1-deoxy--xylulose-5-phosphate synthase () is an enzyme in the non-mevalonate pathway that catalyzes the chemical reaction

The two substrates of this enzyme are pyruvic acid and D-glyceraldehyde 3-phosphate. Its products are 1-deoxy-D-xylulose 5-phosphate and carbon dioxide. The enzyme has been characterised from Escherichia coli and a Streptomyces species.

It belongs to the family of transferases, specifically those transferring aldehyde or ketonic groups (transaldolases and transketolases, respectively). The systematic name of this enzyme class is pyruvate:-glyceraldehyde-3-phosphate acetaldehydetransferase (decarboxylating). Other names in common use include 1-deoxy--xylulose-5-phosphate pyruvate-lyase (carboxylating), and DXP-synthase. The product of the enzyme goes on to form isopentenyl pyrophosphate which is part of the biosynthesis of steroids, and other compounds such as pyridoxol.

Structural studies

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

References