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@ARTICLE{PerezGarcia:1014968,
      author       = {Perez-Garcia, Pablo and Chow, Jennifer and Costanzi, Elisa
                      and Gurschke, Marno and Dittrich, Jonas and Dierkes, Robert
                      F. and Molitor, Rebecka and Applegate, Violetta and
                      Feuerriegel, Golo and Tete, Prince and Danso, Dominik and
                      Thies, Stephan and Schumacher, Julia and Pfleger,
                      Christopher and Jaeger, Karl-Erich and Gohlke, Holger and
                      Smits, Sander H. J. and Schmitz, Ruth A. and Streit,
                      Wolfgang R.},
      title        = {{A}n archaeal lid-containing feruloyl esterase degrades
                      polyethylene terephthalate},
      journal      = {Communications chemistry},
      volume       = {6},
      number       = {1},
      issn         = {2399-3669},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2023-03512},
      pages        = {193},
      year         = {2023},
      abstract     = {Polyethylene terephthalate (PET) is a commodity polymer
                      known to globally contaminate marine and terrestrial
                      environments. Today, around 80 bacterial and fungal
                      PET-active enzymes (PETases) are known, originating from
                      four bacterial and two fungal phyla. In contrast, no
                      archaeal enzyme had been identified to degrade PET. Here we
                      report on the structural and biochemical characterization of
                      PET46 (RLI42440.1), an archaeal promiscuous feruloyl
                      esterase exhibiting degradation activity on semi-crystalline
                      PET powder comparable to IsPETase and LCC (wildtypes), and
                      higher activity on bis-, and mono-(2-hydroxyethyl)
                      terephthalate (BHET and MHET). The enzyme, found by a
                      sequence-based metagenome search, is 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 widens the
                      currently known diversity of PET-hydrolyzing enzymes, by
                      demonstrating PET depolymerization by a plant cell
                      wall-degrading esterase.},
      cin          = {IBG-4 / IMET},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBG-4-20200403 / I:(DE-Juel1)IMET-20090612},
      pnm          = {2171 - Biological and environmental resources for
                      sustainable use (POF4-217) / DFG project 417919780 - Zentrum
                      für strukturelle Studien (417919780)},
      pid          = {G:(DE-HGF)POF4-2171 / G:(GEPRIS)417919780},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {37697032},
      UT           = {WOS:001066506600001},
      doi          = {10.1038/s42004-023-00998-z},
      url          = {https://juser.fz-juelich.de/record/1014968},
}