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Literature summary for 3.6.1.7 extracted from
- Horse muscle acyl phosphatase: purification and some properties (1969), Arch. Biochem. Biophys., 130, 362-369.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 8450 | 10300 | muscle, low speed sedimentation equilibrium, Archibald method | Equus caballus |
| 9400 | - |
muscle, low speed sedimentation equilibrium, Archibald method | Equus caballus |
| 9750 | - |
muscle, gel filtration | Equus caballus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Equus caballus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| muscle | Equus caballus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| muscle | - |
Equus caballus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 3000 | 3200 | muscle | Equus caballus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1,3-diphosphoglycerate + H2O | - |
Equus caballus | 3-phosphoglycerate + phosphate | - |
? |  |
| acetyl phosphate + H2O | - |
Equus caballus | acetate + phosphate | - |
? | |
| acylphosphate + H2O | specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates | Equus caballus | carboxylate + phosphate | - |
? | |
| ATP + H2O | muscle enzyme, very low activity | Equus caballus | ? | - |
? | |
| benzoyl phosphate + H2O | - |
Equus caballus | benzoate + phosphate | - |
? | |
| carbamoyl phosphate + H2O | muscle enzyme, poor substrate | Equus caballus | carbamate + phosphate | - |
? | |
| diphosphate + H2O | muscle enzyme, very low activity | Equus caballus | 2 phosphate | - |
? | |
| additional information | substrate specificity | Equus caballus | ? | - |
? | |
| additional information | specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates | Equus caballus | ? | - |
? | |
| additional information | acetyl-AMP: not a substrate | Equus caballus | ? | - |
? | |
| additional information | liver enzyme and muscle enzyme, no activity with acetyl-AMP, phosphoenolpyruvate and phosvitin | Equus caballus | ? | - |
? | |
| p-nitrobenzoyl phosphate + H2O | - |
Equus caballus | p-nitrobenzoate + phosphate | - |
? | |
| p-nitrophenyl phosphate + H2O | muscle enzyme, very low activity at pH 5.3, no activity at pH 10.4 | Equus caballus | p-nitrophenol + phosphate | - |
? | |
| phosphocreatine + H2O | muscle enzyme, very low activity | Equus caballus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | - |
Equus caballus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Equus caballus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
muscle, pI: 11.4 | Equus caballus |
| additional information | - |
muscle enzyme is very basic protein | Equus caballus |
| 5.3 | - |
assay at | Equus caballus |
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Release 2023.1 (January 2023)
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