Designer metalloenzymes for synthetic biology: Enzyme hybrids for catalysis

Jarvis, Amanda G.

doi:10.1016/j.cbpa.2020.06.004

Cited by 33 publications

(17 citation statements)

References 61 publications

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“…Consequently, biohybrid catalysts have been developed whereby the protein backbone binds a chemical catalyst within its chiral environment, enabling new-to-nature reactions with protein-based stereocontrol. 172,173,193 One of the most broadly applied systems in this context utilizes the high affinity of streptavidin toward biotin derivatives ("biotinylated catalysts"). 193 This concept has been exploited to enable a variety of transition-metal-catalyzed reactions like the "Suzukiase", which uses a biotinylated monophosphine palladium complex bound to a streptavidin variant to catalyze asymmetric Suzuki reactions with up to 90% e.e.…”

Section: A Specific Reactionmentioning

confidence: 99%

“…Novel methods to utilize enzymes for transformations unprecedented in nature have been developed to broaden the synthetic applicability of biocatalysis even further. − …”

Section: Reactions New To Nature Catalyzed By Enzymesmentioning

confidence: 99%

“…As previously stated, enzymes might be considered as huge chiral ligands for any catalytically active molecule in the active site, be it an organocatalyst (e.g., coordinated cofactors such as flavins, pyridoxal 5′-phosphate, or thiamine pyrophosphate) or a metal catalyst (e.g., iron in hemes, copper, or zinc). Consequently, biohybrid catalysts have been developed whereby the protein backbone binds a chemical catalyst within its chiral environment, enabling new-to-nature reactions with protein-based stereocontrol. ,, One of the most broadly applied systems in this context utilizes the high affinity of streptavidin toward biotin derivatives (“biotinylated catalysts”) . This concept has been exploited to enable a variety of transition-metal-catalyzed reactions like the “Suzukiase”, which uses a biotinylated monophosphine palladium complex bound to a streptavidin variant to catalyze asymmetric Suzuki reactions with up to 90% e.e.…”

Section: Reactions New To Nature Catalyzed By Enzymesmentioning

confidence: 99%

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Power of Biocatalysis for Organic Synthesis

2021

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Biocatalysis, using defined enzymes for organic transformations, has become a common tool in organic synthesis, which is also frequently applied in industry. The generally high activity and outstanding stereo-, regio-, and chemoselectivity observed in many biotransformations are the result of a precise control of the reaction in the active site of the biocatalyst. This control is achieved by exact positioning of the reagents relative to each other in a fine-tuned 3D environment, by specific activating interactions between reagents and the protein, and by subtle movements of the catalyst. Enzyme engineering enables one to adapt the catalyst to the desired reaction and process. A well-filled biocatalytic toolbox is ready to be used for various reactions. Providing nonnatural reagents and conditions and evolving biocatalysts enables one to play with the myriad of options for creating novel transformations and thereby opening new, short pathways to desired target molecules. Combining several biocatalysts in one pot to perform several reactions concurrently increases the efficiency of biocatalysis even further.

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Section: A Specific Reactionmentioning

confidence: 99%

“…Novel methods to utilize enzymes for transformations unprecedented in nature have been developed to broaden the synthetic applicability of biocatalysis even further. − …”

Section: Reactions New To Nature Catalyzed By Enzymesmentioning

confidence: 99%

Section: Reactions New To Nature Catalyzed By Enzymesmentioning

confidence: 99%

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Power of Biocatalysis for Organic Synthesis

2021

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“…Whilst the field of artificial metalloenzymes is acknowledged as a promising approach to widen the scope of synthetic biology, it is not considered to be 'non-enzymatic'; therefore it falls outside the scope of this review and instead we direct the reader to recent review articles on the topic. [6][7][8][9] Finally, we will outline possible future directions of this emerging field. First, it is important to define the terms 'biocompatible chemistry' and 'bioorthogonal chemistry' in the context of this review.…”

Section: Introductionmentioning

confidence: 99%

Interfacing non-enzymatic catalysis with living microorganisms

et al. 2021

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“…Most of these enzymes are metalloenzymes, where a reaction on either an iron or copper center takes place. Metalloenzymes are highly versatile in nature and catalyze substrate oxidation and reduction reactions efficiently [7][8][9]. In particular, the oxygen-activating mononuclear iron-containing enzymes are useful in this respect.…”

Section: Introductionmentioning

confidence: 99%

Product Distributions of Cytochrome P450 OleTJE with Phenyl-Substituted Fatty Acids: A Computational Study

Lin

Visser

2021

IJMS

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There are two types of cytochrome P450 enzymes in nature, namely, the monooxygenases and the peroxygenases. Both enzyme classes participate in substrate biodegradation or biosynthesis reactions in nature, but the P450 monooxygenases use dioxygen, while the peroxygenases take H2O2 in their catalytic cycle instead. By contrast to the P450 monooxygenases, the P450 peroxygenases do not require an external redox partner to deliver electrons during the catalytic cycle, and also no external proton source is needed. Therefore, they are fully self-sufficient, which affords them opportunities in biotechnological applications. One specific P450 peroxygenase, namely, P450 OleTJE, reacts with long-chain linear fatty acids through oxidative decarboxylation to form hydrocarbons and, as such, has been implicated as a suitable source for the biosynthesis of biofuels. Unfortunately, the reactions were shown to produce a considerable amount of side products originating from Ca and Cb hydroxylation and desaturation. These product distributions were found to be strongly dependent on whether the substrate had substituents on the Ca and/or Cb atoms. To understand the bifurcation pathways of substrate activation by P450 OleTJE leading to decarboxylation, Ca hydroxylation, Cb hydroxylation and Ca-Cb desaturation, we performed a computational study using 3-phenylpropionate and 2-phenylbutyrate as substrates. We set up large cluster models containing the heme, the substrate and the key features of the substrate binding pocket and calculated (using density functional theory) the pathways leading to the four possible products. This work predicts that the two substrates will react with different reaction rates due to accessibility differences of the substrates to the active oxidant, and, as a consequence, these two substrates will also generate different products. This work explains how the substrate binding pocket of P450 OleTJE guides a reaction to a chemoselectivity.

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Designer metalloenzymes for synthetic biology: Enzyme hybrids for catalysis

Cited by 33 publications

References 61 publications

Power of Biocatalysis for Organic Synthesis

Power of Biocatalysis for Organic Synthesis

Interfacing non-enzymatic catalysis with living microorganisms

Product Distributions of Cytochrome P450 OleTJE with Phenyl-Substituted Fatty Acids: A Computational Study

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