Fructose 1-6-diphosphate aldolase

Kelley, P.M. Freeling, M. (1984b). Anaerobic expression of maize fructose-1,6-diphosphate aldolase. Journal of Biological Chemistry, 259,14180-3. 

Brockamp, H.P, Kula, M.R. and Goetz, F. (1991) A robust microbial fructose-1,6-diphosphate aldolase its manufacture and use in sugar synthesis. DE3940431. 

A syringolide 45, an elicitor of the bacterial plant pathogen Pseudomonas Siringae pv. tomato, has been synthesized in five steps via a fructose 1,6-diphosphate aldolase reaction (Scheme 95) <2000JOC4529>. 

Radhaiah, V., K.V. Joseph, and K.J. Rao. 1989. Toxic effect of fenvalerate on fructose-1,6-diphosphate aldolase activity of liver, gill, kidney, and brain of the fresh water teleost, Tilapia mossambica. Bull. Environ. Contam. Toxicol. 42 150-153. 

Von derOsten, C.H., Sinskey, A.J., Barbas El, C.F., Pederson, R.L., Wang, Y.F. and Wong, C.H., Use of a recombinant bacterial fructose-1,6-diphosphate aldolase in aldol reactions preparative syntheses of 1-deoxynojirimycin, 1-deoxymannojirimycin, l,4-dideoxy-l,4-imino-D-arahinitol, and fagomine. J. Am. Chem. Soc., 1989, 111, 3924. 

Reaction of ribose 5-phosphate 116 with dihydroxyacetone phosphate, catalyzed by fructose 1,6-diphosphate aldolase from rabbit muscle (RAMA) affords the ketose diphosphate 117. Dihydroxyacetone phosphate was formed in situ from fructose 1,6-diphosphate by action of RAMA and triose phosphate isome-rase (TPI). The diphosphate 117 was dephosphorylated enzymatically using acid phosphatase, and the ketose 118 was reduced directly into the a-C-manno-side 119 by treatment with bistrimethylsilyltrifluoroacetamide, trimethylsilyl-triflate and triethylsilane (Scheme 28) [45]. 

An interesting enzyme-catalyzed three-component aldolization reaction has been described by Gijsen and Wong [18]. Here, acetaldeyde, 2-substituted acetaldehydes, and dihydroxyacetone phosphate react in the presence of the aldolases 2-deoxyribose-5-phosphate aldolase (DERA) and fructose 1,6-diphosphate aldolase (RAMA) forming the corresponding 5-deoxyketose derivatives (Scheme 9.9). 

Chenevert R, Dasser M (2000) Chemoenzymatic synthesis of the microbial elicitor (—)-syringolide via a fructose 1,6-diphosphate aldolase-catalyzed condensation reaction. J Org Chem 65 4529 1531... 

Fig. 24 (a, b) Chemo-enzymatic process for synthesis of tetrahydroxylated pyrrolizidines 1-epi-alexine, australine and 3-epi-australine utilising dihydroxyacetone phosphate (DHAP), stereospecific aldol reaction catalysed by fructose-1.6-diphosphate aldolase (FDPA) and acid phosphatase (Pase) [149]... 

Carbon-carbon bond-forming reactions are some of the most important transformations in organic chemistry. Sobolov et al. [33] reported that CLCs of fructose 1,6-diphosphate aldolase from rabbit muscle are much more stable than the soluble enzyme. The synthetic potential of these CLCs was demonstrated by the preparation of a series of compounds shown in Fig. 10. 

Two new stereocenters are established in the DHAP-dependent aldolases-cata-lyzed carbon-carbon bond formation. Consequently four different stereoisomers can be formed (Scheme 5.23). Enantioselective aldolases that catalyze the formation of just one of each of the stereoisomers are available fructose 1,6-diphosphate aldolase (FDP A), rhamnulose 1-phosphate aldolase (Rha 1-PA), L-fucu-lose 1-phosphate aldolase (Fuc 1-PA) and tagatose 1,6-diphosphate aldolase (TDP A). In particular the FDP A, that catalyzes the formation of the D-threo stereochemistry, has been employed in many syntheses. One such FDP A that... 

We faced the problem of the poor solubility of most N-protected amino aldehydes in water, which might account for the low reactivity observed with D-fructose-1,6-diphosphate aldolase from rabbit muscle (RAMA) (14, 15, 19-21). Increasing the percentage of organic co-solvent (e.g. dimethylformamide) in the medium to make the aldehyde soluble may lead to either a dramatic enzyme deactivation [22] or an insolubilization of the donor (e.g. dihydroxyacetone (DHA) and DHAP sodium salt). As a result, no reaction or insufficient product yields are often obtained. 

Bischofberger, N, Waldmann, H, Saito, T, Simon, E S, Lees, W, Bednarski, M D, Whitesides, G M, Synthesis of analogues of 1,3-dihydroxyacetone phosphate and glyceraldehyde 3-phosphate for use in studies of fructose-1,6-diphosphate aldolase, J. Org. Chem., 53, 3457-3465, 1988. 

D-Fructose-1,6-diphosphate aldolase (FDP) catalyzes the reversible aldol addition of DHAP and D-glyceraldehyde-3-phosphate (G3P) to form D-fructose-1,6-diphosphate (FDP), for which Keq 10 M in favor of FDP formation (O Scheme 6). Rabbit muscle aldolase accepts a wide range of aldehyde acceptor substrates with DHAP as the donor to generate 35, 45 vicinal diols, stereospecifically (O Scheme 5). A racemic mixture of non-natural aldehyde acceptors can be partially resolved only under conditions of kinetic control. When... 

Fructose-1,6-diphosphate aldolase of rabbit muscle has been studied very extensively-and it is now commercially available. That of spinach leaves, obviously very accessible, was recently examined (Valentin and Bolte 1993). In the fundamental reaction of glycolysis (reaction 6.8), the donor is dihydroxyacetone phosphate. It can scarcely be varied, but there is more flexibility with the acceptor (David et al. 1991 Bednarski et al. 1989), and sometimes we can wander considerably from the subject of sugar chemistry. In any case, the vicinaZ-diol created at positions 3 and 4 (uloses numbering) has the D-threo configuration. Hence the condensation of the keto aldehyde 6.28 gives ketose 6.29 which, after isolation, is dephosphorylated enzymically in the presence of acid phosphatase. 

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