EC Number |
Metals/Ions |
Reference |
---|
3.1.4.46 | Ca2+ |
10 mM CaCl2, relative activity: 28.5% |
695040 |
3.1.4.46 | Ca2+ |
4 mM, stimulates |
646457 |
3.1.4.46 | Ca2+ |
a calcium atom is chelated by three conserved residues and a glycerol molecule bound in the catalytic groove |
729721 |
3.1.4.46 | Ca2+ |
optimum activity at 10 mM |
751063 |
3.1.4.46 | Ca2+ |
required |
680514 |
3.1.4.46 | Ca2+ |
required for activity |
729721 |
3.1.4.46 | Co2+ |
activating at 0.05 mM, higly inhibitory above 5 mM |
751853 |
3.1.4.46 | Co2+ |
can replace Mg2+ |
680514 |
3.1.4.46 | Co2+ |
optimum concentration 5 mM |
750858 |
3.1.4.46 | Co2+ |
quantification of binding affinity. Metal ions bind to the six-coordinate alpha site of the protein in an entropically driven process with loss of a proton, while binding at the beta site is not detected. Phosphate enhances the metal affinity of the alpha site by increasing the binding entropy and the metal affinity of the beta site by enthalpic (Co) or entropic (Mn) contributions, but no additional loss of protons |
749914 |