Diphosphomevalonate decarboxylase

In enzymology, a diphosphomevalonate decarboxylase is an enzyme that catalyzes the chemical reaction


 * ATP + (R)-5-diphosphomevalonate $$\rightleftharpoons$$ ADP + phosphate + isopentenyl diphosphate + CO2

Thus, the two substrates of this enzyme are ATP and (R)-5-diphosphomevalonate, whereas its 4 products are ADP, phosphate, isopentenyl diphosphate, and CO2.

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is ATP:(R)-5-diphosphomevalonate carboxy-lyase (adding ATP isopentenyl-diphosphate-forming). Other names in common use include pyrophosphomevalonate decarboxylase, mevalonate-5-pyrophosphate decarboxylase, pyrophosphomevalonic acid decarboxylase, 5-pyrophosphomevalonate decarboxylase, mevalonate 5-diphosphate decarboxylase, and ATP:(R)-5-diphosphomevalonate carboxy-lyase (dehydrating). This enzyme participates in biosynthesis of steroids.

Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes, , , and.