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Literature summary for 2.7.8.1 extracted from

  • Roberti, R.; Vecchini, A.; Freysz, L.; Masoom, M.; Binaglia, L.
    An improved procedure for the purification of ethanolaminephosphotransferase. Reconstitution of the purified enzyme with lipids (1989), Biochim. Biophys. Acta, 1004, 80-88.
    View publication on PubMed
Search for more literature for 2.7.8.1

Inhibitors

Inhibitors Comment Organism Structure
dipalmitoylphosphatidylcholine
-
 Rattus norvegicus
Dipalmitoylphosphatidylethanolamine
-
 Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km for CDP-ethanolamine depends on composition of the lipid mixture utilized for reconstitution of solubilized enzyme Rattus norvegicus

Localization

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.705
-
 37°C, pH 8.2 Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CDP-ethanolamine + 1,2-diacylglycerol
-
 Rattus norvegicus CMP + a phosphatidylethanolamine
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Rattus norvegicus