1-deoxy-D-xylulose

Transketolase catalyzes the reversible transfer of a hydroxyacetyl fragment from a ketose to an aldehyde. Because the ketose products formed by transketolase reactions are not acceptors for a consecutive transformation by the same enzyme, we have investigated the option to include a xylose (glucose) isomerase (Xyll E.C. 5.3.1.5), which has similar stereochemical specificity, for ketose to aldose equilibration (Scheme 2.2.5.13). Starting from racemic lactaldehyde 32a, the transketolase forms 5-deoxy-D-xylulose 35a, which indeed was accepted by the Xyll in situ for diastereospecific conversion into 5-deoxy-D-xylose 36a. The latter again proved to be a substrate of transketolase which completed a tandem operation to furnish 7-deoxy-sedoheptulose 37a as the sole bisadduct in 24% overall yield and in enantio- and diastereomerically pure quality [35, 36]. All four stereocenters of the resulting product are completely controlled by the enzymes during this one-pot operation. The procedure profits from the limited tolerance of the isomerase... 

The Synthesis of Sugars from Simpler Substances. Part VII. Enzymic Synthesis of 5-Deoxy-D-xylulose, P. A. J. Gorin, L. Hough, and J. K. N. Jones,/. Chem. Soc., (1953) 2140-2142. 

Hoberman, H. D., Adduct formation between hemoglobin and 5-deoxy-D-xylulose-l-phosphate. Biochem. Biophys. Res. Common. 90, 764-768 (1979). 

Based on a wide range of crystallographic data of the mutant enzymes with D-xylose (18),5-thio-D-glucopyranose (38) or 5-deoxy-D-xylulose (39) (Scheme 15) in their active sites, this view was not supported by the investigators. An in-... 

This thermodynamic driving force is particularly useful tvith multienzyme equilibrium systems such as that used in the gram-scale synthesis of tv ro equivalents ofo-xylulose 5-phosphate (104) from (26) (Figure 10.38) [171,172]. Similarly, the corresponding 1-deoxy-D-xylulose 5-phosphate tvas efficiently produced from pyruvate and (34) by the catalytic action of the thiamine diphosphate-dependent 1-deoxy-D-xylulose 5-phosphate synthase (DXS) (EC 2.2.1.7) from E. coli [173]. 

HARKER M and BRAMLEY P M (1999) Expression of l-deoxy-D-xylulose-5-phosphatases in E. coli increases carotenoid and ubiquinone biosynthesis , FEBSLett, 448, 115-19. 

LicHTENTHALER H K (1999) The 1-deoxy-D-xylulose-5-phosphate pathway of isoprenoid biosynthesis in plants , Ann Rev Plant Physiol Plant Mol Biol, 50, 47-65. 

D-glyceraldehyde-3-phosphate, pyruvate (G3P) l-deoxy-D-xylulose-5-phosphate (DXP) 2C-methyl-D-erythritol-4-phosphate (MEP) 4-diphosph-2C-methyl-D-erythritol (CDP-ME) 4-diphosphocytidyl-2C-methyl-D-erythritol-2-phophate (CDP-MEP)... 

Sprenger, G.A. et al.. 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. USA 94, 12857, 1997. Lange, B.M. et al., A family of transketolases that directs isoprenoid biosynthesis via a mevalonate-independent pathway, Proc. Natl. Acad Sci. USA 95, 2100, 1998. Lois, L.M. et al., Cloning and characterization of a gene from Escherichia coli encoding a transketolase-like enzyme that catalyzes the synthesis of D-1- deoxyxylulose 5-phosphate, a common precursor for isoprenoid, thiamin, and pyridoxol biosynthesis, Proc. Natl. Acad. Sci. USA 95, 2105, 1998. 

Page, J.E. et al., Functional analysis of the final steps of the 1-deoxy-D-xylulose 5-phosphate (DXP) pathway to isoprenoids in plants using virus-induced gene silencing, Plant Physiol. 134, 1401, 2004. 

