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- W1966328705 abstract "The specificity of CTP:phosphocholine cytidylyltransferase from rat liver for phosphorylated bases has been investigated. The apparent Km for phosphocholine was 0.17 mM. As the number of methyl substituents on the phospho-base decreased, the apparent Km increased: 4.0 mM for phosphodimethylethanolamine, 6.9 for phosphomonomethylethanolamine and 68.4 for phosphoethanolamine. The Vmax for the reaction was similar for phosphocholine (12.6 mumol/min per mg protein), phosphomonomethylethanolamine (13.5 mumol/min per mg protein) and phosphoethanolamine (9.2 mumol/min per mg protein). When phosphodimethylethanolamine was the substrate, the Vmax was 3-fold higher (40.3 mumol/min per mg protein). Phosphoethanolamine, phosphomonomethylethanolamine and phosphodimethylethanolamine were competitive inhibitors of the cytidylyltransferase when phosphocholine was used as substrate with Ki values of 18.5 mM, 9.3 mM and 1.5 mM, respectively. The results show that the cytidylyltransferase is highly specific for phosphocholine." @default.
- W1966328705 created "2016-06-24" @default.
- W1966328705 creator A5036771813 @default.
- W1966328705 creator A5073998071 @default.
- W1966328705 date "1991-11-01" @default.
- W1966328705 modified "2023-09-27" @default.
- W1966328705 title "Substrate specificity of CTP: phosphocholine cytidyltransferase" @default.
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- W1966328705 doi "https://doi.org/10.1016/0005-2760(91)90178-k" @default.
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