The enzyme catalyzes the reversible transphosphorylation between N-phospho-L-arginine and ATP thus buffering cellular ATP levels. It uses divalent cations for activity, such as Mg2+ and Mn2+ (PMID16712519).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| MG 402 x | MG | magnesium | magnesium/manganese | mononuclear | Coordinates substrate Electrostatic stabiliser Increases electrophilicity |
*It refers to the MACiE reference pdb: 1bg0
| Metal/s Properties in Resting State | ||||||
| MG 402 x | Resting state enzyme (-) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | unknownGeometry | |||||
| Coordination Number | unknown | |||||
| Notes | - | |||||
| References |
| -Zhou G, Somasundaram T, Blanc E, Parthasarathy G, Ellington WR, Chapman MS Transition state structure of arginine kinase: implications for catalysis of bimolecular reactions. Proc Natl Acad Sci U S A. 1998 Jul 21;95(15):8449-54.(MEDLINE:9671698) |
| - Some information have been also deduced from the MACiE mechanism model |