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Literature summary extracted from

  • Ramponi, G.; Guerritore, A.; Treves, C.; Nassi, P.; Baccari, V.
    Horse muscle acyl phosphatase: purification and some properties (1969), Arch. Biochem. Biophys., 130, 362-369.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.6.1.7 8450 10300 muscle, low speed sedimentation equilibrium, Archibald method Equus caballus
3.6.1.7 9400
-
 muscle, low speed sedimentation equilibrium, Archibald method Equus caballus
3.6.1.7 9750
-
 muscle, gel filtration Equus caballus

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.7 Equus caballus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.7 muscle Equus caballus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.6.1.7 muscle
-
 Equus caballus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.6.1.7 3000 3200 muscle Equus caballus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.7 1,3-diphosphoglycerate + H2O
-
 Equus caballus 3-phosphoglycerate + phosphate
-
 ?
3.6.1.7 acetyl phosphate + H2O
-
 Equus caballus acetate + phosphate
-
 ?
3.6.1.7 acylphosphate + H2O specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Equus caballus carboxylate + phosphate
-
 ?
3.6.1.7 ATP + H2O muscle enzyme, very low activity Equus caballus ?
-
 ?
3.6.1.7 benzoyl phosphate + H2O
-
 Equus caballus benzoate + phosphate
-
 ?
3.6.1.7 carbamoyl phosphate + H2O muscle enzyme, poor substrate Equus caballus carbamate + phosphate
-
 ?
3.6.1.7 diphosphate + H2O muscle enzyme, very low activity Equus caballus 2 phosphate
-
 ?
3.6.1.7 additional information substrate specificity Equus caballus ?
-
 ?
3.6.1.7 additional information specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Equus caballus ?
-
 ?
3.6.1.7 additional information acetyl-AMP: not a substrate Equus caballus ?
-
 ?
3.6.1.7 additional information liver enzyme and muscle enzyme, no activity with acetyl-AMP, phosphoenolpyruvate and phosvitin Equus caballus ?
-
 ?
3.6.1.7 p-nitrobenzoyl phosphate + H2O
-
 Equus caballus p-nitrobenzoate + phosphate
-
 ?
3.6.1.7 p-nitrophenyl phosphate + H2O muscle enzyme, very low activity at pH 5.3, no activity at pH 10.4 Equus caballus p-nitrophenol + phosphate
-
 ?
3.6.1.7 phosphocreatine + H2O muscle enzyme, very low activity Equus caballus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.6.1.7 monomer
-
 Equus caballus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.7 25
-
 assay at Equus caballus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.7 additional information
-
 muscle, pI: 11.4 Equus caballus
3.6.1.7 additional information
-
 muscle enzyme is very basic protein Equus caballus
3.6.1.7 5.3
-
 assay at Equus caballus