | benzoate + phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PhAcP | - |
Pyrococcus horikoshii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
assay at | Pyrococcus horikoshii |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
a rigidifying salt-bridge favors the activity of thermophilic enzyme at high temperatures at the expense of low-temperature activity. The thermophilic acylphosphatase from Pyrococcus horikoshii and its homologous mesophilic acylphosphatase from human is employed as a model to study how local rigidity of an active-site residue affects the enzymatic activity | Pyrococcus horikoshii |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
211 | - |
benzoyl phosphate | pH 5.3, 25°C, mutant enzyme GG91A | Pyrococcus horikoshii | |
228 | - |
benzoyl phosphate | pH 5.3, 25°C, wild-type enzyme | Pyrococcus horikoshii | |
520 | - |
benzoyl phosphate | pH 5.3, 45°C, mutant enzyme GG91A | Pyrococcus horikoshii | |
760 | - |
benzoyl phosphate | pH 5.3, 45°C, wild-type enzyme | Pyrococcus horikoshii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.3 | - |
assay at | Pyrococcus horikoshii |