The first archaeal PET-degrading enzyme belongs to the feruloyl-esterase family
Creators
- 1. Department of Microbiology and Biotechnology, University of Hamburg, Ohnhorststrasse 18, 22609 Hamburg, Germany; Institute for General Microbiology, Christian-Albrechts-Universität zu Kiel, Am Botanischen Garten 1-9, Kiel, Germany
- 2. Department of Microbiology and Biotechnology, University of Hamburg, Ohnhorststrasse 18, 22609 Hamburg, Germany
- 3. Center for Structural Studies (CSS), Heinrich Heine University Düsseldorf, Universitätsstrasse 1, 40225 Düsseldorf, Germany
- 4. Institute for Pharmaceutical and Medicinal Chemistry, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany
- 5. Institute for Pharmaceutical and Medicinal Chemistry, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany; Institute for Bio- and Geosciences (IBG-4: Bioinformatics), Forschungszentrum Jülich, Jülich, Germany
- 6. Center for Structural Studies (CSS), Heinrich Heine University Düsseldorf, Universitätsstrasse 1, 40225 Düsseldorf, Germany; Institute for Biochemistry, Heinrich Heine University Düsseldorf, Universitätsstrasse 1, 40225 Düsseldorf, Germany
- 7. Institute for General Microbiology, Christian-Albrechts-Universität zu Kiel, Am Botanischen Garten 1-9, Kiel, Germany
Description
Polyethylene terephthalate (PET) is a commodity polymer known to globally
contaminate marine and terrestrial environments. Today, around 40 bacterial and fungal PET-active enzymes (PETases) are known, originating from four bacterial and two fungal phyla. In contrast, no archaeal enzyme has been identified to degrade PET. Here we report on the structural and biochemical characterization of PET46, an archaeal promiscuous feruloyl esterase exhibiting degradation activitiy on PET, bis-, and mono-(2-hydroxyethyl) terephthalate (BHET and MHET). The enzyme, found by a sequence-based metagenome search, was derived from a non-cultivated, deep-sea Candidatus Bathyarchaeota archaeon. Biochemical characterization demonstrated that PET46 is a promiscuous, heat-adapted hydrolase. Its crystal structure was solved at a resolution of 1.71 Å. It shares the core alpha/beta-hydrolase fold with bacterial PETases, but contains a unique lid common in feruloyl esterases, which is involved in substrate binding. Thus, our study significantly widens the currently known diversity of PET-hydrolyzing enzymes, by demonstrating PET depolymerization by a lignin degrading esterase.
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The first archael PET-degrading enzyme belongs to the feruloyl-esterase family.pdf
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