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Literature summary extracted from

  • Liguri, G.; Nassi, P.; Camici, G.; Manao, G.; Cappugi, G.; Stefani, M.; Berti, A.; Ramponi, G.
    Studies on synthesis and degradation rates and some molecular properties of guinea-pig muscle acylphosphatase (1984), Biochem. J., 217, 499-505.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.7 Cl- competitive inhibition; GP1, Ki: 29.1 mM Cavia porcellus
3.6.1.7 Cl- competitive inhibition; Ho1, Ki: 40.0 mM Equus caballus
3.6.1.7 Cl- competitive inhibition; T1, Ki: 40.0 mM Meleagris gallopavo
3.6.1.7 phosphate competitive inhibition; GP1, Ki: 1.73 mM Cavia porcellus
3.6.1.7 phosphate competitive inhibition; Ho1, Ki: 1.7 mM Equus caballus
3.6.1.7 phosphate competitive inhibition; T1, Ki: 2.8 mM Meleagris gallopavo

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.7 additional information
-
additional information kinetic data Meleagris gallopavo
3.6.1.7 additional information
-
additional information kinetic data Cavia porcellus
3.6.1.7 additional information
-
additional information kinetic data Equus caballus
3.6.1.7 0.57
-
benzoyl phosphate GP1 Cavia porcellus
3.6.1.7 1
-
benzoyl phosphate T1 Meleagris gallopavo
3.6.1.7 1.08
-
acetyl phosphate GP1 Cavia porcellus
3.6.1.7 2
-
benzoyl phosphate Ho1 Equus caballus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.1.7 cytoplasm
-
Meleagris gallopavo 5737
-
3.6.1.7 cytoplasm
-
Equus caballus 5737
-
3.6.1.7 cytoplasm in proximity to sarcoplasmic reticulum Cavia porcellus 5737
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.6.1.7 11370
-
muscle, calculated from amino acid sequence Equus caballus
3.6.1.7 12000
-
GP1, SDS-PAGE Cavia porcellus
3.6.1.7 12600
-
Ho1, SDS-PAGE Equus caballus
3.6.1.7 13400
-
T1, SDS-PAGE Meleagris gallopavo
3.6.1.7 24000
-
GP3, SDS-PAGE Cavia porcellus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.7 additional information Meleagris gallopavo acylphosphatase seems to have a regulatory function, controlling the concentrations of highly reactive compounds such as acyl phosphates ?
-
?
3.6.1.7 additional information Cavia porcellus acylphosphatase seems to have a regulatory function, controlling the concentrations of highly reactive compounds such as acyl phosphates ?
-
?
3.6.1.7 additional information Equus caballus acylphosphatase seems to have a regulatory function, controlling the concentrations of highly reactive compounds such as acyl phosphates ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.7 Cavia porcellus
-
guinea pig
-
3.6.1.7 Cavia porcellus
-
three molecular forms: GP1, GP2 and GP3
-
3.6.1.7 Equus caballus
-
-
-
3.6.1.7 Meleagris gallopavo
-
turkey
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.7
-
Cavia porcellus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.6.1.7 muscle skeletal muscle Meleagris gallopavo
-
3.6.1.7 muscle skeletal muscle Cavia porcellus
-
3.6.1.7 muscle skeletal 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 3300
-
GP2 Cavia porcellus
3.6.1.7 3500
-
-
Equus caballus
3.6.1.7 3500
-
GP3 Cavia porcellus
3.6.1.7 3500
-
T1 Meleagris gallopavo
3.6.1.7 3600
-
GP1 Cavia porcellus
3.6.1.7 3800
-
Ho1 Equus caballus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.7 acetyl phosphate + H2O
-
Cavia porcellus acetate + 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 Meleagris gallopavo carboxylate + phosphate
-
?
3.6.1.7 acylphosphate + H2O specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Cavia porcellus carboxylate + 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 benzoyl phosphate + H2O
-
Meleagris gallopavo benzoate + phosphate
-
?
3.6.1.7 benzoyl phosphate + H2O
-
Cavia porcellus benzoate + phosphate
-
?
3.6.1.7 benzoyl phosphate + H2O
-
Equus caballus benzoate + phosphate
-
?
3.6.1.7 additional information acylphosphatase seems to have a regulatory function, controlling the concentrations of highly reactive compounds such as acyl phosphates Meleagris gallopavo ?
-
?
3.6.1.7 additional information acylphosphatase seems to have a regulatory function, controlling the concentrations of highly reactive compounds such as acyl phosphates Cavia porcellus ?
-
?
3.6.1.7 additional information acylphosphatase seems to have a regulatory function, controlling the concentrations of highly reactive compounds such as acyl phosphates Equus caballus ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.6.1.7 GP 1-3 multiple forms of guinea pig acylphosphatase Cavia porcellus
3.6.1.7 GP1 multiple forms of guinea pig acylphosphatase, major form Cavia porcellus
3.6.1.7 GP2 multiple forms of guinea pig acylphosphatase Cavia porcellus
3.6.1.7 GP3 multiple forms of guinea pig acylphosphatase Cavia porcellus
3.6.1.7 Ho1 multiple forms of horse acylphosphatase Equus caballus
3.6.1.7 T1 multiple forms of turkey acylphosphatase Meleagris gallopavo

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.7 25
-
assay at Meleagris gallopavo
3.6.1.7 25
-
assay at Cavia porcellus
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 5.1
-
GP1 Cavia porcellus
3.6.1.7 5.3
-
assay at Meleagris gallopavo
3.6.1.7 5.3
-
assay at Cavia porcellus
3.6.1.7 5.3
-
assay at Equus caballus
3.6.1.7 5.3
-
Ho1 Equus caballus
3.6.1.7 5.3
-
T1 Meleagris gallopavo