Autoproteolytic cleavage and activation of human acid ceramidase.

@article{Shtraizent2008AutoproteolyticCA,
  title={Autoproteolytic cleavage and activation of human acid ceramidase.},
  author={Nataly Shtraizent and Efrat Eliyahu and Jae-Ho Park and Xingxuan He and Ruth Shalgi and Edward H Schuchman},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 17},
  pages={11253-9}
}
Herein we report the mechanism of human acid ceramidase (AC; N-acylsphingosine deacylase) cleavage and activation. A highly purified, recombinant human AC precursor underwent self-cleavage into alpha and beta subunits, similar to other members of the N-terminal nucleophile hydrolase superfamily. This reaction proceeded with first order kinetics, characteristic of self-cleavage. AC self-cleavage occurred most rapidly at acidic pH, but also at neutral pH. Site-directed mutagenesis and expression… CONTINUE READING
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