Enzymatic Dynamic Kinetic Resolution of Oxazinones: A New Approach to Enantiopure β<sup>2</sup>‐Amino Acids

Berkessel, Albrecht; Jurkiewicz, Ilona; Mohan, Resmi

doi:10.1002/cctc.201000343

Cited by 33 publications

(14 citation statements)

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“…An alternative DKR running in an organic medium is based on an organocatalytic racemization with a tertiary amine and an enzymatic acylation, furnishing β -2-amino acid derivatives with quantitative conversion in all cases and with up to 96% e.e. when starting from racemic oxazinones 41 . Further DKR processes via combination of organic bases and hydrolases have been developed, which were extensively reviewed earlier 19,42 .…”

Section: Review Articlementioning

confidence: 99%

Opportunities and challenges for combining chemo- and biocatalysis

et al. 2018

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N ature has evolved highly efficient systems in the form of cascade reactions, which assemble the metabolic networks that support life (growth and survival). The basic principle of cascade reactions is also frequently used in biocatalysis, using enzymes in isolation, as well as in combination with chemocatalysts (see Fig. 1 and Box 1 for definition of terms) [1][2][3][4][5][6][7] . As there is no need for purification and isolation of intermediates, operating time, production costs and waste are reduced, and concomitantly, overall yields are improved. In addition, the problem of unstable or difficult to handle intermediates can be overcome, and reactivity as well as selectivity can be enhanced by avoiding unfavourable reaction equilibria through the cooperative effects of multiple catalysts 8 . Starting in the 1980s, the early examples of the combination of chemo-and biocatalysts were reported by the van Bekkum group, who pioneered the development of a process to make the sugar substitute d-mannitol from readily available d-glucose through the combination of a heterogeneous metal-catalysed hydrogenation and an enzyme-catalysed isomerization 9 . The first broadly applied technology for the combination of enzyme and metalcatalysts, which was the research subject of many academic groups as well as industry, emerged in the 1990s from the Williams group 10,11 and aimed to achieve higher yields than classical kinetic resolution of racemates, thus overcoming the limitation of a maximum yield of 50% in the latter case. A prominent example of work that developed this theme is the combination of lipase-catalysed kinetic resolution via acylation of secondary alcohols with Pd-or Rh-catalysed racemization via reversible transfer hydrogenation to achieve a dynamic kinetic resolution (DKR) [12][13][14] . This example was facilitated in part because lipases are active and stable in organic solvents. Later, for instance, Turner's group combined a monoamine oxidase-catalysed imine formation with a chemical reduction 15 to achieve the 100% theoretical yield through a deracemization process. In addition to the combination of metalcatalysis with enzymes, organocatalysis, electrochemistry and light-induced reaction couples have since then been studied extensively, going far beyond the scope of a DKR.The challenges to combining chemo-and biocatalysis in cascades (see Box 1 for definitions and Table 1) can be daunting, not least the requirement for the chemical step to occur in the presence of water, the preferred solvent for enzymes 3 . This Review therefore highlights recent examples of the combination of chemo-and biocatalysts in aqueous multistep syntheses, and looks at how to overcome limitations by, for example, design of appropriate reaction conditions, protein engineering and advanced reactor concepts. Furthermore, trends such as the integration of transition metalcatalysis into microorganisms and the introduction of novel chemistry into engineered enzymes are discussed, and a critical assessment of the impact of this research ...

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Section: Review Articlementioning

confidence: 99%

Opportunities and challenges for combining chemo- and biocatalysis

et al. 2018

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“…Recent examples are the CAL-B-catalyzed transesterification of oxazinones [67] and azlactones [68] using Et 3 N, the hydrolysis of ibuprofen methyl ester employing lipase from Candida rugosa (CRL) at basic pH, [69] and the CAL-B-mediated hydrolysis of methyl 2,3-dihydrobenzo[b]furan-3-carboxylate derivatives in the presence of a diazaphosphorine base. [70] Recently, another interesting approach was proposed by Wiggins and Bielawski, [71] who employed ultrasonication to racemize poly(methylacrylate) chains with binol as pendant groups (Scheme 7a).…”

Section: Using Lipases and Esterasesmentioning

confidence: 99%

Why Leave a Job Half Done? Recent Progress in Enzymatic Deracemizations

Díaz‐Rodríguez¹,

Lavandera

Gotor³

2015

CGC

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Abstract. In recent years the usefulness of enzymatic systems to obtain a single stereoisomerically pure compound starting from a racemate has been expanded. Moreover, current advances in protein engineering, molecular biology and modeling tools are the basis to improve the catalytic properties of enzymes to face novel synthetic challenges. Also, medium engineering and novel immobilization methods of (bio)catalysts are enhancing the productivity of biocatalytic processes making them suitable for being scalable. The development of multienzymatic protocols and the combination of enzymes with other catalysts are providing a wide range of synthetic possibilities that are expanding the scope of these transformations even at industrial scale. Herein we will describe an overview of recent (chemo)enzymatic deracemizations, focusing on the strategy employed (dynamic kinetic resolution, stereoinversion, cyclic deracemization or enantioconvergent process), the type of substrate (e.g., alcohols, amines, carboxylic acid derivatives or carbonylic compounds), and the biocatalyst(s) used.

