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Literature summary for 3.6.1.7 extracted from
- Kinetic studies with muscle acylphosphatase (1972), Biochim. Biophys. Acta, 268, 233-248.
General Stability
| General Stability | Organism |
|---|---|
| muscle enzyme, unusually stable to acid treatment | Gallus gallus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Cl- | - |
Gallus gallus |  |
| ClO4- | - |
Gallus gallus | |
| glucose | glucose buffer, pH 11.2-12.0, progressive inactivation, complete after 1 h | Gallus gallus | |
| Hg2+ | muscle enzyme, 0.1 mM, 30 min: 30% inhibition | Gallus gallus | |
| additional information | no inhibition by carboxylic acid, acetic acid, acetate, Na+ | Gallus gallus | |
| NaCl | - |
Gallus gallus | |
| NaClO4 | - |
Gallus gallus | |
| p-chloromercuribenzoate | muscle enzyme, 1 mM: no inhibition | Gallus gallus | |
| phosphate | phosphate, competitive inhibition | Gallus gallus | |
| Sodium thioglycollate | muscle enzyme, 0.12 M, 3 h: 30% inhibition | Gallus gallus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic data | Gallus gallus | |
| additional information | - |
additional information | kinetic studies | Gallus gallus | |
| additional information | - |
additional information | kinetic characterization, kinetic data | Gallus gallus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | muscle enzyme, no metal ion requirement | Gallus gallus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Gallus gallus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Gallus gallus |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| an acylphosphate + H2O = a carboxylate + phosphate | reaction mechanism | Gallus gallus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| muscle | breast muscle | Gallus gallus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acylphosphate + H2O | specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates | Gallus gallus | carboxylate + phosphate | - |
? | |
| benzoyl phosphate + H2O | - |
Gallus gallus | benzoate + phosphate | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Gallus gallus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
muscle enzyme, unusually thermostable | Gallus gallus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
muscle enzyme, pH analyses of reaction | Gallus gallus |
| additional information | - |
muscle enzyme is very basic protein | Gallus gallus |
| 5 | 6 | - |
Gallus gallus |
| 5.3 | - |
assay at | Gallus gallus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 12 | - |
Gallus gallus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
muscle enzyme, unusually stable to acid | Gallus gallus |
| 1 | - |
stable in acid solutions up to pH 1 | Gallus gallus |
| 11.2 | 12 | progressive inactivation, complete inactivation after 1 h | Gallus gallus |
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