EC Number   |
Subunits |
Reference |
|---|
   3.4.21.83 | ? |
x * 60000, SDS-PAGE |
29788, 663686 |
| 3.4.21.83 | ? |
x * 78000, SDS-PAGE |
717235 |
| 3.4.21.83 | ? |
x * 78000, wild-type enzyme PSP, SDS-PAGE, x * 66000, recombinant truncated enzyme from PSP-Chtr, SDS-PAGE, x * 75000, native enzyme truncated by trypsin treatment, i.e. PSP-Tr, SDS-PAGE |
-, 752738 |
| 3.4.21.83 | ? |
x * 80000, SDS-PAGE under reducing and non-reducing conditions |
668604 |
| 3.4.21.83 | ? |
x * 83400, SDS-PAGE |
755071 |
| 3.4.21.83 | dimer |
2 * 80000, SDS-PAGE |
-, 732683 |
| 3.4.21.83 | homodimer |
2 * 84000, calculated from amino acid sequence |
708953 |
| 3.4.21.83 | monomer |
1 * 58000, SDS-PAGE |
29785 |
| 3.4.21.83 | monomer |
1 * 80000, SDS-PAGE without mercaptoethanol |
29784 |
| 3.4.21.83 | More |
oligopeptidase B is characterized by localization of the catalytic triad (Ser532, Asp617, and His652 in PSP) and also of the substrate binding sites S1 (Glu576 and Asp578) and S2 (Asp460) in the C-terminal catalytic domain, and by an unusual structure of the N-terminal domain: it is a seven-bladed beta-propeller. Such structure allows oligopeptides to penetrate to the catalytic triad localized in the cavity at the interface of two domains and not to admit voluminous molecules of globular proteins to the active center |
-, 752738 |
