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@ARTICLE{AlfonsoPrieto:1005471,
      author       = {Alfonso-Prieto, Mercedes and Cuxart, Irene and
                      Potocki-Véronèse, Gabrielle and André, Isabelle and
                      Rovira, Carme},
      title        = {{S}ubstrate-{A}ssisted {M}echanism for the {D}egradation of
                      {N} -{G}lycans by a {G}ut {B}acterial {M}annoside
                      {P}hosphorylase},
      journal      = {ACS catalysis},
      volume       = {13},
      issn         = {2155-5435},
      address      = {Washington, DC},
      publisher    = {ACS},
      reportid     = {FZJ-2023-01491},
      pages        = {4283 - 4289},
      year         = {2023},
      abstract     = {The unknown human gut bacterium mannoside phosphorylase
                      (UhgbMP) is involved in the metabolization of eukaryotic
                      N-glycans lining the intestinal epithelium, a factor
                      associated with the onset and symptoms of inflammatory bowel
                      diseases. In contrast with most glycoside phosphorylases,
                      the putative catalytic acid of UhgbMP, Asp104, is far from
                      the scissile glycosidic bond, challenging the classical
                      Koshland mechanism. Using quantum mechanics/molecular
                      mechanics metadynamics, we demonstrate that the enzyme
                      operates by substrate-assisted catalysis via the 3-hydroxyl
                      group of the mannosyl unit, following a 1S5/B2,5 →
                      [B2,5]‡ → 0S2 conformational itinerary. Given the
                      conservation of the active site hydrogen bond network across
                      the family, this mechanism is expected to apply to other
                      GH130 enzymes, as well as recently characterized mannoside
                      phosphorylases with similar folds. Gaining insight into the
                      catalytic reaction of these enzymes can aid the design of
                      specific inhibitors to control interactions between gut
                      microbes and the host.},
      cin          = {IAS-5 / INM-9},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000953970600001},
      doi          = {10.1021/acscatal.3c00451},
      url          = {https://juser.fz-juelich.de/record/1005471},
}