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Starting from commercially available fructose 1,6-bisphosphate and hydroxypyruvate, three enzymes were in use: fructose 1,6-bisphosphate aldolase, triosephosphate isomerase, and transketolase; see
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Starting from commercially available fructose 1,6-bisphosphate and hydroxypyruvate, three enzymes were in use: fructose 1,6-bisphosphate aldolase, triosephosphate isomerase, and transketolase; see: F. T. Zimmermann, A. Schneider, U. Schörken, G. A. Sprenger, W.-D. Fessner, Tetrahedron Asymmetry 1999, 10, 1643-1646.
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Starting point was the aldolase-catalyzed cleavage of fructose 1,6-bisphosphate to yield dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde 3-phosphate (Ga3P) in equal amounts. Ga3P was converted into DXP and CO2 using pyruvate as the donor substrate and DXS as catalyst. Reversible interconversion of DHAP and Ga3P was achieved with triosephosphate isomerase. NMR analysis of the product confirmed that the D-threo-pentulose was formed with a high enantiomeric excess; see
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Starting point was the aldolase-catalyzed cleavage of fructose 1,6-bisphosphate to yield dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde 3-phosphate (Ga3P) in equal amounts. Ga3P was converted into DXP and CO2 using pyruvate as the donor substrate and DXS as catalyst. Reversible interconversion of DHAP and Ga3P was achieved with triosephosphate isomerase. NMR analysis of the product confirmed that the D-threo-pentulose was formed with a high enantiomeric excess; see: a) S. V. Taylor, L. D. Vu, T. P. Begley, U. Schörken, G. A. Sprenger, S. Bringer-Meyer, H. Sahm, J. Org. Chem. 1998, 63, 2375-2377.
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0032587126
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An example of application of DXS to prepare labeled DXP for the elucidation of the vitamin B6 pathway is given in
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Schürmann, M.1
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