A giant protease with potential to substitute for some functions of the proteasome.

@article{Geier1999AGP,
  title={A giant protease with potential to substitute for some functions of the proteasome.},
  author={E. Geier and G. Pfeifer and M. Wilm and M. Lucchiari-Hartz and W. Baumeister and K. Eichmann and G. Niedermann},
  journal={Science},
  year={1999},
  volume={283 5404},
  pages={
          978-81
        }
}
An alanyl-alanyl-phenylalanyl-7-amino-4-methylcoumarin-hydrolyzing protease particle copurifying with 26S proteasomes was isolated and identified as tripeptidyl peptidase II (TPPII), a cytosolic subtilisin-like peptidase of unknown function. The particle is larger than the 26S proteasome and has a rod-shaped, dynamic supramolecular structure. TPPII exhibits enhanced activity in proteasome inhibitor-adapted cells and degrades polypeptides by exo- as well as predominantly trypsin-like… Expand
Integration of the ubiquitin-proteasome pathway with a cytosolic oligopeptidase activity.
  • E. W. Wang, B. Kessler, +4 authors R. Glas
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 2000
A tale of two giant proteases.
Tripeptidyl Peptidase II. An Oligomeric Protease Complex from Arabidopsis1
Catalytic activities of the 20 S proteasome, a multicatalytic proteinase complex.
Purification of the Arabidopsis 26 S Proteasome
Characterization of the endopeptidase activity of tripeptidyl-peptidase II.
Structure and function of tripeptidyl peptidase II, a giant cytosolic protease.
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