The chemical basis of serine palmitoyltransferase inhibition by myriocin.

@article{Wadsworth2013TheCB,
  title={The chemical basis of serine palmitoyltransferase inhibition by myriocin.},
  author={John M Wadsworth and David J Clarke and Stephen A. McMahon and Jonathan P Lowther and Ashley Emily Beattie and Pat R. R. Langridge-Smith and Howard B. Broughton and Teresa M. Dunn and James H. Naismith and Dominic J. Campopiano},
  journal={Journal of the American Chemical Society},
  year={2013},
  volume={135 38},
  pages={14276-85}
}
Sphingolipids (SLs) are essential components of cellular membranes formed from the condensation of L-serine and a long-chain acyl thioester. This first step is catalyzed by the pyridoxal-5'-phosphate (PLP)-dependent enzyme serine palmitoyltransferase (SPT) which is a promising therapeutic target. The fungal natural product myriocin is a potent inhibitor of SPT and is widely used to block SL biosynthesis despite a lack of a detailed understanding of its molecular mechanism. By combining… CONTINUE READING

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L - Penicillamine is a mechanism - based inhibitor of serine palmitoyltransferase by forming a pyridoxal - 5 ' - phosphate - thiazolidine adduct

J. Lowther, A. E. Beattie, P. R. R. Langridge-Smith, D. J. Clarke, D. J. Campopiano
MedChemComm • 2012

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