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Literature summary for 3.1.3.16 extracted from

  • Paris, H.; Ganapathi, M.K.; Silberman, S.R.; Aylward, J.H.; Lee, E.Y.C.
    Isolation and characterization of a high molecular weight protein phosphatase from rabbit skeletal muscle (1984), J. Biol. Chem., 259, 7510-7518.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.004
-
phosphorylase a presence of Mn2+ Oryctolagus cuniculus
0.021
-
phosphorylase a absence of Mn2+ Oryctolagus cuniculus
0.058
-
phosphohistone
-
Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ activation Oryctolagus cuniculus

Organic Solvent Stability

Organic Solvent Comment Organism
Ethanol inactivation Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphophosphorylase kinase + H2O specific for alpha-subunit Oryctolagus cuniculus phosphorylase kinase + phosphate
-
?
phosphoproteins + H2O
-
Oryctolagus cuniculus proteins + phosphate
-
?
phosphorylase a + H2O
-
Oryctolagus cuniculus phosphorylase b + phosphate
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
4 min, 50% activity Oryctolagus cuniculus