Abstract
In this chapter our recent progress is compiled in the evaluation of a tetrad of stereochemically complementary microbial aldolases as powerful and broadly applicable enzymic catalysts for use in asymmetric synthesis. Made readily available by recombinant DNA methodology and being remarkably stable, these enzymes are capable of promoting efficient, highly enantio- and diastereocontrolled C-C bond formations of a type that proves useful in the de novo syntheses of carbohydrates and related polyhydroxy compounds. Applications range from preparations of rare l-configurated sugars to that of branched-chain, unsaturated, or differently substituted sugar derivatives. Further developments have been made towards the control of the stereochemistry of additional chiral centers, in subsequent enzymatic conversions of aldolase generated products, or in the assembly of aldolase-based complex multi-enzyme cascade reactions that exploit renewable resources as precursors for simple one-pot syntheses.
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References
Toone, E. J., Simon, E. S., Bednarski, M. D., and Whitesides, G. M. (1989) ‘Enzyme-catalyzed synthesis of carbohydrates’, Tetrahedron 45, 5365–5422.
Drueckhammer, D. G., Hennen, W. J., Pederson, R. L., Barbas, C. F., Gautheron, C. M., Krach, T., and Wong, C.-H. (1991) ‘Enzyme catalysis in synthetic carbohydrate chemistry’, Synthesis, 499–525.
Fessner, W.-D. ‘Enzyme catalyzed aldol additions’, in G. Helmchen, R. W. Hoffmann, J. Mulzer, E. Schaumann (eds.), Methoden der Organischen Chemie (Houben-Weyl) 4. Ed., Vol. E22: Stereoselective Synthesis of Organic Compounds, Thieme, Stuttgart, in press.
Fessner, W.-D., Sinerius, G., Schneider, A., Dreyer, M., Schulz, G. E., Badía, J., and Aguilar, J. (1991) ‘Diastereoselective enzymatic aldol additions: l-rhamnulose and l-fuculose 1-phosphate aldolases from E. coli’, Angew. Chem. Int. Ed. Engl., 30, 555–558.
Fessner, W.-D. and Eyrisch, O. (1992) ‘One-pot synthesis of tagatose 1,6-bisphosphate by diastereoselective enzymatic aldol addition’, Angew. Chem. Int. Ed. Engl., 31, 56–58.
von der Osten, C. H., Sinskey, A. J., Barbas, C. F., Pederson, R. L., Wang, Y.-F., and Wong, C.-H. (1989) ‘Use of a recombinant bacterial fructose-1,6-diphosphate aldolase in aldol reactions: preparative syntheses of 1-deoxynojirimycin, 1-deoxymannojirimycin, 1,4-dideoxy-l,4-imino-d-arabinitol, and fagomine’, J. Am. Chem. Soc., 3924–3927.
Alefounder, P. R., Baldwin, S. A., Perham, R. N., and Short, N. J. (1989) ‘Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli’, Biochem. J. 257, 529–534.
Schreiber, S. L. and Verdine, G. L. (1991) ‘Protein Overproduction for organic chemists’, Tetrahedron 47, 2543–2562.
Ozaki, A., Toone, E. J., von der Osten, C. H., Sinskey, A. J., and Whitesides, G. M. (1990) ‘Overproduction and substrate specificity of a bacterial fuculose-1-phosphate aldolase: a new enzymatic catalyst for stereocontrolled aldol condensation’, J. Am. Chem. Soc. 112, 4970–4971.
Bissett, D. L. and Anderson, R. L. (1980) ‘Lactose and d-galactose metabolism in Staphylococcus aureus IV. Isolation and properties of a class I d-ketose-1,6-diphosphate aldolase that catalyzes the cleavage of d-tagatose 1,6-diphosphate’, J. Biol. Chem. 255, 8750–8755.
Periana, R. A., Motiu-DeGrood, R., Chiang, Y., and Hupe, D. J. (1980) ‘Does substrate rather than protein provide the catalyst for α-proton abstraction in aldolase?’, J. Am. Chem. Soc. 102, 3923–3927
Fessner, W.-D., Sinerius, G., Schneider, A., and Weis, K. (1991) ‘Limits of aldolase stereoselectivity’, 202nd ACS National Meeting, New York City, paper BIOL 9.
Eyrisch, O., Schneider, A., Sinerius, G.,Walter, C., and Fessner, W.-D., unpublished results.
Bednarski, M. D., Simon, E. S., Bischofberger, N., Fessner, W.-D., Kim, M.-J., Lees, W., Saito, T., Waldmann, H., and Whitesides, G. M.(1989) ‘Rabbit muscle aldolase as a catalyst in organic synthesis’, J. Am. Chem. Soc. 111, 627–635.
Fessner, W.-D. and Whitesides, G.M. (1987) ‘Enzymatic Aldol Condensations — Key Step to Unusual Oligosaccharides’, IV. European Carbohydrate Symposium, Darmstadt, FRG, A141.
Durrwachter, J. R. and Wong, C.-H. (1988) ‘Fructose 1,6-diphosphate aldolase catalyzed stereoselective synthesis of C-alkyl and N-containing sugars: thermodynamicall controlled C-C bond formations’, J. Org. Chem. 53, 4175–4181.
Badía, J., Gimenez, R., Baldomá, L., Barnes, E., Fessner, W.-D., and Aguilar, J. (1991) ‘l-Lyxose metabolism employs the l-rhamnose pathway in mutant cells of Escherichia coli adapted to grow on this pentose’, J. Bacteriol. 173, 5144–5150.
Durrwachter, J. R., Drueckhammer, D. G., Nozaki, K., Sweers, H. M., and Wong, C.-H. (1989) ‘Enzymatic aldol condensation/isomerization as a route to unusual sugar derivatives’, J. Org. Chem. 54, 70–77.
Borysenko, C., Spaltenstein, A., Straub, J., and Whitesides, G. M. (1989) ‘Synthesis of aldose sugars from half-protected dialdehydes using rabbit muscle aldolase’, J. Am. Chem. Soc. 111, 9275–9276.
Fessner, W.-D. and Walter, C. (1992) ‘“Artificial metabolisms” for the asymmetric one-pot synthesis of branched-chain saccharides’, Angew. Chem. Int. Ed. Engl., in print.
Babul, J. (1978) ‘Phosphofructokinases from Escherichia coli. Purification and characterization of the nonallosteric isozyme’, J. Biol. Chem. 253, 4350–4355.
Daldal, F. (1983) ‘Molecular cloning of the gene for phosphofructokinase-2 of Escherichia coli and the nature of a mutation, pfkB1, causing a high level of the enzyme’, J. Mol. Biol. 168, 285–305.
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© 1992 Springer Science+Business Media Dordrecht
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Fessner, WD. (1992). A Building Block Strategy for Asymmetric Synthesis: The DHAP-Aldolases. In: Servi, S. (eds) Microbial Reagents in Organic Synthesis. NATO ASI Series, vol 381. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-2444-7_4
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DOI: https://doi.org/10.1007/978-94-011-2444-7_4
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