作者: Hubert Casajus , Aurélie Lagarde , Martin Leremboure , Thomas De Dios Miguel , Lionel Nauton
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摘要: The thermostable transketolase from Geobacillus stearothermophilus (TKgst) was successfully engineered for the synthesis of aliphatic acyloins with varying carbon backbone lengths (C5−C10) based on protein structure‐guided studies. Efficient TKgst variants were identified enhanced activities substrate combinations aldehydes as acceptors together pyruvate homologues donors. single variant L382F able to catalyze efficiently transfer ketol group hydroxypyruvate all targeted (C3−C8) give corresponding 1,3‐dihydroxy ketones good yields and excellent enantioselectivity. combination H102L/H474S mutation previously designed improved utilization a F435I exchange gave new H102L/H474S/F435I, which is acyl goup 2‐oxobutyrate 2‐oxovalerate aldehydes, giving mono hydroxylated ketones.