1-deoxy-D-xylulose-5-phosphate synthase
| 1-deoxy-d-xylulose-5-phosphate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.2.1.7 | ||||||||
| CAS no. | 202218-79-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a 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
- 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. Bibcode:1997PNAS...9412857S. doi:10.1073/pnas.94.24.12857. PMC 24228. 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. PMC 94361. PMID 10648511.
