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Enzymatic Synthesis of Aliphatic Acyloins Catalyzed by Thermostable Transketolase
- Source :
- ChemCatChem, ChemCatChem, Wiley, 2020, ⟨10.1002/cctc.202001160⟩
- Publication Year :
- 2020
- Publisher :
- HAL CCSD, 2020.
-
Abstract
- International audience; 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 with enhanced activities for substrate combinations of aliphatic aldehydes as acceptors together with aliphatic pyruvate homologues as donors. The TKgst single variant L382F was able to catalyze efficiently the transfer of the ketol group from hydroxypyruvate on all targeted aliphatic aldehydes (C3−C8) to give the corresponding 1,3‐dihydroxy ketones with good yields and excellent enantioselectivity. The combination of the H102L/H474S mutation previously designed for the improved utilization of aliphatic pyruvate homologues together with a F435I exchange gave the new variant H102L/H474S/F435I, which is able to transfer the acyl goup of 2‐oxobutyrate and 2‐oxovalerate to aliphatic aldehydes, giving mono hydroxylated ketones.
- Subjects :
- 010405 organic chemistry
Chemistry
Stereochemistry
Organic Chemistry
Mutagenesis
Substrate (chemistry)
New variant
Enzymatic synthesis
Transketolase
010402 general chemistry
01 natural sciences
Catalysis
0104 chemical sciences
Inorganic Chemistry
Biocatalysis
[CHIM]Chemical Sciences
Geobacillus stearothermophilus
Physical and Theoretical Chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 18673899
- Database :
- OpenAIRE
- Journal :
- ChemCatChem, ChemCatChem, Wiley, 2020, ⟨10.1002/cctc.202001160⟩
- Accession number :
- edsair.doi.dedup.....2bec689b8cffbb4a37fc0b6f14430fce