Recent Advances in Selective Biocatalytic (Hydrogen Transfer) Reductions

Gonzalo, Gonzalo de; Lavandera, Iván

doi:10.1002/9783527814237.ch8

Cited by 4 publications

(2 citation statements)

References 141 publications

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“…Most of the examples of biocatalytic cascades employing BVMOs have been developed together with alcohol dehydrogenases (ADHs, EC 1.1.1.x), also called ketoreductases (KREDs). These enzymes are able to catalyze the reversible reduction of carbonyl compounds into the corresponding alcohols (Scheme 2), in general with high selectivity [46][47][48][49]. ADHs require the presence of nicotinamide cofactors for performing their activity, being required to employ effective regeneration systems if these enzymes are employed as isolated biocatalysts.…”

Section: Multi-step Reactions Including Alcohol Dehydrogenases/bvmo A...mentioning

confidence: 99%

Multienzymatic Processes Involving Baeyer–Villiger Monooxygenases

Gonzalo

Alcántara

2021

Catalysts

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Baeyer–Villiger monooxygenases (BVMOs) are flavin-dependent oxidative enzymes capable of catalyzing the insertion of an oxygen atom between a carbonylic Csp2 and the Csp3 at the alpha position, therefore transforming linear and cyclic ketones into esters and lactones. These enzymes are dependent on nicotinamides (NAD(P)H) for the flavin reduction and subsequent reaction with molecular oxygen. BVMOs can be included in cascade reactions, coupled to other redox enzymes, such as alcohol dehydrogenases (ADHs) or ene-reductases (EREDs), so that the direct conversion of alcohols or α,β-unsaturated carbonylic compounds to the corresponding esters can be achieved. In the present review, the different synthetic methodologies that have been performed by employing multienzymatic strategies with BVMOs combining whole cells or isolated enzymes, through sequential or parallel methods, are described, with the aim of highlighting the advantages of performing multienzymatic systems, and show the recent advances for overcoming the drawbacks of using BVMOs in these techniques.

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Section: Multi-step Reactions Including Alcohol Dehydrogenases/bvmo A...mentioning

confidence: 99%

Multienzymatic Processes Involving Baeyer–Villiger Monooxygenases

Gonzalo

Alcántara

2021

Catalysts

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“…Among the six different types of biocatalysts according to the type of reaction they catalyze, oxidoreductases (EC 1) are, together with hydrolases, the most employed family of enzymes with synthetic purposes. This large group of enzymes, with 22 types of oxidoreductase subtypes, are involved in all type of redox reactions, catalyzing oxidation and reductions processes [ 8 , 9 , 10 , 11 ]. The application of oxidoreductases to obtain valuable building blocks is a current area of interest in organic synthesis, due to the mild reaction conditions and oxidants/reductants required for their function, combined with the generally exquisite stereoselectivity afforded by this type of catalysts.…”

Section: Introductionmentioning

confidence: 99%

Biocatalyzed Redox Processes Employing Green Reaction Media

Aranda

Gonzalo

2020

Molecules

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The application of biocatalysts to perform reductive/oxidative chemical processes has attracted great interest in recent years, due to their environmentally friendly conditions combined with high selectivities. In some circumstances, the aqueous buffer medium normally employed in biocatalytic procedures is not the best option to develop these processes, due to solubility and/or inhibition issues, requiring biocatalyzed redox procedures to circumvent these drawbacks, by developing novel green non-conventional media, including the use of biobased solvents, reactions conducted in neat conditions and the application of neoteric solvents such as deep eutectic solvents.

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Rationally Engineering the Cofactor Specificity of LfSDR1 for Biocatalytic Synthesis of the Key Intermediate of Telotristat Ethyl

Zhang

Che

et al. 2022

ChemCatChem

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Switching cofactor preference of oxidoreductases from NADPH to NADH by rational engineering, replacing the expensive cofactor NADP + with the cheap cofactor NAD + , is a focus of attention in the industrial application of oxidoreductases. This study focuses on the reversal of cofactor preference for shortchain dehydrogenases/reductases (SDRs). Combined with bioinformatics analyses and in silico analyses, a small and smart mutant library (Mu1-Mu3) of LfSDR1 was rationally designed and constructed. Thus, the excellent NADH-dependent recombinant LfSDR1-V186A/G92V/E141L/G38D/T15A variant (Mu2) was obtained. Meanwhile, novel enzymatic processes for synthesis of the key intermediates [(R)-2 and (S)-4] of telotristat ethyl and crizotinib were successfully created, which mainly relied on Mu2 coupled with an FDH-catalyzed cofactor regeneration system. A co-expressed E. coli whole-cell biocatalyst containing the genes of Mu2 and PpFDH was developed to reduce ketones 1 and 3. Finally, ketone 1 was almost completely converted into the product (R)-2 with a space-time yield of 115.7 g•L À 1 •d À 1 and a 98.8 % ee value.

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Recent Advances in Selective Biocatalytic (Hydrogen Transfer) Reductions

Cited by 4 publications

References 141 publications

Multienzymatic Processes Involving Baeyer–Villiger Monooxygenases

Multienzymatic Processes Involving Baeyer–Villiger Monooxygenases

Biocatalyzed Redox Processes Employing Green Reaction Media

Rationally Engineering the Cofactor Specificity of LfSDR1 for Biocatalytic Synthesis of the Key Intermediate of Telotristat Ethyl

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