EC Number |
Metals/Ions |
Reference |
---|
2.7.1.232 | Mg2+ |
10 mM used in assay conditions |
761642 |
2.7.1.232 | Mg2+ |
required |
738262, 738435, 738937, 739585, 739710 |
2.7.1.232 | Mg2+ |
required, the enzyme binds two magnesium ions in the active site, four manganese atoms in the dimeric structure, that are additionally coordinated with the nucleotide and water molecules to result in ideal octahedral coordination. The magnesium ions are observed in ideal octahedral coordination with Glu362 and Asp26, several water molecules, and the ADP, overview. The first of the bound metals, designated M1, forms an electrostatic interaction with the beta-phosphate, and its positioning suggests that it plays a direct role in phosphoryl transfer. The second of these metals, designated M2, likely plays a role in coordinating the position of the alpha- and beta-phosphates because it binds to both of these phosphates, whereas a role in modulation of electrostatic charges is also plausible |
738664 |
2.7.1.232 | Mg2+ |
the enzyme contains two Mg2+ ions. Using 4 and 8 mM Mg2+, the activity is highest at a Mg2+/ATP ratio of 2 and drastically drops if the ratio is less than 1. Employing a constant ATP concentration (2.5 mM), the enzyme activity increases with the Mg2+ concentration until a Mg2+/ATP ratio of 8 is reached at 20 mM MgCl2 |
760884 |
2.7.1.232 | Mg2+ |
the enzyme requires Mg2+ or Mn2+, apparent binding of two magnesium ions in the active site showing ideal octahedral binding of the metals. The first of the bound metals, designated M1, forms an electrostatic interaction with the beta-phosphate, and its positioning suggests that it plays a direct role in phosphoryl transfer. The second of these metals, designated M2, likely plays a key role in coordinating the position of the alpha- and beta-phosphates since it binds to both of these phosphates, although a role in modulation of electrostatic charges is also plausible |
738435 |
2.7.1.232 | Mn2+ |
the enzyme requires Mg2+ or Mn2+, apparent binding of two magnesium ions in the active site showing ideal octahedral binding of the metals. The first of the bound metals, designated M1, forms an electrostatic interaction with the beta-phosphate, and its positioning suggests that it plays a direct role in phosphoryl transfer. The second of these metals, designated M2, likely plays a key role in coordinating the position of the alpha- and beta-phosphates since it binds to both of these phosphates, although a role in modulation of electrostatic charges is also plausible |
738435 |