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Literature summary extracted from

  • Rockel, B.; Peters, J.; Mueller, S.A.; Seyit, G.; Ringler, P.; Hegerl, R.; Glaeser, R.M.; Baumeister, W.
    Molecular architecture and assembly mechanism of Drosophila tripeptidyl peptidase II (2005), Proc. Natl. Acad. Sci. USA, 102, 10135-10140.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
3.4.14.10 Drosophila sp. (in: flies)
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.14.10 embryo
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Drosophila sp. (in: flies)
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Subunits

EC Number Subunits Comment Organism
3.4.14.10 More the 150000 Da subunits of Drosophila TPPII assemble into a giant proteolytic complex of 6 MDa, consisting of two segmented and twisted strands that form a spindle-shaped structure. The building blocks of this complex are apparently dimers, within which the 150-kDa monomers are oriented head to head. Stacking of these dimers leads to the formation of twisted single strands, two of which comprise the fully assembled spindle. This spindle also forms when TPPII is heterologously expressed in Escherichia coli, demonstrating that no scaffolding protein is required for complex formation and length determination Drosophila sp. (in: flies)

Synonyms

EC Number Synonyms Comment Organism
3.4.14.10 TPPII
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Drosophila sp. (in: flies)