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Literature summary extracted from

  • Cooper, P.H.; Hawthorne, J.N.
    Phosphomonoesterase hydrolysis of polyphosphoinositides in rat kidney: Properties and subcellular localization of the enzyme system (1975), Biochem. J., 150, 537-551.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.36 cetyltrimethylammonium bromide only activates when added with the substrate and in the presence of Mg2+ Rattus norvegicus
3.1.3.36 Cutsum
-
Rattus norvegicus
3.1.3.36 sodium deoxycholate
-
Rattus norvegicus
3.1.3.36 Triton X-100
-
Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.36 Golgi apparatus
-
Rattus norvegicus 5794
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.36 Ca2+ activates Rattus norvegicus
3.1.3.36 Li+ activates Rattus norvegicus
3.1.3.36 Mg2+ activated Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.36 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.36 kidney the enzyme is more active in the kidney cortex than in the medulla Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.36 phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
-
Rattus norvegicus phosphatidylinositol 4-phosphate + phosphate
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.36 7.5
-
-
Rattus norvegicus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.3.36 6.5 8.3 pH 6.5: about 60% of maximal activity, pH 8.3: about 50% of maximal activity Rattus norvegicus