Enzymes Engineered aldolase

A large number of other aldolases have been isolated and characterized (Table 5).33.42.43.i 11-127 Limited explorations of substrate specificity have been made in many cases but these enzymes have not yet been used in synthetic organic chemistry. In terms of potential utility as catalysts, the aldolases of bacterial origin may be of more use than the enzymes from plant or animal sources because the former are more easily cloned and altered by genetic engineering than the latter. The alterations should prove to be useful for controlling the substrate specificity of these enzymes. 

E. (2009) Substrate channelling in an engineered bifunctional aldolase/kinase enzyme confers catalytic advantage for C-C bond formation. Chem. Commun. (Camb.), 1721-1723. 

Aldolase redesign by protein engineering is mainly focused on enhancing the acceptor and donor tolerance toward a wide stractural spectrum of nucleophiles and electrophiles. In this connection, FSA-Hke enzymes constitute an attractive platform for modification because of their intrinsic tolerance toward structurally diverse donors. 

Recent advances in enzyme-catalyzed aldol addition reactions for biocatalytic carbon-carbon bond formation by means of aldolases are described. They offer an exceptionally stereoselective and green tool for asymmetric framework construction and preparation of innovative molecules with engineered enz5unes. 

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