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Literature summary extracted from

  • Ramponi, G.; Nassi, P.; Cappugi, G.; Treves, C.; Manao, G.
    Purification and some molecular properties of horse liver acyl phosphatase (1972), Biochim. Biophys. Acta, 284, 485-496.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.6.1.7 liver enzyme, stable to acid treatment Equus caballus
3.6.1.7 two acyl phosphatase activities in liver, one labile and the other acid, heat stable Equus caballus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.7 phosphate
-
Equus caballus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.6.1.7 8300
-
liver, gel filtration Equus caballus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.7 1,3-diphosphoglycerate + H2O Equus caballus carbamoyl phosphate and 1,3-diphosphoglycerate can acylate and carbamylate some proteins, acyl phosphatase could prevent such acylation and carbamylation, exerting a regulatory role on the intracellular concentration of 1,3-diphosphoglycerate and carbamoyl phosphate 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O Equus caballus possible physiological substrate 3-phosphoglycerate + phosphate
-
?
3.6.1.7 carbamoyl phosphate + H2O Equus caballus carbamoyl phosphate and 1,3-diphosphoglycerate can acylate and carbamylate some proteins, acyl phosphatase could prevent such acylation and carbamylation, exerting a regulatory role on the intracellular concentration of 1,3-diphosphoglycerate and carbamoyl phosphate carbamate + phosphate
-
?
3.6.1.7 carbamoyl phosphate + H2O Equus caballus liver enzyme, carbamoyl phosphate can reach high concentrations in liver and its level may be partly controlled by acyl phosphatase carbamate + phosphate
-
?
3.6.1.7 carbamoyl phosphate + H2O Equus caballus possible physiological substrate carbamate + phosphate
-
?
3.6.1.7 additional information Equus caballus carbamoyl phosphate and 1,3-diphosphoglycerate can acylate and carbamylate some proteins, acyl phosphatase could prevent such acylation and carbamylation, exerting a regulatory role on the intracellular concentration of 1,3-diphosphoglycerate and carbamoyl phosphate ?
-
?
3.6.1.7 additional information Equus caballus possible role in regulating the glycolytic pathway, ureogenesis and pyrimidine biosynthesis ?
-
?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.7 liver Equus caballus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.6.1.7 brain
-
Equus caballus
-
3.6.1.7 liver
-
Equus caballus
-
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 2800
-
liver 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 1,3-diphosphoglycerate + H2O carbamoyl phosphate and 1,3-diphosphoglycerate can acylate and carbamylate some proteins, acyl phosphatase could prevent such acylation and carbamylation, exerting a regulatory role on the intracellular concentration of 1,3-diphosphoglycerate and carbamoyl phosphate Equus caballus 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O possible physiological substrate 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 liver enzyme, no activity Equus caballus ?
-
?
3.6.1.7 benzoyl phosphate + H2O
-
Equus caballus benzoate + phosphate
-
?
3.6.1.7 carbamoyl phosphate + H2O
-
Equus caballus carbamate + phosphate
-
?
3.6.1.7 carbamoyl phosphate + H2O carbamoyl phosphate and 1,3-diphosphoglycerate can acylate and carbamylate some proteins, acyl phosphatase could prevent such acylation and carbamylation, exerting a regulatory role on the intracellular concentration of 1,3-diphosphoglycerate and carbamoyl phosphate Equus caballus carbamate + phosphate
-
?
3.6.1.7 carbamoyl phosphate + H2O liver enzyme, carbamoyl phosphate can reach high concentrations in liver and its level may be partly controlled by acyl phosphatase Equus caballus carbamate + phosphate
-
?
3.6.1.7 carbamoyl phosphate + H2O possible physiological substrate Equus caballus carbamate + phosphate
-
?
3.6.1.7 diphosphate + H2O liver enzyme, no 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 additional information relative hydrolysis rates Equus caballus ?
-
?
3.6.1.7 additional information carbamoyl phosphate and 1,3-diphosphoglycerate can acylate and carbamylate some proteins, acyl phosphatase could prevent such acylation and carbamylation, exerting a regulatory role on the intracellular concentration of 1,3-diphosphoglycerate and carbamoyl phosphate Equus caballus ?
-
?
3.6.1.7 additional information possible role in regulating the glycolytic pathway, ureogenesis and pyrimidine biosynthesis Equus caballus ?
-
?
3.6.1.7 p-nitrobenzoyl phosphate + H2O
-
Equus caballus p-nitrobenzoate + phosphate
-
?
3.6.1.7 p-nitrophenyl phosphate + H2O liver enzyme, no activity at pH 5.3 and 10.4 Equus caballus p-nitrophenol + phosphate
-
?
3.6.1.7 phosphocreatine + H2O liver enzyme, no activity Equus caballus ?
-
?

Subunits

EC Number Subunits Comment Organism
3.6.1.7 monomer liver, 1 * 8300, SDS-PAGE 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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.6.1.7 additional information
-
enzyme is thermostable Equus caballus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.7 5.3
-
assay at Equus caballus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.6.1.7 additional information
-
liver enzyme is acid stable Equus caballus