Lois, L.M. et al.. Carotenoid biosynthesis during tomato fruit development regulatory role of 1-deoxy-D-xylulose 5-phosphate synthase. Plant J. 22, 503, 2000. 

Hans, J. et al.. Cloning, characterization, and immunolocalization of a mycorrhiza-inducible 1-deoxy-d-xylulose 5-phosphate reductoisomerase in arbuscule-containing cells of maize, Plant Physiol. 134, 614, 2004. 

Estevez, J.M. et al., l-Deoxy-D-xylulose-5-phosphate synthase, a limiting enzyme for plastidic isoprenoid biosynthesis in plants, J. Biol. Chem. 276, 22901, 2001. 

Figure 9.4 Monoterpene biosynthesis in peppermint oil gland secretory cells. The enzymes involved in this pathway are (1) 1-deoxy-D-xylulose 5-phosphate synthase, (2) 2-C-methyl-D-erythritol 4-phosphate reductoisomerase, (3) 2-C-methyl-D-erythritol 4-phosphate cytidyltransferase, (4) 4-(cytidine 5 -diphospho)-2-C-methyl-D-erythritol kinase, (5) 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, (6) isopentenyl diphosphate isomerase, (7) geranyl diphosphate synthase, (8)...

Table 9.2 Incorporation rate of [2-14C]-pyruvate into monoterpenes of isolated peppermint oil gland secretory cells in the presence of fosmidomycin, a specific inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase, an enzyme of the mevalonate-independent pathway of isoprenoid biosynthesis.

LANGE, B.M., CROTEAU, R., Isoprenoid biosynthesis via a mevalonate-independent pathway in plants cloning and heterologous expression of 1-deoxy-D-xylulose 5-phosphate reductoisomerase from peppermint, Arch. Biochem. Biophys., 1999,365,170-174. 

SAGNER, S., EISENREICH, W., FELLERMEIER, M LATZEL, C., BACHER, A., ZENK, M.H., Biosynthesis of 2-C-methyl-D-erythritol in plants by rearrangement of the terpenoid precursor, 1-deoxy-D-xylulose 5-phosphate, Tetrahedron Lett., 1998, 39, 2091-2094. 

TAKAHASHI, S., KUZUYAMA, T WATANABE H., SETO, H., A 1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzing the formation of 2-C-methyl-D-erythritol 4-phosphate in an alternative nonmevalonate pathway, Proc. Natl. Acad. Sci. USA, 1998, 95, 9879-9884. 

ZEIDLER, J., SCHWENDER, J., MULLER, C WIESNER, J., WEIDEMEYER, C., BECK, E., JOMAA, H., LICHTENTHALER, H.K., Inhibition of the non-mevalonate 1-deoxy-D-xylulose 5-phosphate pathway of plant isoprenoid biosynthesis by fosmidomycin, Z. Naturforsch., 1998,53c, 980-986. 

The CPPase substrate DMAPP (15) is formed from isopentenyl pyrophosphate (IPP) (14) via the IPP isomerase reaction. It had been assumed that IPP was generated only via mevalonic acid (12) (Fig. 2), but Rohmer discovered another route, 2-C-methyl-D-erythritol 4-phosphate (13) (MEP) pathway (Fig. 2) [22, 23]. A key step in the MEP pathway is the reaction catalyzed by 1-deoxy-D-xylulose 5-phosphate synthase (DXS), which combines hydroxyethyl thiamine pyrophosphate (hydroxyethyl TPP) generated from pyruvic acid (17) and TPP with glyceral-dehyde 3-phosphate (18) to yield 1-deoxy-D-xylulose 5-phosphate (19) containing five carbons. The mevalonate pathway operates in the cytosol of plants and animals, whereas the MEP pathway is present in the plastid of plants or in eubacteria [24-27]. 

Wanke M, Skorupinska-Tudek K, Swiezewska E (2001) Isoprenoid biosynthesis via 1-deoxy-D-xylulose 5-phosphate/2-C-methyl-D-erythritol 4-phosphate (DOXP/MEP) pathway. Act... 

---