Imine reductases (IREDs)

Mangas‐Sánchez, Juan; Montgomery, Sarah L.; Aleku, Godwin A.; Man, H.; Sharma, Mahima; Ramsden, Jeremy I.; Grogan, Gideon; Turner, Nicholas J.

doi:10.1016/j.cbpa.2016.11.022

Cited by 225 publications

(163 citation statements)

References 52 publications

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“…As an alternative to traditional chemical methods, biocatalysis is becoming an increasingly desirable option for industry owing to the benefits of sustainable catalyst supply, milder reaction conditions, and the enantioselectivity offered by enzymes. One of the more recent additions to the suite of biocatalysts available for chiral amine synthesis are imine reductases (IREDs), which catalyze the asymmetric reduction of prochiral imines by using the cofactor NADPH (Figure a) . It has also been shown that, as well as the reduction of preformed imines, certain enzymes of this class can also enable reductive amination between a carbonyl and amine substrate .…”

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confidence: 99%

Identification of Novel Bacterial Members of the Imine Reductase Enzyme Family that Perform Reductive Amination

et al. 2018

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Reductive amination of carbonyl compounds constitutes one of the most efficient ways to rapidly construct chiral and achiral amine frameworks. Imine reductase (IRED) biocatalysts represent a versatile family of enzymes for amine synthesis through NADPH‐mediated imine reduction. The reductive aminases (RedAms) are a subfamily of IREDs that were recently shown to catalyze imine formation as well as imine reduction. Herein, a diverse library of novel enzymes were expressed and screened as cell‐free lysates for their ability to facilitate reductive amination to expand the known suite of biocatalysts for this transformation and to identify more enzymes with potential industrial applications. A range of ketones and amines were examined, and enzymes were identified that were capable of accepting benzylamine, pyrrolidine, ammonia, and aniline. Amine equivalents as low as 2.5 were employed to afford up to >99 % conversion, and for chiral products, up to >98 % ee could be achieved. Preparative‐scale reactions were conducted with low amine equivalents (1.5 or 2.0) of methylamine, allylamine, and pyrrolidine, achieving up to >99 % conversion and 76 % yield.

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Identification of Novel Bacterial Members of the Imine Reductase Enzyme Family that Perform Reductive Amination

et al. 2018

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“…Since then, IREDs have rapidly assumed an important role as highly stereoselective catalysts for amine synthesis. [18][19][20][21][22][23][24] IREDs strictly require NADPH and are preferentially used in cellular systems, which makes them very suitable for application in photosynthesis-driven whole-cell biotransformations.…”

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Stereoselective Biotransformations of Cyclic Imines in Recombinant Cells of Synechocystis sp. PCC 6803

et al. 2019

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Light-driven biotransformations in recombinant cyanobacteria allow to employ photosynthetic water-splitting for cofactorregeneration and thus, to save the use of organic electron donors. The genes of three recombinant imine reductases (IREDs) were expressed in the cyanobacterium Synechocystis sp. PCC 6803 and eight cyclic imine substrates were screened in whole-cell biotransformations. While initial reactions showed low to moderate rates, optimization of the reaction conditions in combination with promoter engineering allowed to alleviate toxicity effects and achieve full conversion of prochiral imines with initial rates of up to 6.3 mM h À 1 . The high specific activity of up to 22 U g CDW À 1 demonstrates that recombinant cyanobacteria can provide large amounts of NADPH during whole cell reactions. The excellent optical purity of the products with up to > 99 %ee underlines the usefulness of cyanobacteria for the stereoselective synthesis of amines.Biocatalysis has emerged as important catalytic technology with significant contributions for the development of clean reactions. [1] A large number of biocatalytic processes employ [a] H.

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“…[12] Only ah andful of examples have been reported involving enantioselective transformations with modest enantiomeric excess. [16][17][18][19][20][21][22][23][24] These enzymes have also been combined in cascades to carry out multiple transformations in one pot, often with the oxidation and reduction steps taking place concurrently. [16][17][18][19][20][21][22][23][24] These enzymes have also been combined in cascades to carry out multiple transformations in one pot, often with the oxidation and reduction steps taking place concurrently.…”

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Direct Alkylation of Amines with Primary and Secondary Alcohols through Biocatalytic Hydrogen Borrowing

et al. 2017

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The reductive aminase from Aspergillus oryzae (AspRedAm) was combined with a single alcohol dehydrogenase (either metagenomic ADH-150, an ADH from Sphingobium yanoikuyae (SyADH), or a variant of the ADH from Thermoanaerobacter ethanolicus (TeSADH W110A)) in a redox-neutral cascade for the biocatalytic alkylation of amines using primary and secondary alcohols. Aliphatic and aromatic secondary amines were obtained in up to 99 % conversion, as well as chiral amines directly from the racemic alcohol precursors in up to >97 % ee, releasing water as the only byproduct.

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Imine reductases (IREDs)

Cited by 225 publications

References 52 publications

Identification of Novel Bacterial Members of the Imine Reductase Enzyme Family that Perform Reductive Amination

Identification of Novel Bacterial Members of the Imine Reductase Enzyme Family that Perform Reductive Amination

Stereoselective Biotransformations of Cyclic Imines in Recombinant Cells of Synechocystis sp. PCC 6803

Direct Alkylation of Amines with Primary and Secondary Alcohols through Biocatalytic Hydrogen Borrowing

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