We described a strategy for the enzymatic synthesis of 1-deoxy and 1,2-deoxyketoses from the
aliphatic α-ketoacids, pyruvate and 2-oxobutyrate, as donors and natural aldoses of variable chain length … as
acceptors, catalyzed by thermostable transketolase variants from Geobacillus stearothermophilus (TKgst).
Analytical studies have been carried out on a panel of TKgst variants with the appropriate substrates allowing to
select the best combinations and to apply it to the preparative scale synthesis of 1-deoxy and 1,2-deoxyketoses
obtained with good to excellent isolated yields (61%–86%). To optimize the strategy, and as a proof of
principle, the α-ketoacids pyruvate and 2-oxobutyrate were generated in situ from the corresponding d-amino
acids d-alanine and d-homoalanine respectively, using a thermostable d-amino acid oxidase dAAO4536 that
was selected from a screening of 55 putative DAAOs provided by Prozomix Limited. Hence, a one-pot one
step procedure was performed at 50°C by coupling dAAO4536 and the best TKgst variant H102L/L118I/
H474S in the presence of d-alanine or d-homoalanine as α-ketoacids precursors and d-erythrose as acceptor
substrate. The corresponding 1-deoxy and 1,2-dideoxyketoses were isolated with good yields (64% and 72%
respectively, out of two steps)
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