Synthesis of enantiomerically pure alcohols and amines <i>via</i> biocatalytic deracemisation methods

Musa, Musa; Hollmann, Frank; Mutti, Francesco G.

doi:10.1039/c9cy01539f

Cited by 48 publications

(36 citation statements)

References 130 publications

(177 reference statements)

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“…In this context, several biocatalytic methods to obtain enantiopure α‐chiral amines have been developed, including asymmetric synthesis from prochiral ketones using either ω‐transaminases (ωTA), or dehydrogenases (i. e., reductive aminases (RedAm), imine reductases (IRed), amine dehydrogenases (AmDH); from alkenes using either ammonia lyases or engineered cytochrome c; and from alkanes using engineered cytochrome P411 monooxygenases . Enantiomerically pure amines can also be obtained from a racemic mixture by either kinetic resolution (KR) or applying one among several available deracemisation strategies . KR is based on the use of an enantioselective catalyst that acts exclusively on one enantiomer while leaving the other untouched.…”

Section: Figurementioning

confidence: 99%

“…Additionally, KR is a practical approach to assess the efficiency of a biocatalyst that can possibly then be implemented in a deracemisation method. For instance, KR can be combined with a racemisation catalyst (i. e., dynamic KR using e. g., Pd/C, Pd/AIO(OH), VOSO 4 , Ru or Ir complexes) or a hydride transfer reagent (e. g., NaCNBH 3 , NaBH 4 ) . The applicability of KR and DKR for chiral amine synthesis has been demonstrated using hydrolases, ωTAs,– and monoamine oxidases (MAOs), as well as with AmDHs or RedAms in combination with either a NADH oxidase or an alanine dehydrogenase…”

Section: Figurementioning

confidence: 99%

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Kinetic Resolution of Racemic Primary Amines Using Geobacillus stearothermophilus Amine Dehydrogenase Variant

et al. 2020

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A NADH-dependent engineered amine dehydrogenase from Geobacillus stearothermophilus (LE-AmDH-v1) was applied together with a NADH-oxidase from Streptococcus mutans (NOx) for the kinetic resolution of pharmaceutically relevant racemic α-chiral primary amines. The reaction conditions (e. g., pH, temperature, type of buffer) were optimised to yield Sconfigured amines with up to > 99 % ee. ChemCatChemCommunications

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Section: Figurementioning

confidence: 99%

Section: Figurementioning

confidence: 99%

Kinetic Resolution of Racemic Primary Amines Using Geobacillus stearothermophilus Amine Dehydrogenase Variant

et al. 2020

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“…Alcohol oxidation can also be used to produce ketones as intermediates in biocatalytic cascades that can then be used in subsequent reactions, such those catalyzed by transaminases or amine dehydrogenases in chiral amine synthesis [1,[41][42][43] or by ketoreductases or alcohol dehydrogenases in chiral sec-alcohol synthesis (i.e., deracemization or stereoinversion of sec-alcohols). This approach can be achieved in a one pot cascade if different cofactors are used for the oxidation and reduction ( Figure 6) [44]. Figure 5.…”

Section: Cofactor F420-dependent Reactions With Relevance To Biocatalmentioning

confidence: 99%

Cofactor F420-Dependent Enzymes: An Under-Explored Resource for Asymmetric Redox Biocatalysis

et al. 2019

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The asymmetric reduction of enoates, imines and ketones are among the most important reactions in biocatalysis. These reactions are routinely conducted using enzymes that use nicotinamide cofactors as reductants. The deazaflavin cofactor F420 also has electrochemical properties that make it suitable as an alternative to nicotinamide cofactors for use in asymmetric reduction reactions. However, cofactor F420-dependent enzymes remain under-explored as a resource for biocatalysis. This review considers the cofactor F420-dependent enzyme families with the greatest potential for the discovery of new biocatalysts: the flavin/deazaflavin-dependent oxidoreductases (FDORs) and the luciferase-like hydride transferases (LLHTs). The characterized F420-dependent reductions that have the potential for adaptation for biocatalysis are discussed, and the enzymes best suited for use in the reduction of oxidized cofactor F420 to allow cofactor recycling in situ are considered. Further discussed are the recent advances in the production of cofactor F420 and its functional analog FO-5′-phosphate, which remains an impediment to the adoption of this family of enzymes for industrial biocatalytic processes. Finally, the prospects for the use of this cofactor and dependent enzymes as a resource for industrial biocatalysis are discussed.

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“…This approach can be achieved in a one pot cascade if different cofactors are used for the oxidation and reduction ( Fig. 6) [46].…”

Section: Cofactor F420-dependent Reactions With Relevance To Biocatalmentioning

confidence: 99%

Cofactor F<sub>420</sub>-Dependent Enzymes: An Under-Explored Resource for Asymmetric Redox Biocatalysis

Shah¹,

Antoney²,

Kang³

et al. 2019

Preprint

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Asymmetric reduction of enoates, imines and ketones are among the most important reactions in biocatalysis. These reactions are routinely conducted using enzymes that use nicotinamide cofactors as reductants. The deazaflavin cofactor F420 also has electrochemical properties that make it suitable as an alternative to nicotinamide cofactors for use in asymmetric reduction reactions. However, cofactor F420-dependent enzymes remain under-explored as a resource for biocatalysis. In this review, we consider the cofactor F420-dependent enzyme families with greatest potential for the discovery of new biocatalysts: the flavin/deazaflavin-dependent oxidoreductases (FDORs) and the luciferase-like hydride transferases (LLHTs). We discuss characterized F420-dependent reductions that have potential for adaptation for biocatalysis, and we consider the enzymes best suited for use in the reduction of oxidized cofactor F420 to allow cofactor recycling in situ. We also discuss recent advances in the production of cofactor F420 and its functional analog FO-5’- phosphate, which remains an impediment to the adoption of this family of enzymes for industrial biocatalytic processes. Finally, we discuss the prospects for the use of this cofactor and dependent enzymes as a resource for industrial biocatalysis.

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Synthesis of enantiomerically pure alcohols and amines via biocatalytic deracemisation methods

Abstract: Deracemisation via chemo-enzymatic or multi-enzymatic approaches is the optimum substitute for kinetic resolution, which suffers from the limitation of a theoretical maximum 50% yield albeit high enantiomeric excess is attainable.

Cited by 48 publications

References 130 publications

Kinetic Resolution of Racemic Primary Amines Using Geobacillus stearothermophilus Amine Dehydrogenase Variant

Kinetic Resolution of Racemic Primary Amines Using Geobacillus stearothermophilus Amine Dehydrogenase Variant

Cofactor F420-Dependent Enzymes: An Under-Explored Resource for Asymmetric Redox Biocatalysis

Cofactor F<sub>420</sub>-Dependent Enzymes: An Under-Explored Resource for Asymmetric Redox Biocatalysis

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