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

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

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1-deoxy-d-xylulose-5-phosphate synthase
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EC no.2.2.1.7
CAS no.202218-79-9
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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.12 The enzyme has been characterised from Escherichia coli1 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 PDB: 2O1S​ and PDB: 2O1X​.

References

References

  1. 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.
  2. 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.
  3. Enzyme 2.2.1.7 at KEGG Pathway Database.