Enzymatic strategies for asymmetric synthesis

Hall, Mélanie

doi:10.1039/d1cb00080b

Cited by 41 publications

(25 citation statements)

References 334 publications

(394 reference statements)

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“…Biocatalysts has proven to be an excellent and greener complement for classical organic synthesis, as the employ of biocatalysts (either native, chemically, or genetically modified) allows very clean and selective procedures [97][98][99][100][101][102][103][104][105][106]. Regarding the biocatalytic synthesis of 1,3-diketones, a straightforward methodology was initially reported in 2010 by Müller and coworkers [107] by using a recombinant enzyme (YpYerE, a thiamine diphosphate (ThDP)-dependent aldolase from Yersinia pseudotuberculosis O:VI).…”

Section: Biocatalytic Synthesis Of 13-diketonesmentioning

confidence: 99%

Recent Developments in the Synthesis of β-Diketones

Gonzalo

Alcántara

2021

Pharmaceuticals

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Apart from being one of the most important intermediates in chemical synthesis, broadly used in the formation of C–C bonds among other processes, the β-dicarbonyl structure is present in a huge number of biologically and pharmaceutically active compounds. In fact, mainly derived from the well-known antioxidant capability associated with the corresponding enol tautomer, β-diketones are valuable compounds in the treatment of many pathological disorders, such as cardiovascular and liver diseases, hypertension, obesity, diabetes, neurological disorders, inflammation, skin diseases, fibrosis, or arthritis; therefore, the synthesis of these structures is an area of overwhelming interest for organic chemists. This paper is devoted to the advances achieved in the last ten years for the preparation of 1,3-diketones, using different chemical (Claisen, hydration of alkynones, decarboxylative coupling) or catalytic (biocatalysis, organocatalytic, metal-based catalysis) methodologies: Additionally, the preparation of branched β-dicarbonyl compounds by means of α-functionalization of non-substituted 1,3-diketones are also discussed.

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Section: Biocatalytic Synthesis Of 13-diketonesmentioning

confidence: 99%

Recent Developments in the Synthesis of β-Diketones

Gonzalo

Alcántara

2021

Pharmaceuticals

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“…Enzymes are ideal catalysts for chemical synthesis because they can precisely control reactive intermediates to provide unparalleled levels of stereoselectivity. However, they cannot be broadly applied to synthetic challenges because they are often assumed to be limited to their native functions. − We recently demonstrated that flavin-dependent “ene”-reductases (EREDs), when irradiated with visible light, can catalyze non-natural free radical reactions. This strategy has proven general and enabled EREDs to solve selectivity challenges in free radical chemistry that are not easily addressed using small-molecule catalysts. − …”

Section: Introductionmentioning

confidence: 99%

Photoenzymatic Catalysis in a New Light: Gluconobacter “Ene”-Reductase Conjugates Possessing High-Energy Reactivity with Tunable Low-Energy Excitation

et al. 2022

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Non-natural light-driven enzymatic reactivity was recently developed to perform the highly stereoselective reactions required for pharmaceutical synthesis. However, photoenzymes require high-intensity light to function because of the poor absorption properties of their photoactive intermediates. Inspired by the modular architecture of photosynthesis, we designed a conjugate composed of a covalently linked photoenzyme and a light antenna to separate light capture from catalysis. Spectroscopic characterization of the conjugate showed the presence of efficient energy transfer from the light-harvesting components to the photoenzyme. In the presence of energy transfer, a ∼4-fold increase in product yield was observed for intramolecular hydroalkylation of alkenes, and reactivity was enabled for intermolecular hydroalkylation of alkenes. These improvements establish the power of incorporating nature’s design into non-natural photoenzymatic catalysis.

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“…Depending on the support on which they are immobilized, enzymes often improve their biochemical and kinetic properties, and, being recyclable, they can also be used in the scale-up of synthetic processes [ 19 , 20 ]. For quite a long time, successful immobilization of biocatalysts has been largely confined to hydrolytic enzymes [ 21 , 22 , 23 ], but this scenario is changing with the development of enzymes for a wider range of biotransformations, including asymmetric reduction, carbon–carbon bond formation, and oxidation [ 24 , 25 , 26 ]. In this regard, increasing attention is paid to amine oxidases, enzymes belonging to the class of oxidoreductases that are widespread in nature (from bacteria to humans).…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Lathyrus cicera Amine Oxidase on Magnetic Microparticles for Biocatalytic Applications

Fabio

Iazzetti

Incocciati

et al. 2022

IJMS

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Amine oxidases are enzymes belonging to the class of oxidoreductases that are widespread, from bacteria to humans. The amine oxidase from Lathyrus cicera has recently appeared in the landscape of biocatalysis, showing good potential in the green synthesis of aldehydes. This enzyme catalyzes the oxidative deamination of a wide range of primary amines into the corresponding aldehydes but its use as a biocatalyst is challenging due to the possible inactivation that might occur at high product concentrations. Here, we show that the enzyme’s performance can be greatly improved by immobilization on solid supports. The best results are achieved using amino-functionalized magnetic microparticles: the immobilized enzyme retains its activity, greatly improves its thermostability (4 h at 75 °C), and can be recycled up to 8 times with a set of aromatic ethylamines. After the last reaction cycle, the overall conversion is about 90% for all tested substrates, with an aldehyde production ranging between 100 and 270 mg depending on the substrate used. As a proof concept, one of the aldehydes thus produced was successfully used for the biomimetic synthesis of a non-natural benzylisoquinoline alkaloid.

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Enzymatic strategies for asymmetric synthesis

Abstract: Enzymes, at the turn of the 21st century, are gaining a momentum. Especially in the field of synthetic organic chemistry, a broad variety of biocatalysts are being applied in an...

Cited by 41 publications

References 334 publications

Recent Developments in the Synthesis of β-Diketones

Recent Developments in the Synthesis of β-Diketones

Photoenzymatic Catalysis in a New Light: Gluconobacter “Ene”-Reductase Conjugates Possessing High-Energy Reactivity with Tunable Low-Energy Excitation

Immobilization of Lathyrus cicera Amine Oxidase on Magnetic Microparticles for Biocatalytic Applications

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