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Bioprospecting Reveals Class III ω-Transaminases Converting Bulky Ketones and Environmentally Relevant Polyamines

    1. [1] Consejo Superior de Investigaciones Científicas

      Consejo Superior de Investigaciones Científicas

      Madrid, España

    2. [2] Bangor University

      Bangor University

      Bangor, Reino Unido

    3. [3] Universidad CEU San Pablo

      Universidad CEU San Pablo

      Madrid, España

    4. [4] b Institute of Molecular Enzyme Technology, Heinrich Heine University Düsseldorf and Forschungszentrum Jülich GmbH, Jülich, Germany
    5. [5] c NORCE Norwegian Research Centre AS, Bergen, Norway
    6. [6] g Bayer AG, Engineering and Technology Department, Leverkusen, Germany
    7. [7] h Institute for Biological Resources and Marine Biotechnology (IRBIM-CNR), Messina, Italy; i Immanuel Kant Baltic Federal University, Kaliningrad, Russia
  • Localización: Applied and Environmental Microbiology, ISSN 0099-2240, Vol. 85, Nº 2, 2019
  • Idioma: inglés
  • Enlaces
  • Resumen
    • Amine transaminases of the class III ω-TAs are key enzymes for modification of chemical building blocks, but finding those capable of converting bulky ketones and (R) amines is still challenging. Here, by an extensive analysis of the substrate spectra of 10 class III ω-TAs, we identified a number of residues playing a role in determining the access and positioning of bulky ketones, bulky amines, and (R)- and (S) amines, as well as of environmentally relevant polyamines, particularly putrescine. The results presented can significantly expand future opportunities for designing (R)-specific class III ω-TAs to convert valuable bulky ketones and amines, as well as for deepening the knowledge into the polyamine catabolic pathways.


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