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“…Such a dynamic kinetic resolution process was successfully developed by the Berkessel group when starting from racemic 5-substituted oxazinones 35. [64] These substrates contain an activated C-H bond at the AE-position with respect to the carbonyl group, suitable for racemization by means of triethylamine. Combination of this racemization with a lipase-catalyzed enantioselective alcoholysis (ring-opening) reaction then leads to the formation of â 2 -amino acid derivatives (R)-36 (Scheme 17).…”

Section: Combination Of (Nonfunctionalized) Tertiary Amines With Biocmentioning

confidence: 99%

3.8.2 Merging of Metal, Organic, and Enzyme Catalysis

Faber¹,

Fessner²,

Turner³

2015

Biocatalysis in Organic Synthesis 3

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Biotransformations are a valuable tool in organic synthesis, with a long-standing "track record" and an increasing tendency to be used for industrial-scale applications. [1][2][3] Whereas for many decades biocatalysis had rarely been integrated in organic synthetic reaction sequences and had long been considered more as a niche technology in organic synthesis, recently, an increased number of applications of biocatalysis in organic multistep synthesis can be seen, thus enabling alternative de novo approaches to, for example, structurally complex drug molecules, natural products, and fine chemicals. Although such biotransformations are considered to be valuable key steps, complementing the existing "classic" organic reactions as well as chemocatalytic reactions in an advantageous fashion, enzymatic reactions are still often treated as a "stand alone" reaction, which requires workup, isolation, and purification of the substrate required for the biotransformation as well as the product resulting from the biotransformation. In terms of both efficiency and sustainability it would be desirable to integrate biocatalysis more in so-called one-pot processes, which combine reactions without the need to work up intermediates. In doing so, overall solvent consumption as well as waste product formation resulting from downstreamprocessing unit operations can be dramatically decreased and space-time yield can be significantly improved. A prerequisite for such one-pot processes is compatibility of the reaction steps with each other; since enzymes (using water as the "natural solvent of choice") and chemocatalysts (running usually in an organic solvent as the typical "chemists solvent of choice") often have been considered to be poorly compatible or even incompatible, development of chemoenzymatic one-pot processes has been neglected for a long time. However, such catalytic disciplines can be combined with each other and pioneering work in this research area has already illustrated the high potential of this approach to develop more efficient multistep processes, fulfilling economic as well as sustainability requirements. Notably, enzymes as catalysts have turned out to be compatible with a broad range of man-made chemocatalysts, including heterogeneous as well as homogeneous catalysts, and metal catalysts as well as organocatalysts. This review will present an overview of major achievements in this field, noting that only a selection of them can be described herein. Earlier reviews in this field, written from different perspectives, are also available. [4][5][6][7] 3.8.2.1 Merging Metal Catalysis with BiocatalysisA major part of organic chemistry today is related to metal-catalyzed transformations, which are both highly efficient and, in many cases, highly selective. [8][9][10] Notably, in terms of their application range, metal catalysis and enzyme catalysis often complement each other. With respect to chemoenzymatic one-pot processes, combining reactions that cannot be achieved by either discipline alone is of particular inter...

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Enzymatic Dynamic Kinetic Resolution of Oxazinones: A New Approach to Enantiopure β²‐Amino Acids

Cited by 33 publications

References 31 publications

Opportunities and challenges for combining chemo- and biocatalysis

Opportunities and challenges for combining chemo- and biocatalysis

Why Leave a Job Half Done? Recent Progress in Enzymatic Deracemizations

3.8.2 Merging of Metal, Organic, and Enzyme Catalysis

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Enzymatic Dynamic Kinetic Resolution of Oxazinones: A New Approach to Enantiopure β2‐Amino Acids

Cited by 33 publications

References 31 publications

Opportunities and challenges for combining chemo- and biocatalysis

Opportunities and challenges for combining chemo- and biocatalysis

Why Leave a Job Half Done? Recent Progress in Enzymatic Deracemizations

3.8.2 Merging of Metal, Organic, and Enzyme Catalysis

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Enzymatic Dynamic Kinetic Resolution of Oxazinones: A New Approach to Enantiopure β²‐Amino Acids