EC Number   |
Metals/Ions |
Reference |
|---|
   3.2.1.143 | KCl |
100 mM, slight activation |
208525 |
| 3.2.1.143 | KCl |
50 mM, 1.4-1.5fold stimulation |
208526 |
| 3.2.1.143 | KCl |
50-100 mM, stimulates |
208530 |
| 3.2.1.143 | KCl |
50-100 mM, stimulates poly(ADP-ribose) glycohydrolase I |
208517 |
| 3.2.1.143 | Mg2+ |
required for activity, two MG2+ with catalytic function, mechanism, overview. Asp314 is essential for the formation of the binuclear metal center |
754165 |
| 3.2.1.143 | Mg2+ |
required for catalysis, binuclear Mg2+ site, structure overview. The distal ribose of poly(ADP-ribose), enabling the hydroxyl groups of the distal ribose to coordinate the two Mg2+ ions. MgA is coordinated with Asp314, Asp316, Thr317, three hydroxyl groups of the distal ribose and water 269. Meanwhile, MgB is coordinated with the 2'-hydroxyl group of the distal ribose, Thr76, Asp77, Asp78, Asp316, and two water molecules (water 269 and water 85). The sequence alignment and structural comparison reveals that the Mg2+ coordinating acidic residues Asp77, Asp78, Asp314, and Asp316 are fully conserved in homologous ARH enzymes. Both Mg2+ ions are involved in the positioning of water 351 in the catalytic center through hydrogen-bonding interaction. the binding pocket of ARH3 is divided into two subunits by the binuclear Mg2+ sites |
754168 |
| 3.2.1.143 | Mg2+ |
required for hydrolysis of O-acetyl-ADP-ribose |
682516 |
| 3.2.1.143 | MgCl2 |
10 mM, activation |
665741 |
| 3.2.1.143 | NaCl |
100 mM, slight activation |
208525 |
| 3.2.1.143 | NaCl |
50 mM, 1.4-1.5fold stimulation |
208526 |
