The enzyme catalyzes the condensation of IMP with aspartate to form adenylosuccinate in the purine salvage pathway, in a reaction accompanied by the hydrolysis of GTP to GDP in the presence of Mg2+ (PMID14729341).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| MG 435 A | MG | magnesium | magnesium | mononuclear | Coordinates substrate Electrostatic stabiliser Increases acidity Increases electrophilicity |
*It refers to the MACiE reference pdb: 1gim
| Metal/s Properties in Resting State | ||||||
| MG 435 A | Resting state enzyme (-) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | unknownGeometry | |||||
| Coordination Number | unknown | |||||
| Notes | - | |||||
| References |
| -Poland BW, Bruns C, Fromm HJ, Honzatko RB Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli. J Biol Chem. 1997 Jun 13;272(24):15200-5.(MEDLINE:9182542) |
| - Some information have been also deduced from the MACiE mechanism model |