Work

Nicotinamide Cofactor Biomimetics: Design and Structure Activity Relationships

Year: 2025

Type: article

Abstract: High Resolution Image Download MS PowerPoint Slide Biocatalysis is an attractive methodology due to its sustainable metrics, combined with its vaunted regio-, chemo-, and stereoselectivity. Among biocatalysts, oxidoreductases catalyze redox transformations on a wide variety of substrates and are thus particularly attractive for synthetic applications. Many oxidoreductases depend on nicotinamide-based cofactors; however, the high cost and poor atom economy of such cofactors can negate the advantage of biosynthetic processes. The native cofactors (i.e., NADH or NADPH) can be replaced by nicotinamide cofactor biomimetics (NCBs) to address these issues. Additionally, NCBs can enhance enzyme activity due to structures with expanded redox properties. These capabilities open possibilities for reactivity and biorthogonality. Thus, the field has responded with new NCB structures, including variation in their electronic and molecular recognition properties. This perspective focuses on structure-activity relationships of simple NCBs, including their function, stability, and other properties, along with methods for their regeneration in biosynthesis.

Source: ACS Catalysis

DOI: 10.1021/acscatal.5c03814

Authors: Karissa C. Kenney, Tyler P. LaFortune, Gregory A. Weiss

Institution: University of California, Irvine

Language: English

Topic: Enzyme Catalysis and Immobilization

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $4,500

Funder: Advanced Research Projects Agency - Energy