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