Mevalonate diphosphate decarboxylase (MVD)

Mevalonate diphosphate decarboxylase (MVD) is an ATP-dependent enzyme catalyzing the decarboxylation and dehydration of mevalonate 5-diphosphate (MVAPP) to produce isopentenyl diphosphate (IPP), a critical five-carbon building block for all isoprenoids, including cholesterol, ubiquinone, and heme A[1][3][6]. MVD is the final enzyme in the classical mevalonate pathway and belongs to the GHMP kinase superfamily[1]. It acts as a metabolic gatekeeper, with loss or mutation causing severe metabolic or developmental consequences including inherited skin disorders and metabolic deficiencies[5]. It is studied in the context of metabolic engineering, drug development (especially cholesterol biosynthesis), and genetic disease. No approved drugs currently target MVD directly, but it is recognized as potentially “rate-limiting” within the pathway, making it a subject of ongoing research[4][6].

Other names

Diphosphomevalonate decarboxylaseMVDMPDMDDaseMevalonate (diphospho) decarboxylaseMevalonate pyrophosphate decarboxylaseFP17780POROK7

ATP-dependent decarboxylation and dehydration of mevalonate 5-diphosphate to isopentenyl diphosphate Drugs/inhibitors act by blocking substrate binding or catalytic activity, thereby modulating isoprenoid/cholesterol biosynthesis