625-30-9Relevant articles and documents
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Birkofer,L.,Brokmeier,D.
, p. 1325 - 1328 (1968)
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Biochemical and Structural Characterization of an (R)-Selective Transaminase in the Asymmetric Synthesis of Chiral Hydroxy Amines
Li, Fulong,Liang, Youxiang,Wei, Yuwen,Zheng, Yukun,Du, Yan,Yu, Huimin
supporting information, p. 4582 - 4589 (2021/08/07)
An (R)-selective transaminase RbTA with excellent stereoselectivity (>99% ee) in the asymmetric amination of hydroxy ketones was identified. Biochemical characterization showed that RbTA exhibited the highest activity toward 4-hydroxy-2-butanone among reported enzymes, and that it has broad substrate specificity, including for aliphatic, aromatic, and alicyclic ketones. Crystallization of RbTA were performed, as were molecular docking and mutagenesis studies. Residue Tyr125 plays a key role in substrate recognition by forming a hydrogen bond with hydroxy ketone. The applicability of the enzyme was determined in preparative-scale synthesis of (R)-3-amino-1-butanol, demonstrating the potential of RbTA as a green biocatalyst for production of value-added chiral hydroxy amines. This study provides an efficient tool for enzymatic synthesis of chiral hydroxy amines, as well as structural insight into substrate recognition by transaminases in the asymmetric amination of hydroxy ketones. (Figure presented.).
Separate Sets of Mutations Enhance Activity and Substrate Scope of Amine Dehydrogenase
Franklin, Robert D.,Mount, Conner J.,Bommarius, Bettina R.,Bommarius, Andreas S.
, p. 2436 - 2439 (2020/04/16)
Mutations were introduced into the leucine amine dehydrogenase (L-AmDH) derived from G. stearothermophilus leucine dehydrogenase (LeuDH) with the goals of increased activity and expanded substrate acceptance. A triple variant (L-AmDH-TV) including D32A, F101S, and C290V showed an average of 2.5-fold higher activity toward aliphatic ketones and an 8.0 °C increase in melting temperature. L-AmDH-TV did not show significant changes in relative activity for different substrates. In contrast, L39A, L39G, A112G, and T133G in varied combinations added to L-AmDH-TV changed the shape of the substrate binding pocket. L-AmDH-TV was not active on ketones larger than 2-hexanone. L39A and L39G enabled activity for straight-chain ketones as large as 2-decanone and in combination with A112G enabled activity toward longer branched ketones including 5-methyl-2-octanone.