The enzyme catalyzes the decarboxylation and mononucleotide-dependent phosphorylation of oxaloacetate to form phosphoenolpyruvate. To perform the catalytic reaction, it uses a magnesium and another divalent ion, which can be Mn2+,Co2+,Ca2+(PMID9139042).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| MN 543 x | MN | manganese | divalent cation (different per organism) | mononuclear | Coordinates substrate Electrostatic stabiliser Increases electrophilicity |
| MG 544 x | MG | magnesium | magnesium | mononuclear | Coordinates substrate Electrostatic stabiliser Increases electrophilicity |
*It refers to the MACiE reference pdb: 1aq2
| Metal/s Properties in Resting State | ||||||
| MN 543 x | Resting state enzyme (-) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | unknownGeometry | |||||
| Coordination Number | unknown | |||||
| Notes | - | |||||
| MG 544 x | Resting state enzyme (-) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | unknownGeometry | |||||
| Coordination Number | unknown | |||||
| Notes | - | |||||
| References |
| -Matte A, Tari LW, Goldie H, Delbaere LT Structure and mechanism of phosphoenolpyruvate carboxykinase. J Biol Chem. 1997 Mar 28;272(13):8105-8.(MEDLINE:9139042) |
| - Some information have been also deduced from the MACiE mechanism model |