Design of artificial metalloenzymes for the reduction of nicotinamide cofactors

Basle, Mattias; Padley, Henry A.W.; Martins, Floriane L.; Winkler, G. Sebastiaan; Jäger, Christof M.; Pordea, Anca

doi:10.1016/j.jinorgbio.2021.111446

Cited by 11 publications

(11 citation statements)

References 32 publications

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“…34 Currently, successful cases have been reported in the range of improving protein stability and folding, 34 altering specificity and binding affinity, 35 implanting novel enzymatic activities, and preparing high-ordered assemblies. 36,37 The de novo design process usually starts with an unknown sequence and backbone structure and finally requires the determination of the protein sequence that will fold into a certain structure with novel functionality (Figure 2D). It highly relies on computational tools such as AlphaFold2, 38 Rosetta, 26 and Protein WISDOM.…”

Section: Overview Of the Basic Principles And Strategies Of Protein D...mentioning

confidence: 99%

Advances in Rational Protein Engineering toward Functional Architectures and Their Applications in Food Science

Chen

Dai

et al. 2022

J. Agric. Food Chem.

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Protein biomolecules including enzymes, cagelike proteins, and specific peptides have been continuously exploited as functional biomaterials applied in catalysis, nutrient delivery, and food preservation in food-related areas. However, natural proteins usually function well in physiological conditions, not industrial conditions, or may possess undesirable physical and chemical properties. Currently, rational protein design as a valuable technology has attracted extensive attention for the rational engineering or fabrication of ideal protein biomaterials with novel properties and functionality. This article starts with the underlying knowledge of protein folding and assembly and is followed by the introduction of the principles and strategies for rational protein design. Basic strategies for rational protein engineering involving experienced protein tailoring, computational prediction, computation redesign, and de novo protein design are summarized. Then, we focus on the recent progress of rational protein engineering or design in the application of food science, and a comprehensive summary ranging from enzyme manufacturing to cagelike protein nanocarriers engineering and antimicrobial peptides preparation is given. Overall, this review highlights the importance of rational protein engineering in food biomaterial preparation which could be beneficial for food science.

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Section: Overview Of the Basic Principles And Strategies Of Protein D...mentioning

confidence: 99%

Advances in Rational Protein Engineering toward Functional Architectures and Their Applications in Food Science

Chen

Dai

et al. 2022

J. Agric. Food Chem.

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“…13,[17][18][19] Computational analysis of the dened complexes can also guide the selection of bioconjugation sites in the case of the covalent binding of the metal complex to the protein. 20,21 In other approaches, molecular docking in combination with QM and MD simulations was used to control the activity and selectivity of ArMs by understanding substrate binding affinity, exibility, and orientation. 22,23 Despite the above examples and the similarity of the approach to computational drug design, where chemical structures are non-covalently incorporated within proteins as strongly binding inhibitors, 24 docking is not routinely used in ArM design.…”

Section: Introductionmentioning

confidence: 99%

“…26 In our group, we developed ArMs for the reduction of nicotinamide cofactors, starting from the wild type alcohol dehydrogenase from Thermoanaerobacter brockii (TbADH WT), by covalently binding rhodium piano stool complexes at the place of the catalytic zinc site. 21,27 In this work, we aim to simplify the ArMs by designing catalysts for supramolecular binding to avoid the need for the covalent modication of the protein. So far, ArMs based on supramolecular anchoring rely on systems where a natural affinity between the protein and ligand is a pre-requisite, thereby limiting the protein and/or ligand choice; whereas systematic rational strategies to specically design the metal catalysts for supramolecular anchoring to a selected protein scaffold are yet to be developed.…”

Section: Introductionmentioning

confidence: 99%

“…13,17–19 Computational analysis of the defined complexes can also guide the selection of bioconjugation sites in the case of the covalent binding of the metal complex to the protein. 20,21 In other approaches, molecular docking in combination with QM and MD simulations was used to control the activity and selectivity of ArMs by understanding substrate binding affinity, flexibility, and orientation. 22,23…”

Section: Introductionmentioning

confidence: 99%

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Computationally driven design of an artificial metalloenzyme using supramolecular anchoring strategies of iridium complexes to alcohol dehydrogenase

2022

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“…Co-immobilized amine and formate dehydrogenases were used in the continuous production of chiral amine in a packed bed reactor (Franklin et al, 2021 ). FDH catalysis served as a model for the development of artificial metalloenzymes reducing nicotinamide cofactors resilient to high temperatures, compatible with solvents, and lacking FDH complexity (Basle et al, 2021 ).…”

Section: Introductionmentioning

confidence: 99%

Recombinant Enzymatic Redox Systems for Preparation of Aroma Compounds by Biotransformation

et al. 2021

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The aim of this study was to develop immobilized enzyme systems that reduce carbonyl compounds to their corresponding alcohols. The demand for natural aromas and food additives has been constantly growing in recent years. However, it can no longer be met by extraction and isolation from natural materials. One way to increase the availability of natural aromas is to prepare them by the enzymatic transformation of suitable precursors. Recombinant enzymes are currently being used for this purpose. We investigated trans-2-hexenal bioreduction by recombinant Saccharomyces cerevisiae alcohol dehydrogenase (ScADH1) with simultaneous NADH regeneration by recombinant Candida boidinii formate dehydrogenase (FDH). In a laboratory bioreactor with two immobilized enzymes, 88% of the trans-2-hexenal was transformed to trans-2-hexenol. The initial substrate concentration was 3.7 mM. The aldehyde destabilized ScADH1 by eluting Zn2+ ions from the enzyme. A fed-batch operation was used and the trans-2-hexenal concentration was maintained at a low level to limit the negative effect of Zn2+ ion elution from the immobilized ScADH1. Another immobilized two-enzyme system was used to reduce acetophenone to (S)-1-phenylethanol. To this end, the recombinant alcohol dehydrogenase (RrADH) from Rhodococcus ruber was used. This biocatalytic system converted 61% of the acetophenone to (S)-1-phenylethanol. The initial substrate concentration was 8.3 mM. All enzymes were immobilized by poly-His tag to Ni2+, which formed strong but reversible bonds that enabled carrier reuse after the loss of enzyme activity.

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Design of artificial metalloenzymes for the reduction of nicotinamide cofactors

Cited by 11 publications

References 32 publications

Advances in Rational Protein Engineering toward Functional Architectures and Their Applications in Food Science

Advances in Rational Protein Engineering toward Functional Architectures and Their Applications in Food Science

Computationally driven design of an artificial metalloenzyme using supramolecular anchoring strategies of iridium complexes to alcohol dehydrogenase

Recombinant Enzymatic Redox Systems for Preparation of Aroma Compounds by Biotransformation

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