Suggested functions for prolyl oligopeptidase: a puzzling paradox.

@article{Brandt2007SuggestedFF,
  title={Suggested functions for prolyl oligopeptidase: a puzzling paradox.},
  author={Inger Brandt and Simon S Scharp{\'e} and A M Lambeir},
  journal={Clinica chimica acta; international journal of clinical chemistry},
  year={2007},
  volume={377 1-2},
  pages={50-61}
}
Prolyl oligopeptidase (PO, E.C. 3.4.21.26) is a post-proline cleaving enzyme with endopeptidase activity towards peptides not longer than 30 amino acids. It has been purified and characterized from various mammalian and bacterial sources, but despite its thorough enzymological and structural characterization, the exact function of PO remains obscure. Many investigations have addressed the physiological role of this enzyme, mainly by the use of specific PO inhibitors, activity measurements in… CONTINUE READING

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