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Literature summary extracted from

  • Kawakita, N.; Yamazaki, M.
    Immobilization of nucleoside diphosphatase at its allosteric site using immobilized derivatives of pyridoxal 5 -phosphate (1980), Arch. Biochem. Biophys., 204, 326-330.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.6.1.6 ATP 0.2 mM ATP stimulates free enzyme 2.6fold when IDP is used as substrate, immobilized enzyme on CNBr-activated Sepharose is activated almost to the same degree, the immobilized enzyme on the 3-O-pyridoxal 5'-phosphate-Sepharose is less sensitive to ATP Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.1.6 microsome
-
 Rattus norvegicus
-
-

Organism

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.6.1.6 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.6 IDP + H2O
-
 Rattus norvegicus IMP + phosphate
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.6 38
-
 free enzyme Rattus norvegicus
3.6.1.6 50
-
 immobilized enzyme Rattus norvegicus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.6.1.6 50
-
 5 min, immobilized enzyme is stable, free enzyme loses about 90% of its activity Rattus norvegicus
3.6.1.6 55
-
 5 min, about 50% loss of activity of the immobilized enzyme, complete loss of activity of the free enzyme Rattus norvegicus