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Showing 1–7 of 7 results
Advanced filters: Author: Gideon Grogan Clear advanced filters

  • Stereogenic-at-sulfur compounds are important biologically active small molecules, with many drugs featuring chiral sulfur atoms. Here, the authors report that unspecific peroxygenases catalyse the biocatalytic oxygenation of sulfilimines and sulfenimines to form enantiomerically enriched sulfoximines and sulfinimines, respectively, on preparative scale.

    • Jiacheng Li
    • Benjamin Melling
    • Gideon Grogan
    ResearchOpen Access
    Nature Communications
    Volume: 17, P: 1-9

  • New enzymes for the efficient and stereoselective synthesis of chiral amines are of high interest for the pharmaceutical industry. Now, Grogan, Vergne-Vaxelaire and co-workers report the discovery, characterization, crystal structure and engineering of a family of native amine dehydrogenases for the preparation of chiral amines from ketones.

    • Ombeline Mayol
    • Karine Bastard
    • Carine Vergne-Vaxelaire
    Research
    Nature Catalysis
    Volume: 2, P: 324-333

  • An enzyme (AspRedAm) capable of coupling carbonyls with a variety of amines in a reductive amination has now been discovered. Kinetic studies revealed that the enzyme catalysed both the imine formation step, as well as the reduction step. Structure and mutagenesis studies have highlighted essential catalytic residues and preparative scale examples have demonstrated total turnover numbers of up to 32,000.

    • Godwin A. Aleku
    • Scott P. France
    • Nicholas J. Turner
    Research
    Nature Chemistry
    Volume: 9, P: 961-969

  • A biocatalytic enzyme originating from bacteria, EneIRED, facilitates amine-activated conjugate alkene reduction followed by reductive amination, efficiently preparing chiral amine diastereomers, which are commonly used in pharmaceuticals and agrochemicals. 

    • Thomas W. Thorpe
    • James R. Marshall
    • Nicholas J. Turner
    Research
    Nature
    Volume: 604, P: 86-91

  • Structural characterization of the bifunctional enzyme linalool dehydratase isomerase and exploration of its substrate scope demonstrate its potential for catalyzing desirable transformations of various tertiary alcohols.

    • Bettina M Nestl
    • Christopher Geinitz
    • Bernhard Hauer
    Research
    Nature Chemical Biology
    Volume: 13, P: 275-281