MVD (mevalonate diphosphate decarboxylase) catalyzes the ATP-dependent decarboxylation of mevalonate diphosphate to isopentenyl diphosphate, a critical step in the mevalonate pathway for isoprenoid and sterol biosynthesis. The enzyme functions as a cytoplasmic homodimer and is essential for downstream cholesterol synthesis and protein prenylation. Inhibition of MVD activity blocks synthesis of prenylated lipids and suppresses cell proliferation in transformed hematopoietic cell lines, with sensitivity correlating to elevated HMG-CoA reductase activity 1. MVD also regulates the crosstalk between cholesterol and fatty acid biosynthesis; inhibition of MVD causes mevalonate diphosphate accumulation, which suppresses fatty acid synthesis in hepatocytes 2. The enzyme was identified as a potential therapeutic target for hypercholesterolemia given its unique role in the cholesterol biosynthetic pathway 3. Pathogenic variants in MVD are associated with rare genetic disorders including porokeratosis, Griscelli syndrome, and microcephaly-albinism-digital anomalies. MVD functions represent a convergence point for regulating lipid homeostasis and cell proliferation, making the enzyme relevant both to metabolic disease and to oncologic contexts where aberrant mevalonate pathway activity drives cell growth.