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- W4302182893 abstract "An enzyme that converts CMP into CDP-choline has been demonstrated in microsomal preparations of larvae of Artemia salina . We conclude that this enzyme is CDP-choline: 1,2-diglyceride cholinephosphotransferase (EC 2.7.8.2) and that the steady-state of the reaction at low concentrations of CMP appears to favor formation of CDP-choline. The enzymatic activity is completely dependent upon the addition of CMP and metal ions (Mn 2+ , Mg 2+ , or Co 2+ ). No other cytidine compounds can substitute for CMP in the reaction. The optimal pH for formation of CDP-choline is 7.1 and 6.4 with Mg 2+ and Mn 2+ , respectively, as cofactors. Optimal concentrations of Mg 2+ and Mn 2+ are 50 and 5 mM, respectively; and the optimal concentrations of CMP are 75 and 2 μM for Mg 2+ and Mn 2+ , respectively. Enzyme activity is inhibited by Ca 2+ and P -chloromercuribenzoate, whereas F − and iodoacetate have no effect. A stoichiometric relationship exists between the amount of phosphorus lost from phosphatidyl choline and the amount appearing in CDP-choline, indicating that phosphatidyl choline is the source of phosphocholine in CDP-choline formation." @default.
- W4302182893 created "2022-10-06" @default.
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- W4302182893 date "1970-12-01" @default.
- W4302182893 modified "2023-09-23" @default.
- W4302182893 title "Phospholipid metabolism during development of the brine shrimp Artemia salina" @default.
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- W4302182893 doi "https://doi.org/10.1016/0005-2760(70)90009-3" @default.
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