Identification of an 11-residue portion of CTP-phosphocholine cytidylyltransferase that is required for enzyme-membrane interactions.

@article{Yang1997IdentificationOA,
  title={Identification of an 11-residue portion of CTP-phosphocholine cytidylyltransferase that is required for enzyme-membrane interactions.},
  author={Jianmin Yang and Jianwei Wang and Irene Tseu and Maciek Kuliszewski and W Lee and Martin Post},
  journal={The Biochemical journal},
  year={1997},
  volume={325 ( Pt 1)},
  pages={29-38}
}
CTP-phosphocholine cytidylyltransferase (CT) is a key regulatory enzyme in the biosynthesis of phosphatidylcholine (PC) in many cells. Enzyme-membrane interactions appear to play an important role in CT activation. A putative membrane-binding domain appears to be located between residues 236 and 293 from the N-terminus. To map the membrane-binding domain more precisely, glutathione S-transferase fusion proteins were prepared that contained deletions of various domains in this putative lipid… CONTINUE READING

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