Journal ArticleDOI
Synthetic cascades are enabled by combining biocatalysts with artificial metalloenzymes
Valentin Köhler,Yvonne M. Wilson,Marc Dürrenberger,Diego Ghislieri,Ekaterina Churakova,Tommaso Quinto,Livia Knörr,Daniel Häussinger,Frank Hollmann,Nicholas J. Turner,Thomas R. Ward +10 more
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An artificial transfer hydrogenase, based on the incorporation of a biotinylated iridium-piano-stool complex in streptavidin, is shown to be fully compatible with a range of biocatalysts and enables the concurrent interplay with oxidative enzymes.Abstract:
Enzymatic catalysis and homogeneous catalysis offer complementary means to address synthetic challenges, both in chemistry and in biology. Despite its attractiveness, the implementation of concurrent cascade reactions that combine an organometallic catalyst with an enzyme has proven challenging because of the mutual inactivation of both catalysts. To address this, we show that incorporation of a d(6)-piano stool complex within a host protein affords an artificial transfer hydrogenase (ATHase) that is fully compatible with and complementary to natural enzymes, thus enabling efficient concurrent tandem catalysis. To illustrate the generality of the approach, the ATHase was combined with various NADH-, FAD- and haem-dependent enzymes, resulting in orthogonal redox cascades. Up to three enzymes were integrated in the cascade and combined with the ATHase with a view to achieving (i) a double stereoselective amine deracemization, (ii) a horseradish peroxidase-coupled readout of the transfer hydrogenase activity towards its genetic optimization, (iii) the formation of L-pipecolic acid from L-lysine and (iv) regeneration of NADH to promote a monooxygenase-catalysed oxyfunctionalization reaction.read more
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NADPH-dependent Secondary Amine Organocatalysis hosted by a Nucleotide-binding Domain
TL;DR: A generic design strategy is reported that allows generation of a NADPH-dependent hybrid catalyst whose action is orchestrated by a secondary amine; this system recruits a reaction mode not commonly seen among enzymes, whilst involving an intricate cofactor that cannot be used by existing organocatalysts.
Journal ArticleDOI
In Vivo Biocatalytic Cascades Featuring an Artificial‐Enzyme‐Catalysed New‐to‐Nature Reaction**
TL;DR: In this paper , an in vivo biocatalytic cascade is augmented with an artificial enzyme-catalysed new-to-nature reaction, which is a p-aminophenylalanine (pAF)-containing evolved variant of the lactococcal multidrug-resistance regulator, designated LmrR_V15pAF_RMH.
Amine Transaminases in Multi-Step One-Pot Reactions
TL;DR: Amine transaminases are enzymes that catalyze the mild and selective formation of primary amines, which are useful building blocks for biologically active compounds and natural products.
Journal ArticleDOI
Multifunctional Integrated Compartment Systems for Incompatible Pickering Interfacial Catalysis Cascade Reactions Based on Responsive Core–Shell Nanoparticles
Tommy Ngai,Yongkang Xi,Shuxin Wang,Bo Liu,Shuheng Wei,Lukas Zeininger,Shou-Wei Yin,Xiao-Quan Yang +7 more
TL;DR: In this article , combined cascade reactions can expand the scope of single catalytic reactions, offering methods for reducing the production isolation steps, downstream processing costs, and reaction equilibria transformation times.
Journal ArticleDOI
Advances in the One-Step Approach of Polymeric Materials Using Enzymatic Techniques
TL;DR: In this paper , a review analyzes more and deeper strategies and material technologies widely used in multi-enzyme cascade platforms for engineering polymer materials, as well as their potential industrial applications.
References
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Journal ArticleDOI
Improvement of enzyme activity, stability and selectivity via immobilization techniques
Cesar Mateo,Jose M. Palomo,Gloria Fernández-Lorente,Jose M. Guisan,Roberto Fernandez-Lafuente +4 more
TL;DR: In all cases, enzyme engineering via immobilization techniques is perfectly compatible with other chemical or biological approaches to improve enzyme functions and the final success depend on the availability of a wide battery of immobilization protocols.
Journal ArticleDOI
Concurrent tandem catalysis
Journal ArticleDOI
Synthetic protein scaffolds provide modular control over metabolic flux
John E. Dueber,Gabriel C. Wu,G Reza Malmirchegini,G Reza Malmirchegini,Tae Seok Moon,Christopher J. Petzold,Christopher J. Petzold,Adeeti Ullal,Kristala L. J. Prather,Jay D. Keasling +9 more
TL;DR: In this article, synthetic protein scaffolds bearing interaction domains from metazoan signaling proteins were used to spatially recruit metabolic enzymes in a designable manner, and the modularity of these domains enabled them to optimize the stoichiometry of three mevalonate biosynthetic enzymes recruited to a synthetic complex.
Journal ArticleDOI
Understanding enzyme immobilisation
TL;DR: This tutorial review focuses on the understanding of enzyme immobilisation, which can address the issue of enzymatic instability.
Journal ArticleDOI
Advances in enzyme immobilisation
TL;DR: Improvements in current strategies for carrier-based immobilisation have been developed using hetero-functionalised supports that enhance the binding efficacy and stability through multipoint attachment, and promise to enhance the roles of immobilisation enzymes in industry, while opening the door for novel applications.