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Cleavage of Aliphatic α-Hydroxy Ketones by Evolved Transketolase from Geobacillus stearothermophilus

Abstract : The reaction catalyzed by ubiquitous thiamine pyrophosphate-dependent transketolase engaged in cells in the pentose phosphate pathway can be applied in vitro to the cleavage of aliphatic α-hydroxy ketones with thermostable transketolase variants from Geobacillus stearothermophilus obtained through rational design. The simple variant F435I gave the best activity toward (3S)-1,3-dihydroxyhexan-2-one 3, leading to the corresponding product with 92% yield after only 2 h of reaction time. Three triple variants H102L/H474 (S, G, or A)/F118I were found to cleave (±)-4-hydroxyhexan-3-one 6, giving the corresponding product with 90, 82, and 79% yield, respectively, after 24 h, whereas wild-type transketolase was almost ineffective. This biocatalytic strategy offers a promising one-step alternative to other multienzyme or chemical ways for the cleavage of aliphatic α-hydroxy ketones.
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Contributor : Stéphanie Bonnefoy Connect in order to contact the contributor
Submitted on : Monday, March 14, 2022 - 1:47:25 PM
Last modification on : Thursday, August 4, 2022 - 5:14:34 PM
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Hubert Casajus, Aurélie Lagarde, Lionel Nauton, Nazim Ocal, Martin Leremboure, et al.. Cleavage of Aliphatic α-Hydroxy Ketones by Evolved Transketolase from Geobacillus stearothermophilus. ACS Catalysis, American Chemical Society, 2022, 12, pp.3566-3576. ⟨10.1021/acscatal.1c05140⟩. ⟨hal-03607757⟩



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