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@ARTICLE{Hppner:168213,
      author       = {Höppner, Astrid and Schomburg, Dietmar and Niefind,
                      Karsten},
      title        = {{E}nzyme-substrate complexes of the quinate/shikimate
                      dehydrogenase from {C}orynebacterium glutamicum enable new
                      insights in substrate and cofactor binding, specificity, and
                      discrimination},
      journal      = {Biological chemistry},
      volume       = {394},
      number       = {11},
      issn         = {1437-4315},
      address      = {Berlin [u.a.]},
      publisher    = {de Gruyter},
      reportid     = {DESY-2014-02418},
      pages        = {1505-16},
      year         = {2013},
      note         = {(c) by Walter de Gruyter GmbH},
      abstract     = {Quinate dehydrogenase (QDH) catalyzes the reversible
                      oxidation of quinate to 3-dehydroquinate by nicotineamide
                      adenine dinucleotide (NADH) and is involved in the catabolic
                      quinate metabolism required for the degradation of lignin.
                      The enzyme is a member of the family of shikimate/quinate
                      dehydrogenases (SDH/QDH) occurring in bacteria and plants.
                      We characterized the dual-substrate quinate/shikimate
                      dehydrogenase (QSDH) from Corynebacterium glutamicum
                      (CglQSDH) kinetically and revealed a clear substrate
                      preference of CglQSDH for quinate compared with shikimate
                      both at the pH optimum and in a physiological pH range,
                      which is a remarkable contrast to closely related SDH/QDH
                      enzymes. With respect to the cosubstrate, CglQSDH is
                      strictly NAD(H) dependent. These substrate and cosubstrate
                      profiles correlate well with the details of three atomic
                      resolution crystal structures of CglQSDH in different
                      functional states we report here: with bound NAD+ (binary
                      complex) and as ternary complexes with NADH plus either
                      shikimate or quinate. The CglQSDH-NADH-quinate structure is
                      the first complex structure of any member of the SDH/QDH
                      family with quinate. Based on this novel structural
                      information and systematic sequence and structure
                      comparisons with closely related enzymes, we can explain the
                      strict NAD(H) dependency of CglQSDH as well as its
                      discrimination between shikimate and quinate.},
      cin          = {EMBL-User},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {DORIS Beamline BW7 (POF2-54G13) / DORIS Beamline K1.2
                      (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-BW7-20130405 /
                      G:(DE-H253)POF2-K1.2-20130405},
      experiment   = {EXP:(DE-H253)D-BW7-20150101 / EXP:(DE-H253)D-K1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000325717100014},
      pubmed       = {pmid:23929881},
      doi          = {10.1515/hsz-2013-0170},
      url          = {https://bib-pubdb1.desy.de/record/168213},
}