PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15225629-0 2004 The selective utilization of substrates in vivo by the phosphatidylethanolamine and phosphatidylcholine biosynthetic enzymes Ept1p and Cpt1p in yeast. Phosphatidylcholines 84-103 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 135-140 15225629-1 2004 In yeast, the aminoalcohol phosphotransferases Ept1p and Cpt1p catalyze the final steps in the CDP-ethanolamine and CDP-choline routes leading to phosphatidylethanolamine (PE) and phosphatidylcholine (PC), respectively. Phosphatidylcholines 180-199 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 57-62 15225629-1 2004 In yeast, the aminoalcohol phosphotransferases Ept1p and Cpt1p catalyze the final steps in the CDP-ethanolamine and CDP-choline routes leading to phosphatidylethanolamine (PE) and phosphatidylcholine (PC), respectively. Phosphatidylcholines 201-203 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 57-62 15225629-3 2004 Analysis of newly synthesized PE and PC using electrospray ionization tandem mass spectrometry revealed that PE and PC produced by Ept1p and Cpt1p have different species compositions, demonstrating that the enzymes consume distinct sets of diacylglycerol species in vivo. Phosphatidylcholines 37-39 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 141-146 15225629-3 2004 Analysis of newly synthesized PE and PC using electrospray ionization tandem mass spectrometry revealed that PE and PC produced by Ept1p and Cpt1p have different species compositions, demonstrating that the enzymes consume distinct sets of diacylglycerol species in vivo. Phosphatidylcholines 116-118 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 141-146 7961735-5 1994 The CPT1 gene product was responsible for 95% of phosphatidylcholine (PC) synthesis via the CDP-choline pathway in vivo. Phosphatidylcholines 49-68 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 4-8 11251067-2 2001 In yeast, diacylglycerol accepts a phosphocholine moiety through a CPT1-derived cholinephosphotransferase activity to directly synthesize phosphatidylcholine. Phosphatidylcholines 138-157 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 67-71 11251067-4 2001 In this study we report that CPT1- and EPT1-derived cholinephosphotransferase activities can significantly overlap in vivo such that EPT1 can contribute to 60% of net phosphatidylcholine synthesis via the Kennedy pathway. Phosphatidylcholines 167-186 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 29-33 8611148-13 1996 Phosphatidylcholine (and its structural analogue sphingomyelin) were the best lipid activators of Cpt1p, the main biologically relevant CPT activity in S. cerevisiae. Phosphatidylcholines 0-19 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 98-103 9642212-2 1998 Mutations (cki1, cct1, and cpt1) in the CDP-choline pathway for phosphatidylcholine synthesis suppress the sec14 growth defect (2), permitting sec14(ts) cki1, sec14(ts) cct1, and sec14(ts) cpt1 strains to grow at the sec14(ts) restrictive temperature. Phosphatidylcholines 64-83 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 27-31 9642212-2 1998 Mutations (cki1, cct1, and cpt1) in the CDP-choline pathway for phosphatidylcholine synthesis suppress the sec14 growth defect (2), permitting sec14(ts) cki1, sec14(ts) cct1, and sec14(ts) cpt1 strains to grow at the sec14(ts) restrictive temperature. Phosphatidylcholines 64-83 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 189-193 7961735-5 1994 The CPT1 gene product was responsible for 95% of phosphatidylcholine (PC) synthesis via the CDP-choline pathway in vivo. Phosphatidylcholines 70-72 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 4-8 7961735-7 1994 Chimeric CPT1/EPT1 enzymes with diacylglycerol and CDP-aminoalcohol specificities both similar and distinct from the parental enzymes were used to determine the specific segments of the CPT1/EPT1 gene products required to restore PC synthesis to cpt- cells in vivo. Phosphatidylcholines 230-232 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 9-13 7961735-7 1994 Chimeric CPT1/EPT1 enzymes with diacylglycerol and CDP-aminoalcohol specificities both similar and distinct from the parental enzymes were used to determine the specific segments of the CPT1/EPT1 gene products required to restore PC synthesis to cpt- cells in vivo. Phosphatidylcholines 230-232 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 186-190 7961735-12 1994 The data also implicate the CPT1 gene product in PC biosynthesis from an endogenous source of choline derived from turnover of PC via the phosphatidylserine-dependent route for PC synthesis. Phosphatidylcholines 49-51 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 28-32 7961735-12 1994 The data also implicate the CPT1 gene product in PC biosynthesis from an endogenous source of choline derived from turnover of PC via the phosphatidylserine-dependent route for PC synthesis. Phosphatidylcholines 127-129 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 28-32 7961735-12 1994 The data also implicate the CPT1 gene product in PC biosynthesis from an endogenous source of choline derived from turnover of PC via the phosphatidylserine-dependent route for PC synthesis. Phosphatidylcholines 127-129 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 28-32 7961445-5 1994 Such an ethanolamine-dependent reduction in bulk membrane PC content was observed for both choline kinase (cki) and choline phosphotransferase (cpt1) mutants, but it was not observed for mutants defective in cholinephosphate cytidylyltransferase, the enzyme that catalyzes the penultimate reaction of the CDP-choline pathway for PC biosynthesis. Phosphatidylcholines 58-60 diacylglycerol cholinephosphotransferase Saccharomyces cerevisiae S288C 144-148