Directed Evolution of Nonheme Fe Enzymes for Enantioselective and Regiodivergent 1,3- and 1,4-Nitrogen Migration: Biocatalytic Asymmetric Synthesis of Noncanonical α- and β-Amino Acids
exhibited similar kinetic isotope effects for both 1,5- and 1,6-HAT pathways, suggesting that enzyme engineering controls regio- and enantioselectivity but does not alter the intrinsic transition-state properties of the HAT event. Together, these results further established engineered nonheme Fe enzymes as an excellent platform for the development of stereoselective, synthetically useful non-native biocatalytic transformations.
Authors
- Peng Liu (ORCID: https://orcid.org/0000-0002-8188-632X)
- Huichong Liu
- Shengchun Wang (ORCID: https://orcid.org/0000-0003-3038-3404)
- Ruiqi Ding (ORCID: https://orcid.org/0000-0002-2043-1524)
- Shijia Li (ORCID: https://orcid.org/0000-0001-9310-2978)
- Yang Yang (ORCID: https://orcid.org/0000-0002-4956-2034)
- Liu-Peng Zhao (ORCID: https://orcid.org/0009-0000-5239-8135)
Institutions
- Howard Hughes Medical Institute (US)
- University of California, Santa Barbara (US)
- University of Pittsburgh (US)
Publication Details
- Journal
- Journal of the American Chemical Society
- Published
- 2026-07-27
- DOI
- https://doi.org/10.1021/jacs.6c08775
- Primary Topic
- Enzyme Catalysis and Immobilization
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Science Foundation
- David and Lucile Packard Foundation
- Howard Hughes Medical Institute
- Alfred P. Sloan Foundation
- National Institutes of Health