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Literature summary extracted from

  • Satchell, D.P.N.; Spencer, N.; White, G.F.
    Kinetic studies with muscle acylphosphatase (1972), Biochim. Biophys. Acta, 268, 233-248.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.6.1.7 muscle enzyme, unusually stable to acid treatment Gallus gallus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.7 Cl-
-
 Gallus gallus
3.6.1.7 ClO4-
-
 Gallus gallus
3.6.1.7 glucose glucose buffer, pH 11.2-12.0, progressive inactivation, complete after 1 h Gallus gallus
3.6.1.7 Hg2+ muscle enzyme, 0.1 mM, 30 min: 30% inhibition Gallus gallus
3.6.1.7 additional information no inhibition by carboxylic acid, acetic acid, acetate, Na+ Gallus gallus
3.6.1.7 NaCl
-
 Gallus gallus
3.6.1.7 NaClO4
-
 Gallus gallus
3.6.1.7 p-chloromercuribenzoate muscle enzyme, 1 mM: no inhibition Gallus gallus
3.6.1.7 phosphate phosphate, competitive inhibition Gallus gallus
3.6.1.7 Sodium thioglycollate muscle enzyme, 0.12 M, 3 h: 30% inhibition Gallus gallus

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 Gallus gallus
3.6.1.7 additional information
-
 additional information kinetic studies Gallus gallus
3.6.1.7 additional information
-
 additional information kinetic characterization, kinetic data Gallus gallus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.7 additional information muscle enzyme, no metal ion requirement Gallus gallus

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.7 Gallus gallus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.7
-
 Gallus gallus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.6.1.7 an acylphosphate + H2O = a carboxylate + phosphate reaction mechanism Gallus gallus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.6.1.7 muscle breast muscle Gallus gallus
-

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 Gallus gallus carboxylate + phosphate
-
 ?
3.6.1.7 benzoyl phosphate + H2O
-
 Gallus gallus benzoate + phosphate
-
 ?

Temperature Optimum [°C]

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.6.1.7 additional information
-
 muscle enzyme, unusually thermostable Gallus gallus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.7 additional information
-
 muscle enzyme, pH analyses of reaction Gallus gallus
3.6.1.7 additional information
-
 muscle enzyme is very basic protein Gallus gallus
3.6.1.7 5 6
-
 Gallus gallus
3.6.1.7 5.3
-
 assay at Gallus gallus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.6.1.7 3 12
-
 Gallus gallus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.6.1.7 additional information
-
 muscle enzyme, unusually stable to acid Gallus gallus
3.6.1.7 1
-
 stable in acid solutions up to pH 1 Gallus gallus
3.6.1.7 11.2 12 progressive inactivation, complete inactivation after 1 h Gallus gallus