The enzyme catalyzes the convertion of phosphoenolpyruvate to phosphonopyruvate. It is a tetramer and requires magnesium ions to perform the reaction mechanism (PMID10378273).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| MG 1003 A | MG | magnesium | magnesium | mononuclear | Electrostatic stabiliser Coordinates substrate Promotes heterolysis |
*It refers to the MACiE reference pdb: 1pym
| Metal/s Properties in Resting State | ||||||
| MG 1003 A | Resting state enzyme (1s2v) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | octahedral | |||||
| Coordination Number | 6 | |||||
| Notes | - | |||||
| References |
| -Lu Z, Jia Y, Dunaway-Mariano D, Herzberg O Dissociative phosphoryl transfer in PEP mutase catalysis: structure of the enzyme/sulfopyruvate complex and kinetic properties of mutants. Biochemistry. 2002 Aug 13;41(32):10270-6.(MEDLINE:12162742) |
| -Li Z, Jia Y, Dunaway-Mariano D, Herzberg O Helix swapping between two alpha/beta barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg(2+)-oxalate. Structure. 1999 May;7(5):539-48.(MEDLINE:10378273) |