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Literature summary for 3.1.3.16 extracted from

  • Stewart, A.A.; Cohen, P.
    Protein phosphatase-2B from rabbit skeletal muscle: a Ca2+-dependent, calmodulin-stimulated enzyme (1988), Methods Enzymol., 159, 409-416.
    View publication on PubMed
Search for more literature for 3.1.3.16

General Stability

General Stability Organism
Ca2+, lability in muscle extracts Oryctolagus cuniculus
calmodulin-Sepharose chromatography, decrease of stability Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Oryctolagus cuniculus 5737
-

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
phosphatase 2B 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

Storage Stability

Storage Stability Organism
-20°C, 50 mM Tris-HCl buffer, pH 7.0, 50% glycerol, up to 6 months Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoproteins + H2O
-
 Oryctolagus cuniculus proteins + phosphate
-
 ?
phosphorylated cAMP-dependent protein kinase + H2O regulatory subunit Oryctolagus cuniculus cAMP-dependent protein kinase + phosphate
-
 ?
phosphorylated inhibitor-1 + H2O
-
 Oryctolagus cuniculus inhibitor-1 + phosphate
-
 ?