EC Number |
Metals/Ions |
Reference |
---|
3.5.4.19 | Cd2+ |
0.95 Cd2+ per enzyme subunit, competes with and replaces Zn2+, binding affects the enzyme structure, three Cd2+ are coordinated by residues Asp85 and Cys86 from one monomer and Cys109 from the other monomer, the fourth Cd2+ is bound by His16 and Asp89 |
667617 |
3.5.4.19 | Mg2+ |
required for cataltic activity. The C93 reactivity is modulated by the presence of the Zn2+ and Mg2+ and substantiates the role of this residue as a metal ligand |
726992 |
3.5.4.19 | Zn2+ |
a single tightly bound Zn2+ per subunit |
246720 |
3.5.4.19 | Zn2+ |
metalloprotein. The Zn2+ coordination site involves the three conserved cysteine residues. The C93 reactivity is modulated by the presence of the Zn2+ and Mg2+ and substantiates the role of this residue as a metal ligand |
726992 |
3.5.4.19 | Zn2+ |
required for activity, zinc-metalloenzyme |
667617 |