Asymmetric Reduction of Cyclic Imines Catalyzed by a Whole‐Cell Biocatalyst Containing an (<i>S</i>)‐Imine Reductase

Leipold, Friedemann; Hussain, Shahed; Ghislieri, Diego; Turner, Nicholas J.

doi:10.1002/cctc.201300539

Cited by 146 publications

(120 citation statements)

References 30 publications

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“…[222] Then ecessity of aqueous reaction media for most enzymatic transformations imposes ar estriction on biocatalytic imine reductions,n amely the use of parent imines that withstand hydrolysis in the aqueous environment. [223] (Figure 76).…”

Section: Reduction Of C=nb Ondsmentioning

confidence: 99%

Enantioselective Chemo‐ and Biocatalysis: Partners in Retrosynthesis

et al. 2017

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Recent developments of stereoselective biocatalytic and chemocatalytic methods are discussed. The review provides a guide to the use of biocatalytic methods in the area of chemical synthesis with focused attention on retrosynthetic considerations and analysis. The transformations presented are organized according to bond disconnections and attendant synthetic methods. The review is expected to lead to better understanding of the characteristics and distinctions of the two complementary approaches. It depicts for researchers in bio- and chemocatalysis a road map of challenges and opportunities for the evolution (and at times revolution) in chemical synthesis.

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Section: Reduction Of C=nb Ondsmentioning

confidence: 99%

Enantioselective Chemo‐ and Biocatalysis: Partners in Retrosynthesis

et al. 2017

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“…Given the significance of chiral amines, their efficient synthesis in enantiopure form has become an attractive challenge to organic chemists and biologists in recent years [2][3][4]. Recently, many biocatalytic methods for the production of chiral amines have been developed using biocatalysts, such as lipase [5], amine oxidase [6], imine reductase [7], transaminase [8], ammonia lyases [9], Pictet-Spenglerase [10], barberine bridge enzyme [11], engineered P450 monooxygenase [12], and amine dehydrogenase (AmDH) [3]. Each enzyme has its own advantages and disadvantages for the synthesis of chiral amines ( [13] and references therein for more details).…”

Section: Introductionmentioning

confidence: 99%

The Kinetic Resolution of Racemic Amines Using a Whole-Cell Biocatalyst Co-Expressing Amine Dehydrogenase and NADH Oxidase

et al. 2017

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Amine dehydrogenase (AmDH) possesses tremendous potential for the synthesis of chiral amines because AmDH catalyzes the asymmetric reductive amination of ketone with high enatioselectivity. Although a reductive application of AmDH is favored in practice, the oxidative route is interesting as well for the preparation of chiral amines. Here, the kinetic resolution of racemic amines using AmDH was first extensively studied, and the AmDH reaction was combined with an NADH oxidase (Nox) to regenerate NAD + and to drive the reaction forward. When the kinetic resolution was carried out with 10 mM rac-2-aminoheptane and 5 mM rac-α-methylbenzylamine (α-MBA) using purified enzymes, the enantiomeric excess (ee) values were less than 26% due to the product inhibition of AmDH by ketone and the inhibition of Nox by the substrate amine. The use of a whole-cell biocatalyst co-expressing AmDH and Nox apparently reduces the substrate and product inhibition, and/or it increases the stability of the enzymes. Fifty millimoles (50 mM) rac-2-aminoheptane and 20 mM rac-α-MBA were successfully resolved into the (S)-form with >99% ee using whole cells. The present study demonstrates the potential of a whole-cell biocatalyst co-expressing AmDH and Nox for the kinetic resolution of racemic amines.

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“…14 These IREDs were shown to be dependent for activity exclusively on the nicotinamide cofactor NADPH, and to exist in solution as homodimers of monomers, each of approximately 30 kDa. Subsequently, Turner and co‐workers have shown that cells of E. coli expressing 3546‐IRED are able to catalyse the asymmetric reduction of a wide range of monocyclic and bicyclic imines, providing a biocatalyst with the potential for the preparation of chiral amine products 15…”

Section: Introductionmentioning

confidence: 99%

Structure, Activity and Stereoselectivity of NADPH‐Dependent Oxidoreductases Catalysing the S‐Selective Reduction of the Imine Substrate 2‐Methylpyrroline

et al. 2015

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Oxidoreductases from Streptomyces sp. GF3546 [3546-IRED], Bacillus cereus BAG3X2 (BcIRED) and Nocardiopsis halophila (NhIRED) each reduce prochiral 2-methylpyrroline (2MPN) to (S)-2-methylpyrrolidine with >95 % ee and also a number of other imine substrates with good selectivity. Structures of BcIRED and NhIRED have helped to identify conserved active site residues within this subgroup of imine reductases that have S selectivity towards 2MPN, including a tyrosine residue that has a possible role in catalysis and superimposes with an aspartate in related enzymes that display R selectivity towards the same substrate. Mutation of this tyrosine residue-Tyr169-in 3546-IRED to Phe resulted in a mutant of negligible activity. The data together provide structural evidence for the location and significance of the Tyr residue in this group of imine reductases, and permit a comparison of the active sites of enzymes that reduce 2MPN with either R or S selectivity.

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Asymmetric Reduction of Cyclic Imines Catalyzed by a Whole‐Cell Biocatalyst Containing an (S)‐Imine Reductase

Cited by 146 publications

References 30 publications

Enantioselective Chemo‐ and Biocatalysis: Partners in Retrosynthesis

Enantioselective Chemo‐ and Biocatalysis: Partners in Retrosynthesis

The Kinetic Resolution of Racemic Amines Using a Whole-Cell Biocatalyst Co-Expressing Amine Dehydrogenase and NADH Oxidase

Structure, Activity and Stereoselectivity of NADPH‐Dependent Oxidoreductases Catalysing the S‐Selective Reduction of the Imine Substrate 2‐Methylpyrroline

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