1 -Deoxy-D-xylulose-5-phosphate

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]. 

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... 

The enzymatic conversion of l-deoxy-D-xylulose-5-phosphate to pyridoxol phosphate (Vitamin B6) in E. coli was demonstrated <99JA7722>. 

From the many enzymes that are known to make and break C-C bonds, we first chose the two transferases, transketolase (TKT) and transaldolase (TAL), both from the Gram-negative bacterium Escherichia coli. While project B21 evolved, we learned that this microorganism holds other and so far unknown enzymes which are of interest for asymmetric syntheses. One transketolase-like enzyme, 1-deoxy-D-xylulose 5-phosphate synthase (DXS), turned out to be the first enzyme of a novel biosynthetic pathway leading to isoprenoids in bacteria, algae, and plants. The other, fructose 6-phosphate aldolase (ESA) - while similar to transaldolase - allows the direct use of the inexpensive dihydroxyacetone in aldol condensations. 

C-C-Bonding Microbial Enzymes 317 2.2.2.2.2 1-Deoxy-D-xylulose 5-Phosphate Synthase (DXS)... 

Another example of successful engineering of terpene biosynthesis is the constitutive overexpression of the gene encoding the first-step enzyme 1-deoxy-D-xylulose-5-phosphate synthase (DXPS) in the DXP pathway in bacteria and Arabidopsis. In both cases, increased enzyme activity caused increased accumulation of downstream terpenoids, suggesting that DXPS is rate-limiting [8]. 

Acetohydroxy acid synthase (acetolactate synthase) 1-Deoxy-D-xylulose 5-phosphate synthase Transketolase ... 

The biochemical isoprene units may be derived by two pathways, by way of intermediates mevalonic acid (MVA) (Figure 5.4) or 1-deoxy-D-xylulose 5-phosphate (deoxyxylulose phosphate DXP) (Figure 5.6). Mevalonic acid, itself a product of acetate metabolism, had been established as a precursor of the animal sterol cholesterol, and... 

Deoxy-D-xylulose 5-phosphate is formed from the glycolytic pathway intermediates pyruvic acid and glyceraldehyde 3-phosphate with the loss of the pyruvate carboxyl (Figure 5.6). Thiamine diphosphate-mediated decarboxylation of pyruvate... 

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