Phosphomevalonate Kinase (PMVK)

PMVK (EC 2.7.4.2) is a peroxisomal enzyme that catalyzes the conversion of mevalonate 5-phosphate into mevalonate 5-diphosphate as the fifth reaction of the cholesterol biosynthetic pathway. The deduced 192-amino acid PMVK protein has a calculated molecular mass of about 22 kD. It contains a C-terminal peroxisomal targeting sequence, and a single methionine is removed from the N terminus upon maturation of the protein. Expression was highest in heart and skeletal muscle, with slightly lower levels in liver, kidney, and pancreas, and low but detectable levels in brain, lung, and placenta.Analysis of transcripts from human lymphoblasts subcultured in lipid-depleted sera (LDS) and LDS supplement with lovastatin indicated that PMVK expression is subject to regulation by sterol at the level of transcription.