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@ARTICLE{Kutter:94208,
      author       = {Kutter, S. and Weiss, M. S. and Wille, G. and Golbik, R.
                      and Spinka, M. and König, S. and DESY},
      title        = {{C}ovalently {B}ound {S}ubstrate at the {R}egulatory {S}ite
                      of {Y}east {P}yruvate {D}ecarboxylases {T}riggers
                      {A}llosteric {E}nzyme {A}ctivation},
      journal      = {The journal of biological chemistry},
      volume       = {284},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PHPPUBDB-12657},
      pages        = {12136-12144},
      year         = {2009},
      abstract     = {The mechanism by which the enzyme pyruvate decarboxylase
                      from two yeast species is activated allosterically has been
                      elucidated. A total of seven three-dimensional structures of
                      the enzyme, of enzyme variants, or of enzyme complexes from
                      two yeast species, three of them reported here for the first
                      time, provide detailed atomic resolution snapshots along the
                      activation coordinate. The prime event is the covalent
                      binding of the substrate pyruvate to the side chain of
                      cysteine 221, thus forming a thiohemiketal. This reaction
                      causes the shift of a neighboring amino acid, which
                      eventually leads to the rigidification of two otherwise
                      flexible loops, one of which provides two histidine residues
                      necessary to complete the enzymatically competent active
                      site architecture. The structural data are complemented and
                      supported by kinetic investigations and binding studies,
                      providing a consistent picture of the structural changes
                      occurring upon enzyme activation.},
      keywords     = {Allosteric Regulation: physiology / Enzyme Activation:
                      physiology / Fungal Proteins: chemistry / Kinetics /
                      Kluyveromyces: enzymology / Protein Structure, Tertiary:
                      physiology / Pyruvate Decarboxylase: chemistry / Pyruvic
                      Acid: chemistry / Fungal Proteins (NLM Chemicals) / Pyruvic
                      Acid (NLM Chemicals) / Pyruvate Decarboxylase (NLM
                      Chemicals)},
      cin          = {EMBL},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {FS Beamline without reference (POF1-550)},
      pid          = {G:(DE-H253)POF1-No-Ref-20130405},
      experiment   = {EXP:(DE-H253)Unknown-BL-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19246454},
      pmc          = {pmc:PMC2673282},
      UT           = {WOS:000265494600045},
      doi          = {10.1074/jbc.M806228200},
      url          = {https://bib-pubdb1.desy.de/record/94208},
}