Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Manao, G.; Camici, G.; Stefani, M.; Berti, A.; Cappugi, G.; Liguri, G.; Nassi, P.; Ramponi, G.
    Affinity chromatographic purification of horse muscle acylphosphatase: evidence of the existence of multiple molecular forms (1983), Arch. Biochem. Biophys., 226, 414-424.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.7 Cl- competitive inhibition; Ho1, Ki: 40.0 mM; Ho2, Ki: 50.0 mM; Ho3, Ki: 40.0 mM Equus caballus
3.6.1.7 phosphate competitive inhibition; Ho1, Ki: 1.7 mM; Ho2, Ki: 2.3 mM; Ho3, Ki: 1.6 mM Equus caballus

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 Equus caballus
3.6.1.7 additional information
-
 additional information kinetic parameters of Ho1 and Ho3 are quite similar Equus caballus
3.6.1.7 1.1
-
 benzoyl phosphate Ho3 Equus caballus
3.6.1.7 2
-
 benzoyl phosphate Ho1 Equus caballus
3.6.1.7 2.1
-
 benzoyl phosphate Ho2 Equus caballus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.6.1.7 12000
-
 Ho3, 2 * 12000, S-S dimer, SDS-PAGE with 2-mercaptoethanol Equus caballus
3.6.1.7 12100
-
 Ho2, SDS-PAGE Equus caballus
3.6.1.7 12600
-
 Ho1, SDS-PAGE Equus caballus
3.6.1.7 24200
-
 Ho3, SDS-PAGE Equus caballus

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.7 Equus caballus
-
 multiple molecular forms: Ho1, Ho2 and Ho3
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.7 multiple molecular forms: Ho1, Ho2 and Ho3 Equus caballus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.6.1.7 an acylphosphate + H2O = a carboxylate + phosphate thermodynamic data Equus caballus
a

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
-
 Ho2 Equus caballus
3.6.1.7 3500
-
 Ho3 Equus caballus
3.6.1.7 3900
-
 Ho1 Equus caballus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 Equus caballus benzoate + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.6.1.7 dimer Ho3, 2 * 12000, S-S dimer, SDS-PAGE with 2-mercaptoethanol Equus caballus
3.6.1.7 monomer Ho1, 1 * 12600, SDS-PAGE Equus caballus
3.6.1.7 monomer Ho2, 1 * 12100, SDS-PAGE Equus caballus

Synonyms

EC Number Synonyms Comment Organism
3.6.1.7 Ho 1-3 multiple forms of horse acylphosphatase Equus caballus
3.6.1.7 Ho1 multiple forms of horse acylphosphatase Equus caballus
3.6.1.7 Ho2 multiple forms of horse acylphosphatase Equus caballus
3.6.1.7 Ho3 multiple forms of horse acylphosphatase 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 5.3
-
 assay at Equus caballus
3.6.1.7 5.3
-
 Ho1, Ho2 and Ho3 Equus caballus