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Literature summary for 3.6.1.7 extracted from
- Affinity chromatographic purification of horse muscle acylphosphatase: evidence of the existence of multiple molecular forms (1983), Arch. Biochem. Biophys., 226, 414-424.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Cl- | competitive inhibition; Ho1, Ki: 40.0 mM; Ho2, Ki: 50.0 mM; Ho3, Ki: 40.0 mM | Equus caballus |  |
| phosphate | competitive inhibition; Ho1, Ki: 1.7 mM; Ho2, Ki: 2.3 mM; Ho3, Ki: 1.6 mM | Equus caballus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic data | Equus caballus | |
| additional information | - |
additional information | kinetic parameters of Ho1 and Ho3 are quite similar | Equus caballus | |
| 1.1 | - |
benzoyl phosphate | Ho3 | Equus caballus | |
| 2 | - |
benzoyl phosphate | Ho1 | Equus caballus | |
| 2.1 | - |
benzoyl phosphate | Ho2 | Equus caballus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 12000 | - |
Ho3, 2 * 12000, S-S dimer, SDS-PAGE with 2-mercaptoethanol | Equus caballus |
| 12100 | - |
Ho2, SDS-PAGE | Equus caballus |
| 12600 | - |
Ho1, SDS-PAGE | Equus caballus |
| 24200 | - |
Ho3, SDS-PAGE | Equus caballus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Equus caballus | - |
multiple molecular forms: Ho1, Ho2 and Ho3 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| multiple molecular forms: Ho1, Ho2 and Ho3 | Equus caballus |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| an acylphosphate + H2O = a carboxylate + phosphate | thermodynamic data | 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 | - |
Ho2 | Equus caballus |
| 3500 | - |
Ho3 | Equus caballus |
| 3900 | - |
Ho1 | Equus caballus |
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 | Equus caballus | carboxylate + phosphate | - |
? | |
| benzoyl phosphate + H2O | - |
Equus caballus | benzoate + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | Ho3, 2 * 12000, S-S dimer, SDS-PAGE with 2-mercaptoethanol | Equus caballus |
| monomer | Ho1, 1 * 12600, SDS-PAGE | Equus caballus |
| monomer | Ho2, 1 * 12100, SDS-PAGE | Equus caballus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Ho 1-3 | multiple forms of horse acylphosphatase | Equus caballus |
| Ho1 | multiple forms of horse acylphosphatase | Equus caballus |
| Ho2 | multiple forms of horse acylphosphatase | Equus caballus |
| Ho3 | multiple forms of horse acylphosphatase | 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 |
|---|---|---|---|
| 5.3 | - |
assay at | Equus caballus |
| 5.3 | - |
Ho1, Ho2 and Ho3 | Equus caballus |
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