Post-translational modification of human brain type I inositol-1,4,5-trisphosphate 5-phosphatase by farnesylation.

@article{Smedt1996PosttranslationalMO,
  title={Post-translational modification of human brain type I inositol-1,4,5-trisphosphate 5-phosphatase by farnesylation.},
  author={Florence De Smedt and Alain Boom and Xavier Pesesse and Serge N. Schiffmann and Christophe Erneux},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 17},
  pages={10419-24}
}
In brain, type I inositol-1,4,5-trisphosphate 5-phosphatase (InsP3 5-phosphatase) is the major isoenzyme hydrolyzing the calcium-mobilizing second messenger InsP3. Activity of this enzyme could be measured in both soluble and particulate fractions of tissue homogenates. The protein sequence showed a putative C-terminal isoprenylation site (CVVQ). In this study, two mutants have been generated. The first mutant (C409S) has a serine replacing a cysteine at position 409 of the wild-type enzyme… CONTINUE READING
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