EC Number   |
Reaction |
Reference |
|---|
    2.7.4.2 | ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate |
kinetic mechanism, the enzyme follows hyperbolic kinetics and a sequential mechanism |
671609 |
| 2.7.4.2 | ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate |
ordered mechanism |
645174 |
| 2.7.4.2 | ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate |
residue R110 is important to PMK catalysis, which is also influenced by K48 and R73. R111 and R84 contribute to binding of mevalonate 5-phosphate and R141 to binding of ATP |
672221 |
| 2.7.4.2 | ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate |
residue R22 is important for catalysis |
672134 |
| 2.7.4.2 | ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate |
sequential mechanism |
645177 |
| 2.7.4.2 | ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate |
the phosphorylation reaction mechanism of phosphomevalonate kinase is studied by using molecular dynamics and hybrid QM/MM methods, overview. A conserved residue (Ser106) is reorientated to anchor ATP via a stable H-bond interaction. In addition, Ser213 located on the alpha-helix at the catalytic site is repositioned to further approach the substrate, facilitating the proton transfer during the phosphorylation. Lys101 functions to neutralize the negative charge developed at the beta-, gamma-bridging oxygen atom of ATP during phosphoryl transfer |
759656 |
