Mevalonate Decarboxylase (MVD)

The enzyme mevalonate pyrophosphate decarboxylase (MVD, EC 4.1.1.33) catalyzes the conversion of mevalonate pyrophosphate into isopentenyl pyrophosphate. This unusual enzyme decarboxylates and dehydrates its substrate while hydrolyzing ATP. As a unique enzyme in one of the early steps in cholesterol biosynthesis, MVD may be a useful target for drugs aimed at lowering serum cholesterol levels.

Toth and Huwyler (1996) cloned the human MVD gene from a liver cDNA library. The cDNA encoded a 400-amino acid polypeptide. Northern blot analysis revealed a 2-kb mRNA present at similar levels in various human tissues. Expression studies indicated that the recombinant human enzyme is active as a 43-kD homodimer.