Skip to main content

  | मौसम…

411 समाचार
Public archive edition · Attributed source reporting with original dates · AI drafts are excluded

411 REFERENCE · Wikipedia

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

Reference material by Wikipedia contributors. This retains its source identity and is not 411 news reporting.

Class of enzymes vanc 6 {{DISPLAYTITLE:1-deoxy-D-xylulose-5-phosphate synthase}} 1-deoxy-d-xylulose-5-phosphate synthase 2.2.1.7 202218-79-9 0008661 1-deoxy-d-xylulose-5-phosphate synthase (2.2.1.7) is an enzyme in the non-mevalonate pathway that catalyzes the chemical reaction 70% Pyruvic acid 0.6 + Q26992303 D-glyceraldehyde-3-phosphate CO2 1-Deoxy-D-xylulose 5-phosphate 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. Sprenger GA, Schörken U, Wiegert T, Grolle S, de Graaf AA, Taylor SV, Begley TP, Bringer-Meyer S, Sahm H 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 November 1997 9371765 10.1073/pnas.94.24.12857 free 24228 Kuzuyama T, Takagi M, Takahashi S, Seto H 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 February 2000 10648511 10.1128/JB.182.4.891-897.2000 94361 The enzyme has been characterised from Escherichia coli and a Streptomyces species. 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.2.2.1.7 The product of the enzyme goes on to form isopentenyl pyrophosphate which is part of the biosynthesis of steroids, and other compounds such as pyridoxol. Structural studies As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2O1S and 2O1X. References 1 Biology no Category:EC 2.2.1 Category:Enzymes of known structure