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@ARTICLE{Kachalova:94652,
      author       = {Kachalova, G. and Decker, K. and Holt, A. and Bartunik, H.
                      D. and DESY},
      title        = {{C}rystallographic snapshots of the complete reaction cycle
                      of nicotine degradation by an amine oxidase of the monoamine
                      oxidase ({MAO}) family},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {108},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {Academy},
      reportid     = {PHPPUBDB-18289},
      pages        = {4800-4805},
      year         = {2011},
      abstract     = {FAD-linked oxidases constitute a class of enzymes which
                      catalyze dehydrogenation as a fundamental biochemical
                      reaction, followed by reoxidation of reduced flavin. Here,
                      we present high-resolution crystal structures showing the
                      flavoenzyme 6-hydroxy-l-nicotine oxidase in action. This
                      enzyme was trapped during catalytic degradation of the
                      native substrate in a sequence of discrete reaction states
                      corresponding to the substrate-reduced enzyme, a complex of
                      the enzyme with the intermediate enamine product and
                      formation of the final aminoketone product. The inactive
                      d-stereoisomer binds in mirror symmetry with respect to the
                      catalytic axis, revealing absolute stereospecificity of
                      hydrogen transfer to the flavin. The structural data suggest
                      deprotonation of the substrate when bound at the active
                      site, an overall binary complex mechanism and oxidation by
                      direct hydride transfer. The amine nitrogen has a critical
                      role in the dehydrogenation step and may activate
                      carbocation formation at the α-carbon via delocalization
                      from the lone pair to σ* C(α)-H. Enzymatically assisted
                      hydrolysis of the intermediate product occurs at a remote
                      (P site) cavity. Substrate entry and product exit follow
                      different paths. Structural and kinetic data suggest that
                      substrate can also bind to the reduced enzyme, associated
                      with slower reoxidation as compared to the rate of
                      reoxidation of free enzyme. The results are of general
                      relevance for the mechanisms of flavin amine oxidases.},
      keywords     = {Arthrobacter: enzymology / Bacterial Proteins: chemistry /
                      Catalytic Domain / Crystallography, X-Ray / Kinetics /
                      Monoamine Oxidase: chemistry / Nicotine: chemistry /
                      Oxidation-Reduction / Oxidoreductases Acting on CH-NH Group
                      Donors: chemistry / Structure-Activity Relationship /
                      Bacterial Proteins (NLM Chemicals) / Nicotine (NLM
                      Chemicals) / Monoamine Oxidase (NLM Chemicals) /
                      Oxidoreductases Acting on CH-NH Group Donors (NLM Chemicals)
                      / 6-hydroxy-L-nicotine oxidase (NLM Chemicals)},
      cin          = {HASYLAB / MPG},
      ddc          = {000},
      cid          = {$I:(DE-H253)HASYLAB_-2012_-20130307$ /
                      $I:(DE-H253)MPG_-2012_-20120307$},
      pnm          = {DORIS Beamline BW6 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-BW6-20130405},
      experiment   = {EXP:(DE-H253)D-BW6-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21383134},
      pmc          = {pmc:PMC3064382},
      UT           = {WOS:000288712200025},
      doi          = {10.1073/pnas.1016684108},
      url          = {https://bib-pubdb1.desy.de/record/94652},
}