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Literature summary for 3.6.1.7 extracted from

  • Shiokawa, H.; Noda, L.
    Isolation and crystallization of acyl phosphatase from rabbit muscle (1970), J. Biol. Chem., 245, 669-673.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
23500
-
sedimentation equilibrium Oryctolagus cuniculus

Organic Solvent Stability

Organic Solvent Comment Organism
Acetone 70% v/v, stable at -10°C for 3 h Oryctolagus cuniculus
Ethanol unstable to Oryctolagus cuniculus
Methanol unstable to Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
860
-
muscle Oryctolagus cuniculus

Storage Stability

Storage Stability Organism
-10°C, crystalline enzyme, 42% ammonium sulfate, stable for long periods, 1 year with no loss of activity Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl phosphate + H2O
-
Oryctolagus cuniculus acetate + phosphate
-
?
acylphosphate + H2O specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Oryctolagus cuniculus carboxylate + phosphate
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4
-
muscle, assay at Oryctolagus cuniculus

pH Stability

pH Stability pH Stability Maximum Comment Organism
additional information
-
stable at acidic and neutral pH, somewhat unstable at alkaline pH Oryctolagus cuniculus
3 5.4 stable 12 h , 37°C Oryctolagus cuniculus
9
-
1 h, 2°C: 30% loss of activity Oryctolagus cuniculus