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@ARTICLE{Bollinger:873889,
      author       = {Bollinger, Alexander and Thies, Stephan and
                      Knieps-Grünhagen, Esther and Gertzen, Christoph and Kobus,
                      Stefanie and Höppner, Astrid and Ferrer, Manuel and Gohlke,
                      Holger and Smits, Sander H. J. and Jaeger, Karl-Erich},
      title        = {{A} {N}ovel {P}olyester {H}ydrolase {F}rom the {M}arine
                      {B}acterium {P}seudomonas aestusnigri – {S}tructural and
                      {F}unctional {I}nsights},
      journal      = {Frontiers in microbiology},
      volume       = {11},
      issn         = {1664-302X},
      address      = {Lausanne},
      publisher    = {Frontiers Media},
      reportid     = {FZJ-2020-01079},
      pages        = {114},
      year         = {2020},
      abstract     = {Biodegradation of synthetic polymers, in particular
                      polyethylene terephthalate (PET), is of great importance,
                      since environmental pollution with PET and other plastics
                      has become a severe global problem. Here, we report on the
                      polyester degrading ability of a novel carboxylic ester
                      hydrolase identified in the genome of the marine
                      hydrocarbonoclastic bacterium Pseudomonas aestusnigri
                      VGXO14T. The enzyme, designated PE-H, belongs to the type
                      IIa family of PET hydrolytic enzymes as indicated by amino
                      acid sequence homology. It was produced in Escherichia coli,
                      purified and its crystal structure was solved at 1.09 Å
                      resolution representing the first structure of a type IIa
                      PET hydrolytic enzyme. The structure shows a typical
                      α/β-hydrolase fold and high structural homology to known
                      polyester hydrolases. PET hydrolysis was detected at 30°C
                      with amorphous PET film (PETa), but not with PET film from a
                      commercial PET bottle (PETb). A rational mutagenesis study
                      to improve the PET degrading potential of PE-H yielded
                      variant PE-H (Y250S) which showed improved activity,
                      ultimately also allowing the hydrolysis of PETb. The crystal
                      structure of this variant solved at 1.35 Å resolution
                      allowed to rationalize the improvement of enzymatic
                      activity. A PET oligomer binding model was proposed by
                      molecular docking computations. Our results indicate a
                      significant potential of the marine bacterium P. aestusnigri
                      for PET degradation.},
      cin          = {IMET},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IMET-20090612},
      pnm          = {581 - Biotechnology (POF3-581) / DFG project 417919780 -
                      Zentrum für strukturelle Studien},
      pid          = {G:(DE-HGF)POF3-581 / G:(GEPRIS)417919780},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {32117139},
      UT           = {WOS:000517512900001},
      doi          = {10.3389/fmicb.2020.00114},
      url          = {https://juser.fz-juelich.de/record/873889},
}