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@ARTICLE{Tokin:473443,
      author       = {Tokin, Radina and Frandsen, Kristian E. H. and Ipsen, Johan
                      Ørskov and Lo Leggio, Leila and Poojary, Mahesha M. and
                      Berrin, Jean-Guy and Grisel, Sacha and Brander, Søren and
                      Jensen, Poul Erik and Johansen, Katja Salomon},
      title        = {{I}nhibition of lytic polysaccharide monooxygenase by
                      natural plant extracts},
      journal      = {The new phytologist},
      volume       = {232},
      number       = {3},
      issn         = {0028-646X},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {PUBDB-2022-00063},
      pages        = {1337 - 1349},
      year         = {2021},
      note         = {Waiting for fulltext},
      abstract     = {Lytic polysaccharide monooxygenases (LPMOs) are monocopper
                      enzymes of industrial and biological importance. In
                      particular, LPMOs play important roles in fungal lifestyle.
                      No inhibitors of LPMOs have yet been reported. In this
                      study, a diverse library of 100 plant extracts was screened
                      for LPMO activity-modulating effects. By employing protein
                      crystallography and LC–MS, we successfully identified a
                      natural LPMO inhibitor. Extract screening revealed a
                      significant LPMO inhibition by methanolic extract of
                      Cinnamomum cassia (cinnamon), which inhibited $Ls$AA9A LPMO
                      from Lentinus similis in a concentration-dependent manner.
                      With a notable exception, other microbial LPMOs from
                      families AA9 and AA10 were also inhibited by this cinnamon
                      extract. The polyphenol cinnamtannin B1 was identified as
                      the inhibitory component by crystallography. Cinnamtannin B1
                      was bound to the surface of $Ls$AA9A at two distinct binding
                      sites: one close to the active site and another at a pocket
                      on the opposite side of the protein. Independent
                      characterization of cinnamon extract by LC–MS and
                      subsequent activity measurements confirmed that the compound
                      inhibiting $Ls$AA9A was cinnamtannin B1. The results of this
                      study show that specific natural LPMO inhibitors of plant
                      origin exist in nature, providing the opportunity for future
                      exploitation of such compounds within various
                      biotechnological contexts.},
      cin          = {DOOR ; HAS-User},
      ddc          = {580},
      cid          = {I:(DE-H253)HAS-User-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / BIOSTRUCT-X -
                      Transnational access and enhancement of integrated
                      Biological Structure determination at synchrotron X-ray
                      radiation facilities (283570)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(EU-Grant)283570},
      experiment   = {EXP:(DE-H253)P-P11-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34389999},
      UT           = {WOS:000691795100001},
      doi          = {10.1111/nph.17676},
      url          = {https://bib-pubdb1.desy.de/record/473443},
}