2.7.7.15	drug target	CTP:phosphocholine cytidylyltransferase beta3 (CCTbeta3) may be targeted to suppress prolonged autophagy in cancer cells in vivo	761981	
2.7.7.15	evolution	the conformational malleability of the x02E helix pair that bridges the membrane binding and catalytic domains of the enzyme makes it an ideal element adapted by evolution for transducing signals from membrane to active site	761489	
2.7.7.15	evolution	the enzyme is a member of the cytidylyltransferase family of enzymes that utilize cytidine 5'-triphosphate (CTP) to synthesize molecules that are typically precursors to membrane phospholipids	737438	
2.7.7.15	malfunction	acute prelamin A accumulation after reduction of the activity of the ZMPSTE24 endoprotease by siRNA knockdown, results in the generation of a complex nucleoplasmic reticulum that depends for its formation on the CTP:phosphocholinecytidylyltransferase-a, this structure can form during interphase, confirming that it is independent of mitosis and therefore not a consequence of disordered nuclear envelope assembly	722861	
2.7.7.15	malfunction	isozyme CTbeta2 deficiency in distal axons reduces the incorporation of choline into by 95% whereas phosphatidylcholine synthesis in cell bodies/proximal axons is unaltered. Brains of mice lacking CTbeta2 have normal phosphatidylethanolamine content despite having 35% lower enzyme activity than wild-type brains. Axon branching, but not axon extension, is impaired in CTbeta2-deficient neurons. Phenotypes, overview	-, 721714	
2.7.7.15	malfunction	mutations in the gene encoding CTP:phosphocholine cytidylyltransferase (PCYT1A) cause three distinct pathologies in humans: lipodystrophy, spondylometaphyseal dysplasia with cone-rod dystrophy (SMD-CRD), and isolated retinal dystrophy	761500	
2.7.7.15	malfunction	without cholinephosphate cytidylyltransferase (CPCT), Leishmania major parasites cannot incorporate choline into phosphatidylcholine, yet the CPCT-null mutants contain similar levels of phosphatidylcholine and phosphatidylethanolamine as wild type parasites. Loss of CPCT does not affect the growth of parasites in complete medium or their virulence in mice. The results suggest that other mechanisms of phosphatidylcholine synthesis can compensate the loss of CPCT. CPCT-null parasites exhibit severe growth defects when ethanolamine and exogenous lipids became limited or when they are co-cultured with certain bacteria that are known to be members of sandfly midgut microbiota	762463	
2.7.7.15	metabolism	CTP:phosphocholine cytidylyltransferase is the key regulatory enzyme in phosphatidylcholine synthesis	761500	
2.7.7.15	metabolism	key enzyme in phosphatidylcholine synthesis	761489	
2.7.7.15	metabolism	rate limiting step of the de novo phosphatidylcholine biosynthesis is catalysed by CTP:phosphocholine cytidylyltransferase, which has a key regulatory function within the pathway	762404