% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Smits:11495,
      author       = {Smits, S.H.J. and Meyer, T. and Müller, A. and van Os, N.
                      and Stoldt, M. and Willbold, D. and Schmitt, L. and
                      Grieshaber, M.K.},
      title        = {{I}nsights into the mechanism of ligand binding to octopine
                      dehydrogenase from {P}ecten maximus by {NMR} and
                      crystallography},
      journal      = {PLoS one},
      volume       = {5},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {PreJuSER-11495},
      pages        = {e12312},
      year         = {2010},
      note         = {This work was supported by the Deutsche Forschungs
                      Gemeinschaft (grant GR456/20-4 to M.K.G.) and a stipendium
                      of the North Rhein Westphalia graduate school Biostruct to
                      T.M. The funders had no role in study design, data
                      collection and analysis, decision to publish, or preparation
                      of the manuscript.},
      abstract     = {Octopine dehydrogenase (OcDH) from the adductor muscle of
                      the great scallop, Pecten maximus, catalyzes the NADH
                      dependent, reductive condensation of L-arginine and pyruvate
                      to octopine, NAD(+), and water during escape swimming and/or
                      subsequent recovery. The structure of OcDH was recently
                      solved and a reaction mechanism was proposed which implied
                      an ordered binding of NADH, L-arginine and finally pyruvate.
                      Here, the order of substrate binding as well as the
                      underlying conformational changes were investigated by NMR
                      confirming the model derived from the crystal structures.
                      Furthermore, the crystal structure of the OcDH/NADH/agmatine
                      complex was determined which suggests a key role of the side
                      chain of L-arginine in protein cataylsis. Thus, the order of
                      substrate binding to OcDH as well as the molecular signals
                      involved in octopine formation can now be described in
                      molecular detail.},
      keywords     = {Agmatine: pharmacology / Amino Acid Oxidoreductases:
                      antagonists $\&$ inhibitors / Amino Acid Oxidoreductases:
                      chemistry / Amino Acid Oxidoreductases: metabolism / Animals
                      / Crystallography, X-Ray / Ligands / Models, Molecular /
                      Nuclear Magnetic Resonance, Biomolecular / Pecten:
                      enzymology / Protein Binding / Protein Structure, Tertiary /
                      Ligands (NLM Chemicals) / Agmatine (NLM Chemicals) / Amino
                      Acid Oxidoreductases (NLM Chemicals) / D-octopine
                      dehydrogenase (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-3},
      ddc          = {500},
      cid          = {I:(DE-Juel1)VDB942},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20808820},
      pmc          = {pmc:PMC2924402},
      UT           = {WOS:000281075500029},
      doi          = {10.1371/journal.pone.0012312},
      url          = {https://juser.fz-juelich.de/record/11495},
}