Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | contains one Ca2+ ion per subunit of native enzyme. Treatment with trans-l,2-diaminocyclohexane-N,N,N',N'-tetraacetic acid at 30°C leads to an catalytically inactive apo-form. Upon incubation of the apo-form with Ca2 + and pyrroloquinoline quinone a fully active holo-enzyme is reconstituted. Incubation of apo-enzyme with Sr2+ and pyrroloquinoline quinone leads to the formation of an active Sr2+-form. The Sr2+ and the Ca2+-forms of the enzyme differ in their absorption spectra. | Pseudomonas aeruginosa | |
Sr2+ | incubation of apo-enzyme with Sr2+ and pyrroloquinoline quinone leads to the formation of an active Sr2+-form. The Sr2+ and the Ca2+-forms of the enzyme differ in their absorption spectra. The Sr2+-form is inactivated by trans-l,2-diaminocyclohexane-N,N,N',N'-tetraacetic acid twice as fast as the Ca2+-form. | Pseudomonas aeruginosa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas aeruginosa | - |
- |
- |
Renatured (Comment) | Organism |
---|---|
treatment with trans-l,2-diaminocyclohexane-N,N,N',N'-tetraacetic acid at 30°C leads to an catalytically inactive apo-form. Upon incubation of the apo-form with Ca2+ and pyrroloquinoline quinone a fully active holo-enzyme is reconstituted. Incubation of apo-enzyme with Sr2+ and pyrroloquinoline quinone leads to the formation of an active Sr2+-form. The Sr2+ and the Ca2+-forms of the enzyme differ in their absorption spectra. | Pseudomonas aeruginosa |