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@ARTICLE{Jckering:1032182,
      author       = {Jäckering, Anna and Göttsch, Frederike and Schäffler,
                      Moritz and Doerr, Mark and Bornscheuer, Uwe T. and Wei, Ren
                      and Strodel, Birgit},
      title        = {{F}rom {B}ulk to {B}inding: {D}ecoding the {E}ntry of {PET}
                      into {H}ydrolase {B}inding {P}ockets},
      journal      = {JACS Au},
      volume       = {4},
      number       = {10},
      issn         = {2691-3704},
      address      = {Washington, DC},
      publisher    = {ACS Publications},
      reportid     = {FZJ-2024-06051},
      pages        = {4000 - 4012},
      year         = {2024},
      abstract     = {Plastic-degrading enzymes facilitate the
                      biocatalyticrecycling of poly(ethylene terephthalate) (PET),
                      a significantsynthetic polymer, and substantial progress has
                      been made inutilizing PET hydrolases for industrial
                      applications. To fully exploitthe potential of these
                      enzymes, a deeper mechanistic understandingfollowed by
                      targeted protein engineering is essential. Throughadvanced
                      molecular dynamics simulations and free energy
                      analysismethods, we elucidated the complete pathway from the
                      initialbinding of two PET hydrolases�the thermophilic
                      leaf-branchcompost cutinase (LCC) and polyester hydrolase 1
                      (PES-H1)�toan amorphous PET substrate, ultimately leading
                      to a PET chainentering the active site in a hydrolyzable
                      conformation. Ourfindings indicate that initial PET binding
                      is nonspecific and drivenby polar and hydrophobic
                      interactions. We demonstrate that the subsequent entry of
                      PET into the active site can occur via one ofthree key
                      pathways, identifying barriers related to both PET−PET and
                      PET−enzyme interactions, as well as specific
                      residueshighlighted through in silico and in vitro
                      mutagenesis. These insights not only enhance our
                      understanding of the mechanismsunderlying PET degradation
                      and facilitate the development of targeted enzyme
                      enhancement strategies but also provide a novelframework
                      applicable to enzyme studies across various disciplines.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {39483243},
      UT           = {WOS:001323931400001},
      doi          = {10.1021/jacsau.4c00718},
      url          = {https://juser.fz-juelich.de/record/1032182},
}