EC Number   |
Metals/Ions |
Reference |
|---|
    1.2.1.39 | Ca2+ |
1 mM stimulates by 53% |
690567 |
| 1.2.1.39 | Cs+ |
monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order |
390292 |
| 1.2.1.39 | K+ |
monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order |
390292 |
| 1.2.1.39 | Li+ |
monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order |
390292 |
| 1.2.1.39 | Mg2+ |
1 mM stimulates by 42% |
690567 |
| 1.2.1.39 | Mg2+ |
the enzyme includes both an activating and inhibitory metal binding site in the catalytic mechanism of NPADH. The activating divalent metal binding site may be best described as the direct interaction of the metal ion with the pyrophosphate linkage joining the nicotinamide mononucleotide and adenosine mononucleotide components of the pyridine nucleotide structure. A second mononuclear metal binding site, occupied by Mg2+ is detected in this structure. The Mg2+ in this site assumes a roughly octahedral geometry and is coordinated by the backbone carbonyl oxygens of Val40, Asp109, Glu196, and Val345, as well as a monodentate interaction with a carboxylate oxygen of Asp109. The sixth ligand is a crystallographically resolved water molecule |
741787 |
| 1.2.1.39 | Mn2+ |
1 mM stimulates by 17% |
690567 |
| 1.2.1.39 | Mn2+ |
inhibits and activates |
741787 |
| 1.2.1.39 | more |
divalent cations (Mg2+, Ca2+) are inactive |
390292 |
| 1.2.1.39 | more |
is not stimulated by 10 mM KCl |
690567 |
