Two bacterial aldolases, RhuA and FucA, which are readily accessible by overex‐pression, catalyze the asymmetric addition of dihydroxyacetone phosphate to various aldehydes. The high degree of enantio‐and diastereoselectivity for the L‐threo (RhuA) and D‐erythro (FucA) stereochemistry of the products and the high stability of the enzymes make it possible to prepare rare carbohydrates and their derivatives as well as other polyhydroxylated compounds.
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