Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone.

@article{Hennig1998SelectiveIO,
  title={Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone.},
  author={Lothar Hennig and C E Christner and Marc Kipping and B Schelbert and Karl Peter Ruecknagel and Susanne Grabley and Gerhard Kuellertz and Gunter Fischer},
  journal={Biochemistry},
  year={1998},
  volume={37 17},
  pages={5953-60}
}
In contrast to FK506 binding proteins and cyclophilins, the parvulin family of peptidyl-prolyl cis/trans isomerases (PPIases; E.C. 5.2.1.8) cannot be inhibited by either FK506 or cyclosporin A. We have found that juglone, 5-hydroxy-1,4-naphthoquinone, irreversibly inhibits the enzymatic activity of several parvulins, like the E. coli parvulin, the yeast Ess1/Ptf1, and human Pin1, in a specific manner, thus allowing selective inactivation of these enzymes in the presence of other PPIases. The… CONTINUE READING

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