Tailoring Protein–Polymer Conjugates as Efficient Artificial Enzymes for Aqueous Asymmetric Aldol Reactions

Zhang, Ningning; Wu, Changzhu

doi:10.1021/acssynbio.2c00387

Cited by 6 publications

(2 citation statements)

References 51 publications

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“…[63] The ArPoly platform allows further tuning of the polymer chain, e. g. by introduction of hydrophobic moieties leading to increased reactivity and selectivity. [64] In addition, the L-proline moiety in the polymer side chain can coordinate copper(II) ions leading to an ArPoly generating an artificial clickase for alkyne-azide coupling. This clickase converted several alkynes and azides completely to the corresponding triazols at a low catalyst loading of 0.157 mol % (referring to the copper content).…”

Section: Case Study 3: Artificial Polyenzymesmentioning

confidence: 99%

“…The change of the protein scaffold to BSA improved the performance of the ArPoly and up to 65 % conversion and 99 % ee were achieved with different arylaldehyde aldol acceptors [63] . The ArPoly platform allows further tuning of the polymer chain, e. g. by introduction of hydrophobic moieties leading to increased reactivity and selectivity [64] . In addition, the L‐proline moiety in the polymer side chain can coordinate copper(II) ions leading to an ArPoly generating an artificial clickase for alkyne‐azide coupling.…”

Section: Artificial Enzymes Using Non‐canonical Amino Acidsmentioning

confidence: 99%

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Artificial Biocatalysis: Quo Vadis?

Ingram,

Oike

2024

ChemCatChem

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Astonishing progress has been achieved in unlocking new‐to‐nature biocatalysis in the past decades. The progress in protein engineering enabled research to efficiently incorporate artificial structural elements into enzyme design. Recent trends include cofactor mimetics, artificial metalloenzymes and non‐canonical amino acids. In this perspective article, we present the state‐of‐the‐art, discuss recent examples and our view on what we call artificial biocatalysis. Although these artificial systems undoubtedly increase the scope of biocatalysis, their applicability remains challenging. Fundamental questions regarding the impact of this research field are addressed in this perspective.

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Section: Case Study 3: Artificial Polyenzymesmentioning

confidence: 99%

Section: Artificial Enzymes Using Non‐canonical Amino Acidsmentioning

confidence: 99%

Artificial Biocatalysis: Quo Vadis?

Ingram,

Oike

2024

ChemCatChem

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

Zhu,

Hu,

et al. 2024

Angewandte Chemie

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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.

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A Supramolecular Approach to Engineering Living Cells with Enzymes for Adaptive and Recyclable Cascade Synthesis

Wang,

Hübner,

Karring

et al. 2024

Angewandte Chemie

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Biocatalytic transformation in nature is inherently dynamic, spontaneous, and adaptive, enabling complex chemical synthesis and metabolism. These processes often involve supramolecular recognition among cells, enzymes, and biomacromolecules, far surpassing the capabilities of isolated cells and enzymes used in industrial synthesis. Inspired by nature, here we design a supramolecular approach to equip living cells with these capacities, enabling recyclable, efficient cascade reactions. Our two‐step "plug‐and‐play" methodology begins by coating Escherichia coli cells with guest‐containing polymers (SupraBAC) via supramolecular charge interactions, followed by the introduction of β‐cyclodextrin‐functionalized host enzymes through host‐guest chemistry, creating a robust cell‐enzyme complex. This supramolecular coating not only protects cells from various stresses, such as UV radiation, heat, and organic solvents, but also facilitates the overexpression of intracellular enzymes and the attachment of extracellular enzymes within and on SupraBAC. This combination results in efficient multienzyme cascade synthesis, enabling two‐ and three‐step reactions in one pot. Importantly, the multienzyme system can be recycled up to five times without significant loss of activity. Our findings introduce a versatile, adaptive supramolecular coating for whole‐cell catalysts, offering a sustainable and efficient solution for complex synthesis in both chemistry and industrial biotechnology.

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Tailoring Protein–Polymer Conjugates as Efficient Artificial Enzymes for Aqueous Asymmetric Aldol Reactions

Cited by 6 publications

References 51 publications

Artificial Biocatalysis: Quo Vadis?

Artificial Biocatalysis: Quo Vadis?

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

A Supramolecular Approach to Engineering Living Cells with Enzymes for Adaptive and Recyclable Cascade Synthesis

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