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Creation of a Tailored Aldolase for the Parallel Synthesis of Sialic Acid Mimetics

Authors

  • Thomas Woodhall,

    1. School of Chemistry, University of Leeds, Leeds, LS2 9JT, UK, Fax: (+44) 113-233-6565
    2. Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT, UK
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  • Gavin Williams Dr.,

    1. Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT, UK
    2. School of Biochemistry and Microbiology, University of Leeds, Leeds, LS2 9JT, UK
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  • Alan Berry Dr.,

    1. Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT, UK
    2. School of Biochemistry and Microbiology, University of Leeds, Leeds, LS2 9JT, UK
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  • Adam Nelson Dr.

    1. School of Chemistry, University of Leeds, Leeds, LS2 9JT, UK, Fax: (+44) 113-233-6565
    2. Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT, UK
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Abstract

original image

Erweiterte Substratspezifität: Eine modifizierte Form der Sialinsäure-Aldolase (E192N) hat eine 640fach höhere Substratspezifität als das Wildtyp-Enzym. Die Ozonolyse der ungesättigten Amide 1 und ein anschließender E192N-vermittelter Schritt wurden für die parallele Synthese von 14 Sialinsäuremimetika der allgemeinen Formel 2 genutzt.

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