High impact information on Pcyt2

• CTP:phosphoethanolamine cytidylyltransferase (ET) (ethanolamine-phosphate cytidylyltransferase, EC 2.7.7.14), which is generally considered as the rate-regulatory enzyme of phosphatidylethanolamine synthesis via the CDP-ethanolamine pathway, was purified to homogeneity from a rat liver postmicrosomal supernatant [1].
• The diminution of PE biosynthesis, however, was paralleled by a depressed activity of CTP:phosphoethanolamine cytidylyltransferase (ET), the pace-setting enzyme of the CDP-ethanolamine pathway [2].
• We have now obtained evidence for the presence in myelin of CTP:phosphoethanolamine cytidylyltransferase, the enzyme catalyzing formation of CDP-ethanolamine [3].
• With regard to the enzymes involved in the synthesis of PtdEtn, the three peroxisome proliferators enhanced the activity of phosphatidylserine (PtdSer) decarboxylase and markedly decreased the activity of CTP:phosphoethanolamine cytidylyltransferase [4].
• The activities of glycerol-3-phosphate acyltransferase, diacylglycerol kinase and PtdSer decarboxylase were significantly increased upon PFOA feeding, whereas the activities of CTP:phosphoethanolamine cytidylyltransferase and PtdEtn N-methyltransferase were decreased [5].

Associations of Pcyt2 with chemical compounds

• CTP:phosphoethanolamine cytidylyltransferase (ET) is a key regulatory enzyme in the CDP-ethanolamine pathway for phosphatidylethanolamine synthesis [6].

Analytical, diagnostic and therapeutic context of Pcyt2

• Surprisingly, the activity of CTP:phosphoethanolamine cytidylyltransferase (EC 2.7.7.14) was virtually unchanged after partial hepatectomy [7].

References