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1-deoxy-D-xylulose-5-phosphate synthase Identifiers EC number 2.2.1.7 CAS number 202218-79-9 Databases IntEnz IntEnz view BRENDA BRENDA entry ExPASy NiceZyme view KEGG KEGG entry MetaCyc metabolic pathway PRIAM profile PDB structures Gene Ontology AmiGO / EGO Search PMC articles PubMed articles In enzymology, a 1-deoxy-D-xylulose-5-phosphate synthase (EC 2.2.1.7) is an enzyme that catalyzes the chemical reaction pyruvate + D-glyceraldehyde 3-phosphate 1-deoxy-D-xylulose 5-phosphate + CO2 Thus, the two substrates of this enzyme are pyruvate and D-glyceraldehyde 3-phosphate, whereas its two products are 1-deoxy-D-xylulose 5-phosphate and CO2. This enzyme 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. This enzyme participates in biosynthesis of steroids. Structural studies As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2O1S and 2O1X. References SV, Begley TP, Bringer-Meyer S, Sahm H (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". Proc. Natl. Acad. Sci. U. S. A. 94 (24): 12857–62. doi:10.1073/pnas.94.24.12857. PMID 9371765.  Kuzuyama T, Takagi M, Takahashi S, Seto H (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". J. Bacteriol. 182 (4): 891–7. doi:10.1128/JB.182.4.891-897.2000. PMID 10648511.  This transferase article is a stub. You can help Wikipedia by expanding it. v • d • e