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Literature summary for 3.6.1.7 extracted from
- A novel 8-nm protein cage formed by Vibrio cholerae acylphosphatase (2014), J. Mol. Biol., 426, 36-38.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C20R | the mutant is nearly 100000 times more efficient in catalysis than the wild type protein | Vibrio cholerae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.36 | - |
acetyl phosphate | mutant enzyme C20R, pH and temperature not specified in the publication | Vibrio cholerae |  |
| 8.53 | - |
acetyl phosphate | wild type enzyme, pH and temperature not specified in the publication | Vibrio cholerae | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Vibrio cholerae | A5F8G9 | - |
- |
| Vibrio cholerae O395 | A5F8G9 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl phosphate + H2O | - |
Vibrio cholerae | acetate + phosphate | - |
? | |
| acetyl phosphate + H2O | - |
Vibrio cholerae O395 | acetate + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ACP | - |
Vibrio cholerae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00000155 | - |
acetyl phosphate | wild type enzyme, pH and temperature not specified in the publication | Vibrio cholerae | |
| 0.043 | - |
acetyl phosphate | mutant enzyme C20R, pH and temperature not specified in the publication | Vibrio cholerae | |
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