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Çѱ¹½Ä¹°ÇÐȸ / v.38, no.4, 1995³â, pp.359-364

( Partial Characterization of Soybean cDNA Encoding CTP: Phosphocholine Cytidylyltransferase )
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As the first step to elucidate the relationship between the structure and function of CTP:phosphocholine cytidylyltransferase (EC 2.7.7.15) in plants, the partial nucleotide sequence of soybean cytidylyltransferase cDNA was determined using a polymerase chain reaction (PCR). Degenerate oligonucleotide primers were synthesized from the conserved region revealed from the rat and yeast cytidylyltransferase DNA sequences. The catalytic domain region showed 78 and 76% homology with the rat and yeast amino acid sequences, respectivly. The hydropathy profile indicated that the C-terminal non-catalytic portion of the protein was very hydrophilic, and in the region between the catalytic domain and the C-terminal region, there was a large amphipathic $alpha$-helical domain that was believed to bind the membrane surface in the active formation. There are 7 potential sites for phosphorylation by protein kinase C and 4 potential sites for phosphorylation by Ca2+/calmodulin kinase within the determined sequence.
 
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soybean;CTP;phosphochocholine cytidylyltransferase;phosphatidylcholine;amphipathic helix;
 
Journal of Plant Biology / v.38, no.4, 1995³â, pp.359-364
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ISSN : 1226-9239
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO199511920117485)
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