The enzyme catalyzes the phosphorylation of nucleoside diphosphates into triphosphates. It is a Mg-dependent enzyme (PMID11277918).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| MG 156 A | MG | magnesium | magnesium | mononuclear | Coordinates substrate Electrostatic stabiliser Increases electrophilicity |
*It refers to the MACiE reference pdb: 1kdn
| Metal/s Properties in Resting State | ||||||
| MG 156 A | Resting state enzyme (-) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | unknownGeometry | |||||
| Coordination Number | unknown | |||||
| Notes | - | |||||
| References |
| -Gallois-Montbrun S, Chen Y, Dutartre H, Sophys M, Morera S, Guerreiro C, Schneider B, Mulard L, Janin J, Veron M, Deville-Bonne D, Canard B Structural analysis of the activation of ribavirin analogs by NDP kinase: comparison with other ribavirin targets. Mol Pharmacol. 2003 Mar;63(3):538-46.(MEDLINE:12606760) |
| -Hutter MC, Helms V The mechanism of phosphorylation of natural nucleosides and anti-HIV analogues by nucleoside diphosphate kinase is independent of their sugar substituents. Chembiochem. 2002 Jul 2;3(7):643-51.(MEDLINE:12324998) |





