EC Number   |
Subunits |
Reference |
|---|
   3.4.22.59 | ? |
x * 15000, cleaved enzyme, SDS-PAGE |
731574 |
| 3.4.22.59 | ? |
x * 32000, pro-enzyme, SDS-PAGE |
732370 |
| 3.4.22.59 | ? |
x * 34000, pro-Casp6a, SDS-PAGE, x * 23000, pro-Casp6b, SDS-PAGE |
717804 |
| 3.4.22.59 | ? |
x * 35000, Western blot analysis, small subunit (15000) resulting from cleavage at Asp194 |
703561 |
| 3.4.22.59 | ? |
x * about 30000, caspase-6 with a 23-amino-acid deletion in the pro-domain, SDS-PAGE |
732330 |
| 3.4.22.59 | dimer |
2 * 34000, isozyme pro-caspase-6alpha, SDS-PAGE |
718437 |
| 3.4.22.59 | dimer |
procaspase 6, SDS-PAGE, chemical cross-linking and gel filtration, nearly identical CD spectra of rCaspase 6 and D316A caspase 6, indicating that overal structures of both precursor and mature forms of caspase 6 should be almost indistinguishable |
667462 |
| 3.4.22.59 | homodimer |
2 * 32183.5, mass spectrometry, dimer: 63070, multi-angle light scattering, 58000, ultracentrifugation, after proteolytic maturation each subunit of the active enzyme is a two-chain molecule consisting of the p18 (19668.1 Da, residues 24-179) and p11 (12563.5 Da, residues 194-293), mass spectrometry |
707434 |
| 3.4.22.59 | More |
activation by proteolytic self-cleavage, during activation, the N-terminal prodomain is removed by cleavage at a TETD site. Double cleavage in an unstructured linker region at a DVVD and a TEVD site gives rise to a large 20-kDa and a small 10-kDa subunit. The two large p20 and two small p10 subunits then assemble to form the active CASP6 complex |
718437 |
| 3.4.22.59 | More |
active canonical conformation of the apoenzyme apo-caspase-6, comparison to the apostructure of pH-inactivated caspase-6,crystal structure analysis, overview. Caspase-6 subunits p20 and p10 comprise residues 24179 and 194293, respectively |
717997 |
