34693-15-7Relevant articles and documents
Efficient production of 2-deoxyribose 5-phosphate from glucose and acetaldehyde by coupling of the alcoholic fermentation system of baker's yeast and deoxyriboaldolase-expressing Escherichia coli
Horinouchi, Nobuyuki,Ogawa, Jun,Kawano, Takako,Sakai, Takafumi,Saito, Kyota,Matsumoto, Seiichiro,Sasaki, Mie,Mikami, Yoichi,Shimizu, Sakayu
, p. 1371 - 1378 (2008/02/11)
2-Deoxyribose 5-phosphate production through coupling of the alcoholic fermentation system of baker's yeast and deoxyriboaldolase-expressing Escherichia coli was investigated. In this process, baker's yeast generates fructose 1,6-diphosphate from glucose and inorganic phosphate, and then the E. coli convert the fructose 1,6-diphosphate into 2-deoxyribose 5-phosphate via D-glyceraldehyde 3-phosphate. Under the optimized conditions with toluene-treated yeast cells, 356 mM (121 g/l) fructose 1,6-diphosphate was produced from 1,111 mM glucose and 750 mM potassium phosphate buffer (pH 6.4) with a catalytic amount of AMP, and the reaction supernatant containing the fructose 1,6-diphosphate was used directly as substrate for 2-deoxyribose 5-phosphate production with the E. coli cells. With 178 mM enzymatically prepared fructose 1,6-diphosphate and 400 mM acetaldehyde as substrates, 246 mM (52.6 g/l) 2-deoxyribose 5-phosphate was produced. The molar yield of 2-deoxyribose 5-phosphate as to glucose through the total two step reaction was 22.1%. The 2-deoxyribose 5-phosphate produced was converted to 2-deoxyribose with a molar yield of 85% through endogenous or exogenous phosphatase activity.
Anomerization of Furanose Sugars and Sugar Phosphates
Pierce, John,Serianni, Anthony S.,Barker, Robert
, p. 2448 - 2456 (2007/10/02)
Thermodynamic and kinetic parameters for the ring-opening and -closing reactions of several aldo- and ketofuanoses and their phosphate esters have been determined by NMR line-width and saturation-transfer methods.Cyclic forms interconvert via a single, acyclic carbonyl form under either acid or base catalysis.Ring-opening rates do not correlate with thermodynamic stability of the rings.For aldofuranose phosphates, α anomers open faster than β anomers; for ketofuranose phosphates the converse is observed.Intramolecular catalysis of anomerization by the phosphate group of sugar phosphates is documented.Biological and mechanistic implications of the observed kinetics are discussed.
Chemical and Enzymatic Syntheses of 6-Deoxyhexoses. Conversion to 2,5-Dimethyl-4-hydroxy-2,3-dihydrofuran-3-one (Furaneol) and Analogues
Wong, Chi-Huey,Mazenod, Francois P.,Whitesides, George M.
, p. 3493 - 3497 (2007/10/02)
6-Deoxy-D-fructose 1-phosphate (6-deoxyF-1-P) forms when a solution containing D-fructose 1,6-diphosphate (FDP) and D-lactaldehyde is treated with the enzymes aldolase and triosephosphate isomerase (Scheme I).This transformation involves three reactions: aldolase-catalyzed cleavage of FDP to a mixture of dihydroxyacetone phosphate and D-glyceraldehyde phosphate, triosephosphate isomerase catalyzed equilibration of dihydroxyacetone phosphate and D-glyceraldehyde phosphate, and aldolase-catalyzed condensation of dihydroxyacetone phosphate and D-lactaldehyde to 6-deoxyF-1-P.An analogous process converts a mixture of FDP and L-lactaldehyde to 6-deoxysorbose 1-phosphate (6-deoxyS-1-P).Aldolase-catalyzed reaction of dihydroxyacetone phosphate, prepared separately, with D-lactaldehyde yields 6-deoxyF-1-P directly; similar reaction of dihydroxyacetone phosphate with α-hydroxybutyraldehyde yields a mixture of 6-methyl-6-deoxyhexose 1-phosphates.Acid-catalyzed hydrolysis of the sugar phosphates releases the corresponding free sugars.A mixture containing 6-deoxyhexoses is formed directly by base-catalyzed aldol condensation of dihydroxyacetone and D,L-lactaldehyde.Treatment of any of the 6-deoxyhexoses with acids generates 2,5-dimethyl-4-hydroxy-2,3-dihydrofuran-3-one (Furaneol, a flavor principle).Furaneol can also be prepared in moderate yields by hydrogenolysis of FDP and other hexose phosphates in alkaline media.
