A Single Enzyme in Enantiocomplementary Synthesis of β-Nitroalcohols: Bidirectional Catalysis by Hydroxynitrile Lyase.

Autor: Rana S; Biocatalysis and Enzyme Engineering Laboratory, Department of Biochemistry, School of Life Sciences, University of Hyderabad, Hyderabad, 500 046, India., Chatterjee A; Biocatalysis and Enzyme Engineering Laboratory, Department of Biochemistry, School of Life Sciences, University of Hyderabad, Hyderabad, 500 046, India., Kumar Padhi S; Biocatalysis and Enzyme Engineering Laboratory, Department of Biochemistry, School of Life Sciences, University of Hyderabad, Hyderabad, 500 046, India.
Jazyk: angličtina
Zdroj: Chembiochem : a European journal of chemical biology [Chembiochem] 2024 Nov 04; Vol. 25 (21), pp. e202400618. Date of Electronic Publication: 2024 Sep 12.
DOI: 10.1002/cbic.202400618
Abstrakt: A single enzyme, Baliospermum montanum hydroxynitrile lyase (BmHNL), without alteration, enabled bidirectional catalysis in enantiocomplementary synthesis of chiral β-nitroalcohols. BmHNL catalyzed promiscuous Henry (24 examples) and retro-Henry reaction (22 examples) provided up to >99 % and 50 % conversion to (S)- and (R)-β-nitroalcohols respectively, while both cases displayed up to >99 % ee. The broad substrate scope and high stereoselectivity of BmHNL represents its synthetic applications in sustainable production of diverse chiral β-nitroalcohols. Kinetic parameters of BmHNL was determined for Henry and retro-Henry reaction, which reveals poor catalytic efficiency for both the promiscuous transformations, however, the former has better efficiency than the latter. Practical applicability of the biocatalyst and transformation was illustrated by preparative scale synthesis of chiral intermediates of (S)-Tembamide, and (S)-Micanozole.
(© 2024 Wiley-VCH GmbH.)
Databáze: MEDLINE
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