EC Number   |
Metals/Ions |
Reference |
|---|
   3.5.1.88 | Cd2+ |
the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF |
757033 |
| 3.5.1.88 | Co2+ |
- |
675277, 675609, 677015, 699575 |
| 3.5.1.88 | Co2+ |
activates |
758334 |
| 3.5.1.88 | Co2+ |
activates and stabilizes |
756536 |
| 3.5.1.88 | Co2+ |
can replace Fe2+ without loss of activity, enhances stability |
666013, 666015 |
| 3.5.1.88 | Co2+ |
Co2+ is an optimal metal for increasing the activity of purified thioredoxin-fused PDF |
713456 |
| 3.5.1.88 | Co2+ |
Co2+-bound enzyme, highly stable |
393800 |
| 3.5.1.88 | Co2+ |
Co2+-substituted isoform PDF-1 exhibits much higher enzymatic activity than that of Ni2+ and Zn2+ substituted PDF-1 |
712968 |
| 3.5.1.88 | Co2+ |
cobalt-substituted enzyme |
393821 |
| 3.5.1.88 | Co2+ |
enzymatic activity of Escherichia coli PDF is retained after replacement of the active-site Fe2+ ion with Co2+ |
712509 |
