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

{{Short description|Class of enzymes}} {{cs1 config|name-list-style=vanc|display-authors=6}} {{DISPLAYTITLE:1-deoxy-<small>D</small>-xylulose-5-phosphate synthase}} {{infobox enzyme | Name = 1-deoxy-{{sm|d}}-xylulose-5-phosphate synthase | EC_number = 2.2.1.7 | CAS_number = 202218-79-9 | GO_code = 0008661 | image = | width = | caption = }} '''1-deoxy-{{sm|d}}-xylulose-5-phosphate synthase''' ({{EC number|2.2.1.7}}) is an enzyme in the non-mevalonate pathway that catalyzes the chemical reaction

{{Chemrxn|width=70%| {{Chemrxn/cpd|Pyruvic acid|upright=0.6 }} {{Chemrxn/txt|+ }} {{Chemrxn/cpd|qid=Q26992303|caption=D-glyceraldehyde-3-phosphate }} {{Chemrxn/arw|fwd_out={{chem2|CO2}} }} {{Chemrxn/cpd|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.<ref name=Sprenger>{{cite journal | vauthors = Sprenger GA, Schörken U, Wiegert T, Grolle S, de Graaf AA, Taylor SV, Begley TP, Bringer-Meyer S, Sahm H | title = 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 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 94 | issue = 24 | pages = 12857–12862 | date = November 1997 | pmid = 9371765 | doi = 10.1073/pnas.94.24.12857 | doi-access = free | pmc = 24228 }}</ref><ref name=Kuzuyama>{{cite journal | vauthors = Kuzuyama T, Takagi M, Takahashi S, Seto H | title = 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 = Journal of Bacteriology | volume = 182 | issue = 4 | pages = 891–897 | date = February 2000 | pmid = 10648511 | doi = 10.1128/JB.182.4.891-897.2000 | pmc = 94361 }}</ref> The enzyme has been characterised from ''Escherichia coli''<ref name=Sprenger/> and a ''Streptomyces'' species.<ref name=Kuzuyama/>

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:{{sm|d}}-glyceraldehyde-3-phosphate acetaldehydetransferase (decarboxylating)'''. Other names in common use include '''1-deoxy-{{sm|d}}-xylulose-5-phosphate pyruvate-lyase (carboxylating)''', and '''DXP-synthase'''.<ref>{{KEGG enzyme|2.2.1.7}}</ref> The product of the enzyme goes on to form isopentenyl pyrophosphate which is part of the biosynthesis of steroids,<ref name=Kuzuyama/> and other compounds such as pyridoxol.<ref name=Sprenger/>

==Structural studies== As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|2O1S}} and {{PDB link|2O1X}}.

== References == {{reflist|1}} *

Category:EC 2.2.1 Category:Enzymes of known structure