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@ARTICLE{Turak:642766,
      author       = {Turak, Onur and Gagsteiger, Andreas and Upadhyay, Ashank
                      and Kriegel, Mark and Salein, Peter and Böhnke-Brandt,
                      Stefanie and Agarwal, Seema and Borchert, Erik and Höcker,
                      Birte},
      title        = {{A} third type of {PET}ase from the marine
                      {H}alopseudomonas lineage},
      journal      = {Protein science},
      volume       = {34},
      number       = {10},
      issn         = {0961-8368},
      address      = {Hoboken, NJ},
      publisher    = {Wiley},
      reportid     = {PUBDB-2025-05615},
      pages        = {e70305},
      year         = {2025},
      abstract     = {The enzymatic degradation of polyethylene terephthalate
                      (PET) offers a sustainable solution for PET recycling. Over
                      the past two decades, more than 100 PETases have been
                      characterized, primarily exhibiting similar sequences and
                      structures. Here, we report PET-degrading α/β hydrolases,
                      including HaloPETase1 from the marine Halopseudomonas
                      lineage, thereby extending the narrow sequence space by
                      novel features at the active site. The crystal structure of
                      HaloPETase1 was determined to a resolution of 1.16 Å,
                      revealing a unique active site architecture and a lack of
                      the canonical π-stacking clamp found in PETases so far.
                      Further, variations in active site composition and loop
                      structures were observed. Additionally, we found five more
                      enzymes from the same lineage, two of which have a high
                      similarity to type IIa bacterial PETases, while the other
                      three resemble HaloPETase1. All these enzymes exhibited high
                      salt tolerance ranging from 2.5 to 5 M NaCl, leading to
                      higher total product releases upon PET degradation at 40 or
                      50°C. Based on these findings, we propose an extension of
                      the existing PETase classification system to include type
                      III PETases.},
      cin          = {EMBL-User},
      ddc          = {610},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / SFB 1357 C03 -
                      Enzymatischer Abbau synthetischer Polymere (C03)
                      (419410411)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(GEPRIS)419410411},
      experiment   = {EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1002/pro.70305},
      url          = {https://bib-pubdb1.desy.de/record/642766},
}