Journal
ACS CATALYSIS
Volume 10, Issue 14, Pages 7950-7957Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.0c01895
Keywords
amino acids; 2-ketoacids; enzymatic cascade; transaminase; bioinformatic enzyme discovery
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Funding
- National Key R&D Program of China [2018YFA0901600]
- National Natural Science Foundation of China [31822002]
- Biological Resources Programme from the Chinese Academy of Sciences [KFJ-BRP-009]
- Key Research Program of Frontier Sciences from the Chinese Academy of Sciences [ZDBS-LY-SM014]
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The use of 2-ketoacids is very common in feeds, food additives, and pharmaceuticals, and 2-ketoacids are valuable precursors for a plethora of chemically diverse compounds. Biocatalytic synthesis of 2-ketoacids starting from L-amino acids would be highly desirable because the substrates are readily available from biomass feedstock. Here, we report bioinformatic exploration of a series of aminotransferases (ATs) to achieve the desired conversion. Thermodynamic control was achieved by coupling an L-glutamate oxidation reaction in the cascade for the recycling of the amine acceptor. These enzymes were able to convert a majority of proteinogenic amino acids into the corresponding 2-ketoacids with high conversion (up to 99%) extendable, and one-pot two-step processes were established for the synthesis of D-amino acids and N-methylated amino acids, achieving great overall conversion (up to 99%) and high ee values (>99%). These developed enzymatic methodologies offer convenient routes for utilizing amino acids as synthetic reagents.
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