1-deoxy-d-xylulose-5-phosphate synthase (EC 2.2.1.7) 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.[1][2] The enzyme has been characterised from Escherichia coli[1] and a Streptomyces species.[2]
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:d-glyceraldehyde-3-phosphate acetaldehydetransferase (decarboxylating). Other names in common use include 1-deoxy-d-xylulose-5-phosphate pyruvate-lyase (carboxylating), and DXP-synthase.[3] The product of the enzyme goes on to form isopentenyl pyrophosphate which is part of the biosynthesis of steroids,[2] and other compounds such as pyridoxol.[1]
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2O1S and 2O1X.
References
- ^ a b c Sprenger GA, Schörken U, Wiegert T, Grolle S, de Graaf AA, Taylor SV, et al. (November 1997). “Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol”. Proceedings of the National Academy of Sciences of the United States of America. 94 (24): 12857–12862. doi:10.1073/pnas.94.24.12857. PMC 24228. PMID 9371765.
- ^ a b c Kuzuyama T, Takagi M, Takahashi S, Seto H (February 2000). “Cloning and characterization of 1-deoxy-D-xylulose 5-phosphate synthase from Streptomyces sp. Strain CL190, which uses both the mevalonate and nonmevalonate pathways for isopentenyl diphosphate biosynthesis”. Journal of Bacteriology. 182 (4): 891–897. doi:10.1128/JB.182.4.891-897.2000. PMC 94361. PMID 10648511.
- ^ Enzyme 2.2.1.7 at KEGG Pathway Database.
