EC Number |
Metals/Ions |
Reference |
---|
3.4.14.4 | Co2+ |
10-100 micromol, potent activation |
707596 |
3.4.14.4 | Co2+ |
174.4% relative activity at 0.1 mM |
699225 |
3.4.14.4 | Co2+ |
516% activity in the presence of 0.1 mM Co2+, 758% activity in the presence of 1 mM Co2+ |
668562 |
3.4.14.4 | Co2+ |
activation up to 2fold at micromolar concentrations |
650445 |
3.4.14.4 | Co2+ |
activation up to 50% at 0.001-0.0001 mM, inbhibitory above 0.002 mM |
650445 |
3.4.14.4 | Co2+ |
increase of activity |
36176, 36177, 36178, 36179, 36195, 586911 |
3.4.14.4 | Co2+ |
may substitue for Zn2+ |
650025 |
3.4.14.4 | Co2+ |
significant activation |
752887 |
3.4.14.4 | Cu2+ |
activity of the cupric derivative for Lys-Ala-beta-naphthylamide is about 30% of that of the wild-type zinc enzyme. The enzyme activity of mutant Cu(II)-del-DPP III, in which Leu453 is deleted from the metal-binding motif, is only 1-2% of the enzyme activity of del-DPP III. The EPR spectra of Cu(II) del-DPP III do not change in the presence of excess Lys-Ala-beta-naphthylamide. The deletion of Leu453 from the HELLGH motif of rat DPP III leads to a complete loss of flexibility in the ligand geometry around the cupric ions |
731219 |
3.4.14.4 | Cu2+ |
may substitue for Zn2+ |
650025 |