Abstract
CTP:phosphoethanolamine cytidylyltransferase (ethanolamine-phosphate cytidylyltransferase) is considered as key regulatory enzyme of the biosynthesis of phosphatidylethanolamine via the CDPethanolamine pathway. The assay and partial purification of cytosolic enzyme discussed in the chapter. The assay is based on the conversion of phospho[1,2-14C]ethanolamine to CDP[l,2-14C]ethanolamine. Radioactive substrate and reaction product are separated by thin-layer chromatography; followed by the determination of the radioactivity in CDPethanolamine. Phosphoethanolamine cytidylyltransferase has a sharp optimum at pH 7.8 and a broader one with lower maximal activity, around pH 6. The enzyme has a limited stability below pH 7. The activity of purified enzyme is dependent on the presence of dithiothreitol in the assay mixture. The enzyme has a molecular weight of 100,000 to 120,000 as estimated by superose 12 gel filtration. In contrast to CTP:phosphocholine cytidylyltransferase, which is an ambiquitous enzyme, phosphoethanolamine cytidylyltransferase is localized predominantly in the cytosol.
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