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Results 1 - 10 of 22 > >>
EC Number Metals/Ions Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.4Co2+ 10-100 micromol, potent activation 707596
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.4Co2+ 174.4% relative activity at 0.1 mM 699225
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.4Co2+ 516% activity in the presence of 0.1 mM Co2+, 758% activity in the presence of 1 mM Co2+ 668562
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.4Co2+ activation up to 2fold at micromolar concentrations 650445
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.4Co2+ activation up to 50% at 0.001-0.0001 mM, inbhibitory above 0.002 mM 650445
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.4Co2+ increase of activity 36176, 36177, 36178, 36179, 36195, 586911
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.4Co2+ may substitue for Zn2+ 650025
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.4Co2+ significant activation 752887
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.4Cu2+ 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
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.4Cu2+ may substitue for Zn2+ 650025
Results 1 - 10 of 22 > >>