Abstract
AbstractTransketolase (TK) from various origins (including Escherichia coli and yeast) has been described to be fully enantiomer specific for (2R)‐hydroxyaldehyde substrates. A thermostable TK from Geobacillus stearothermophilus (TKgst) was found to display a minor reactivity for (2S)‐hydroxylated aldehydes. To improve this activity by directed protein evolution, we have built a library of TKgst variants by site saturation mutagenesis on two key positions L382 and D470. The best TKgst double mutant L382D/D470S shows up to 4‐ and 5‐fold higher activities towards L‐lactaldehyde and L‐glyceraldehyde as acceptor substrates, respectively. Preparative utility of this mutant was demonstrated by the one‐step synthesis of valuable L‐ribulose and its 5‐deoxy analogue with the L‐erythro (3S,4S) configuration, which were previously inaccessible by using common TK sources.magnified image
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