InspIRED by Nature: NADPH-Dependent Imine Reductases (IREDs) as Catalysts for the Preparation of Chiral Amines. (Q53649779)

16 May 2018

title

InspIRED by Nature: NADPH-Dependent Imine Reductases (IREDs) as Catalysts for the Preparation of Chiral Amines. (English)

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16 May 2018

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Gideon Grogan

1

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16 May 2018

Nicholas J Turner

series ordinal

2

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16 May 2018

language of work or name

English

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publication date

15 December 2015

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16 May 2018

Chemistry—A European Journal

published in

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16 May 2018

Structure, dynamics, and catalytic function of dihydrofolate reductase

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Two Structures of a Thiazolinyl Imine Reductase from Yersinia enterocolitica Provide Insight into Catalysis and Binding to the Nonribosomal Peptide Synthetase Module of HMWP1

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Asymmetric synthesis of chiral cyclic amine from cyclic imine by bacterial whole-cell catalyst of enantioselective imine reductase

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Purification and characterization of a novel (R)-imine reductase from Streptomyces sp. GF3587.

21 January 2018

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A NADPH-dependent (S)-imine reductase (SIR) from Streptomyces sp. GF3546 for asymmetric synthesis of optically active amines: purification, characterization, gene cloning, and expression.

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An (R)-Imine Reductase Biocatalyst for the Asymmetric Reduction of Cyclic Imines

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

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Engineering an enantioselective amine oxidase for the synthesis of pharmaceutical building blocks and alkaloid natural products

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Structure and activity of NADPH-dependent reductase Q1EQE0 from Streptomyces kanamyceticus, which catalyses the R-selective reduction of an imine substrate

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Pteridine reductase mechanism correlates pterin metabolism with drug resistance in trypanosomatid parasites

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

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Enzyme Toolbox: Novel Enantiocomplementary Imine Reductases

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Development of an R -Selective Amine Oxidase with Broad Substrate Specificity and High Enantioselectivity

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21 January 2018

Identifiers

DOI

10.1002/CHEM.201503954

1 reference

16 May 2018

PubMed ID

26667842

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16 May 2018