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@ARTICLE{Rindfleisch:482580,
      author       = {Rindfleisch, Soeren and Krull, Matthias and Uranga, Jon and
                      Schmidt, Tobias and Rabe von Pappenheim, Fabian and Kirck,
                      Laura Liliana and Balouri, Angeliki and Schneider, Thomas
                      and Chari, Ashwin and Kluger, Ronald and Bourenkov, Gleb and
                      Diederichsen, Ulf and Mata, Ricardo A. and Tittmann, Kai},
      title        = {{G}round-state destabilization by electrostatic repulsion
                      is not a driving force in orotidine-5′-monophosphate
                      decarboxylase catalysis},
      journal      = {Nature catalysis},
      volume       = {5},
      number       = {4},
      issn         = {2520-1158},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {PUBDB-2022-04841},
      pages        = {332 - 341},
      year         = {2022},
      abstract     = {The origins of enzyme catalysis have been attributed to
                      both transition-state stabilization as well as ground-state
                      destabilization of the substrate. For the latter paradigm,
                      the enzyme orotidine-5′-monophosphate decarboxylase
                      (OMPDC) serves as a reference system as it contains a
                      negatively charged residue at the active site that is
                      thought to facilitate catalysis by exerting an electrostatic
                      stress on the substrate carboxylate leaving group. Snapshots
                      of how the substrate binds to the active site and interacts
                      with the negative charge have remained elusive. Here we
                      present crystallographic snapshots of human OMPDC in complex
                      with the substrate, substrate analogues, transition-state
                      analogues and product that defy the proposed ground-state
                      destabilization by revealing that the substrate carboxylate
                      is protonated and forms a favourable low-barrier hydrogen
                      bond with a negatively charged residue. The catalytic
                      prowess of OMPDC almost entirely results from the
                      transition-state stabilization by electrostatic interactions
                      of the enzyme with charges spread over the substrate. Our
                      findings bear relevance for the design of (de)carboxylase
                      catalysts.},
      cin          = {EMBL-User / EMBL},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P13-20150101 / EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000784635500001},
      doi          = {10.1038/s41929-022-00771-w},
      url          = {https://bib-pubdb1.desy.de/record/482580},
}