1-deoxy-D-xylulose-5-phosphate synthase

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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 $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2O1S and 2O1X.

[edit] References

IUBMB entry for 2.2.1.7
BRENDA references for 2.2.1.7 (Recommended.)
PubMed references for 2.2.1.7
PubMed Central references for 2.2.1.7
Google Scholar references for 2.2.1.7
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: 12857–62. 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: 891–7. PMID 10648511.