Design and Evolution of an Enzyme for the Asymmetric Michael Addition of Cyclic Ketones to Nitroolefins by Enamine Catalysis.

Angew Chem Int Ed Engl

School of Life Sciences and Health Engineering, Jiangnan University, Wuxi, 214122, China.

Published: August 2024

Consistent introduction of novel enzymes is required for developing efficient biocatalysts for challenging biotransformations. Absorbing catalytic modes from organocatalysis may be fruitful for designing new-to-nature enzymes with novel functions. Herein we report a newly designed artificial enzyme harboring a catalytic pyrrolidine residue that catalyzes the asymmetric Michael addition of cyclic ketones to nitroolefins through enamine activation with high efficiency. Diverse chiral γ-nitro cyclic ketones with two stereocenters were efficiently prepared with excellent stereoselectivity (up to 97 % e.e., >20 : 1 d.r.) and good yield (up to 86 %). This work provides an efficient biocatalytic strategy for cyclic ketone functionalization, and highlights the usefulness of artificial enzymes for extending biocatalysis to further non-natural reactions.

Download full-text PDF

Source
http://dx.doi.org/10.1002/anie.202404312DOI Listing

Publication Analysis

Top Keywords

cyclic ketones
12
asymmetric michael
8
michael addition
8
addition cyclic
8
ketones nitroolefins
8
nitroolefins enamine
8
design evolution
4
evolution enzyme
4
enzyme asymmetric
4
cyclic
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!