EC Number   |
Subunits |
Reference |
|---|
   3.4.14.10 | ? |
- |
647141, 647143 |
| 3.4.14.10 | ? |
x * 100000-140000, SDS-PAGE of recombinant protein, full-length TPP II and shortened versions thereof |
731331 |
| 3.4.14.10 | ? |
x * 135000, SDS-PAGE under reducing conditions |
647141, 647142, 647143 |
| 3.4.14.10 | ? |
x * 138000, the subunits form an active complex with a MW of 1000000 Da, the complex can sponateously dissociate in vitro into dimers which retain 1/10th of the original specific activity. The dissociated enzyme can reassociate at elevated temperatures, provided the protein concentration is sufficiently high. This reassociation is accompanied by a reactivation |
647152 |
| 3.4.14.10 | ? |
x * 38000, recombinant enzyme, SDS-PAGE |
-, 752530 |
| 3.4.14.10 | More |
compared with other subtilases, TPP II has a 200 amino-acid insertion between the catalytic Asp44 and His264 residues and is active as an oligomeric complex. The insert is important for the formation of the active high-molecular mass complex |
647153 |
| 3.4.14.10 | More |
conformation of the native complex, transmission electron microscopy, the complex dissociates into MW 270000 dimers upon dialysis against Tris-HCl buffer |
647150 |
| 3.4.14.10 | More |
enzyme from an alternatively spliced cDNA variant contains an additional 39 bp, encoding 13 amino acids in the C-terminal end of the protein forms a larger complex. The C-terminal 13 amino acids are important for aggregation of subunits |
647154 |
| 3.4.14.10 | More |
enzyme N-terminal peptide mapping |
-, 752530 |
| 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 |
666724 |
