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Literature summary for 2.7.7.41 extracted from

  • Van Heusden, G.P.H.; Van den Bosch, H.
    The influence of exogenous and of membrane-bound phosphatidate concentration on the activity of CTP: phosphatidate cytidylyltransferase and phosphatidate phosphohydrolase (1978), Eur. J. Biochem., 84, 405-412.
    View publication on PubMed
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Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
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 Rattus norvegicus
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Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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Source Tissue

Source Tissue Comment Organism Textmining
liver
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 Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CTP + phosphatidate the enzyme shows a linear increase in activity with membrane-bound phosphatidate concentrations up to at least 100 nmol phosphatidate per mg of microsomal protein. The enzyme has a large reserve capacity and suggests that the enzyme is operating intracellularly, i.e. at phosphatidate concentrations of 5-10 mM/mg endoplasmic reticulum protein, far below the maximal capacity. The ratio of phosphatidate conversion into CDP diglyceride and 1,2-diglyceride seems to be constant for a large range of membrane-bounmd phosphatidate concentrations. The membrane-bound enzyme cannot utilize phosphatidate substrate present in heat denatured membranes, but is active on phosphatidate incorporated into membranes of phospholipid vesicles Rattus norvegicus diphosphate + CDPdiacylglycerol
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