• Open Access

Tight Binding of Transition-State Analogues to a Peptidyl-Aminoacyl-L/D-Isomerase from Frog Skin

Authors

  • Verena Gehmayr,

    1. Institute of Organic Chemistry, Johannes Kepler University Linz, Altenberger Strasse 69, 4040 Linz (Austria)
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  • Christa Mollay,

    1. Institute of Molecular Biology, Austrian Academy of Sciences, Billrothstrasse 11, 5020 Salzburg (Austria)
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  • Lorenz Reith,

    1. Institute of Organic Chemistry, Johannes Kepler University Linz, Altenberger Strasse 69, 4040 Linz (Austria)
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  • Prof. Dr. Norbert Müller,

    1. Institute of Organic Chemistry, Johannes Kepler University Linz, Altenberger Strasse 69, 4040 Linz (Austria)
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  • Dr. Alexander Jilek

    Corresponding author
    1. Chair of Bioinformatics, Department of Biotechnology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna (Austria)
    2. Institute of Organic Chemistry, Johannes Kepler University Linz, Altenberger Strasse 69, 4040 Linz (Austria)
    3. Institute of Molecular Biology, Austrian Academy of Sciences, Billrothstrasse 11, 5020 Salzburg (Austria)
    • Chair of Bioinformatics, Department of Biotechnology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna (Austria)
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Abstract

original image

Changing hands: In the biosynthesis of bombinin H, an isomerase catalyses the inversion of chirality of an amino acid in peptide linkage through a deprotonation/protonation mechanism. We have synthesized two substrate analogues (1) that are potent inhibitors of the enzyme reaction. Our results strongly support a planar transition state, such as an enolate anion intermediate (2).

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