Exploring the synthetic potential of dihydroxyacetone-aldolases from acidophilic organisms

Abstract

Two novel dihydroxyacetone (DHA)-aldolases have been identified from acidophilic bacteria and subjected to biochemical characterization to assess their substrate scope in comparison to the E. coli counterpart. These enzymes showcase unique characteristics within their active sites, distinguishing them from the known E. coli DHA-aldolase. Notably, the production efficiency of D-threose was significantly augmented compared to previously published methodologies. Furthermore, a diverse array of monosaccharides were synthesized, encompassing previously reported methods obtained through alternative routes, along with novel compounds previously inaccessible. In particular, we reavealed the first DHA aldolase capable of using acetaldehyde as the nucleophile with a non-phosphorylated electrophile. This remarkable capability opens the way to the synthesis of chiral compounds, facilitating access to a broad range of new synthons useful in the preparation of biologically active compounds.