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@ARTICLE{Dick:281037,
      author       = {Dick, Markus and Weiergräber, Oliver H. and Classen,
                      Thomas and Bisterfeld, Carolin and Bramski, Julia and
                      Gohlke, Holger and Pietruszka, Jörg},
      title        = {{T}rading off stability against activity in extremophilic
                      aldolases},
      journal      = {Scientific reports},
      volume       = {6},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2016-00748},
      pages        = {17908 -},
      year         = {2016},
      abstract     = {Understanding enzyme stability and activity in
                      extremophilic organisms is of great biotechnological
                      interest, but many questions are still unsolved. Using
                      2-deoxy-D-ribose-5-phosphate aldolase (DERA) as model
                      enzyme, we have evaluated structural and functional
                      characteristics of different orthologs from psychrophilic,
                      mesophilic and hyperthermophilic organisms. We present the
                      first crystal structures of psychrophilic DERAs, revealing a
                      dimeric organization resembling their mesophilic but not
                      their thermophilic counterparts. Conversion into monomeric
                      proteins showed that the native dimer interface contributes
                      to stability only in the hyperthermophilic enzymes.
                      Nevertheless, introduction of a disulfide bridge in the
                      interface of a psychrophilic DERA did confer increased
                      thermostability, suggesting a strategy for rational design
                      of more durable enzyme variants. Constraint network analysis
                      revealed particularly sparse interactions between the
                      substrate pocket and its surrounding α-helices in
                      psychrophilic DERAs, which indicates that a more flexible
                      active center underlies their high turnover numbers.},
      cin          = {IBOC / IBG-1 / ICS-6},
      ddc          = {000},
      cid          = {I:(DE-Juel1)IBOC-20090406 / I:(DE-Juel1)IBG-1-20101118 /
                      I:(DE-Juel1)ICS-6-20110106},
      pnm          = {581 - Biotechnology (POF3-581)},
      pid          = {G:(DE-HGF)POF3-581},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000368330900001},
      pubmed       = {pmid:26783049},
      doi          = {10.1038/srep17908},
      url          = {https://juser.fz-juelich.de/record/281037},
}