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

Author:

Coscolín Cristina1,Katzke Nadine2,García-Moyano Antonio3,Navarro-Fernández José1,Almendral David1,Martínez-Martínez Mónica1,Bollinger Alexander2,Bargiela Rafael4,Gertler Christoph4,Chernikova Tatyana N.4,Rojo David5,Barbas Coral5ORCID,Tran Hai4,Golyshina Olga V.46,Koch Rainhard7,Yakimov Michail M.89ORCID,Bjerga Gro E. K.3,Golyshin Peter N.46ORCID,Jaeger Karl-Erich2ORCID,Ferrer Manuel1ORCID

Affiliation:

1. Institute of Catalysis, Consejo Superior de Investigaciones Científicas, Madrid, Spain

2. Institute of Molecular Enzyme Technology, Heinrich Heine University Düsseldorf and Forschungszentrum Jülich GmbH, Jülich, Germany

3. NORCE Norwegian Research Centre AS, Bergen, Norway

4. School of Natural Sciences, Bangor University, Bangor, United Kingdom

5. Centro de Metabolómica y Bioanálisis (CEMBIO), Facultad de Farmacia, Universidad CEU San Pablo, Boadilla del Monte, Madrid, Spain

6. Centre for Environmental Biotechnology, Bangor University, Bangor, United Kingdom

7. Bayer AG, Engineering and Technology Department, Leverkusen, Germany

8. Institute for Biological Resources and Marine Biotechnology (IRBIM-CNR), Messina, Italy

9. Immanuel Kant Baltic Federal University, Kaliningrad, Russia

Abstract

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.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

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