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Creation of ( R )-Amine Transaminase Activity within an α-Amino Acid Transaminase Scaffold

Abstract : The enzymatic transamination of ketones into (R)-amines represents an important route for accessing a range of pharmaceuticals or building blocks. Although many publications have dealt with enzyme discovery, protein engineering, and the application of (R)-selective amine transaminases [(R)-ATA] in biocatalysis, little is known about the actual in vivo role and how these enzymes have evolved from the ubiquitous a-amino acid transaminases (alpha-AATs). Here, we show the successful introduction of an (R)-transaminase activity in an alpha-amino acid aminotransferase with one to six amino acid substitutions in the enzyme's active site. Bioinformatic analysis combined with computational redesign of the D-amino acid aminotransferase (DATA) led to the identification of a sextuple variant having a specific activity of 326 milliunits mg(-1) in the conversion of (R)-phenylethylamine and pyruvate to acetophenone and b-alanine. This value is similar to those of natural (R)-ATAs, which typically are in the range of 250 milliunits mg(-1). These results demonstrate that (R)-ATAs can evolve from alpha-AAT as shown here for the DATA scaffold.
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Contributor : Suzette Astruc <>
Submitted on : Tuesday, November 24, 2020 - 10:00:26 AM
Last modification on : Wednesday, May 12, 2021 - 8:09:18 AM


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Moritz Voss, Chao Xiang, Jeremy Esque, Alberto Nobili, Marian Menke, et al.. Creation of ( R )-Amine Transaminase Activity within an α-Amino Acid Transaminase Scaffold. ACS Chemical Biology, American Chemical Society, 2020, 15 (2), pp.416-424. ⟨10.1021/acschembio.9b00888⟩. ⟨hal-02529029⟩



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