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Literature summary for 3.6.1.6 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

Activating Compound Comment Organism Structure
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

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Rattus norvegicus
-
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

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