EC Number   |
Metals/Ions |
Reference |
|---|
   4.1.1.64 | Ba2+ |
gives 10fold lower activity compared to monovalent alkali cations of similar ionic radius, increases association of pyridoxal 5'-phosphate and decreases dissociation rate constant of pyridoxal 5'-phosphate |
661129 |
| 4.1.1.64 | Ca2+ |
gives 10fold lower activity compared to monovalent alkali cations of similar ionic radius |
661129 |
| 4.1.1.64 | Cs+ |
activates to a lesser extent than K+ |
661129 |
| 4.1.1.64 | K+ |
activates |
4752, 4753, 664227 |
| 4.1.1.64 | K+ |
activity is dependent on cations. K+ is the monovalent cation with the optimal size for catalytic activity, increases association of pyridoxal 5'-phosphate and decreases dissociation rate constant of pyridoxal 5'-phosphate |
661129 |
| 4.1.1.64 | K+ |
the K+-activated enzyme in solution exists in two conformations differing in catalytic competence |
4753 |
| 4.1.1.64 | Li+ |
activates to a lesser extent than K+ |
661129 |
| 4.1.1.64 | Mg2+ |
gives 10fold lower activity compared to monovalent alkali cations of similar ionic radius |
661129 |
| 4.1.1.64 | more |
a binding site for alkali metal ions is close to the active site. Exchange of K+ for Na+ at this site is shown to affect the conformation of two active site residues |
4752 |
| 4.1.1.64 | more |
hysteretic enzyme whose conformational distribution is controlled by the identity of the alkali metal ion bound near the active site |
4753 |
