Diphosphomevalonate decarboxylase
![Proposed mechanism for human mevalonate diphosphate decarboxylase. Amino acid residues colored to correspond to crystal structure image of active site residues. ATP is brown to show phosphoryl transfer.[1]](/uploads/202501/09/Mechanism_for_Mevalonate_Diphosphate_Decarboxylase4952.jpg)
![Crystal structure of the active cite of human mevalonate diphosphate decarboxylase, generated from 3D4J. Proposed important residues for mechanism and substrate binding are highlighted: Arg-161 (green), Ser-127 (blue), Asp-305 (orange), and Asn-17 (red). Sulfate ion aided in better understanding the substrate binding. Mevalonate diphosphate is proposed to be positioned so the terminal phosphate is near the sulfate ion in the crystal structure.[1]](/uploads/202501/09/Important_residues_of_active_site_of_mevalonate_diphosphate_decarboxylase4952.png)
Diphosphomevalonate decarboxylase (EC4.1.1.33), most commonly referred to in scientific literature as mevalonate diphosphate decarboxylase, is an enzyme that catalyzes the chemical reaction
This enzyme converts mevalonate 5-diphosphate (MVAPP) to isopentenyl diphosphate (IPP) through ATP dependent decarboxylation. The two substrates of this enzyme are ATP and mevalonate 5-diphosphate, whereas its 4 products are ADP, phosphate, isopentenyl diphosphate, and CO2.