Among dihydroxyacetone phosphate (DHAP) aldolases, tagatose-1,6-bisphosphate aldolases (TagA) remain the nonexplored family in biocatalysis despite the synthetic importance of the (2 S,3 S )−2,3-dihydroxyketone motif. Using a genome-mining approach to access natural biodiversity, we identified and characterized a TagA from Anaerotruncus colihominis . This enzyme displayed the best potential for the stereoselective synthesis of d -tagatose-1,6-bisphosphate as well as structurally related analogs obtained with varying diastereomeric purities. Notably, five compounds with ( S, S ) configuration were obtained with this DHAP-aldolase. Interestingly, even when the enzyme exhibited a preference for the ( S, R ) configuration, its broad electrophilic substrate scope allowed it to outperform fructose-1,6-bisphosphate aldolases (FruA) by producing d -xylulose-1,5-bisphosphate, an important monosaccharide that FruA are unable to generate.
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Paulat et al. (2026) studied this question.
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