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@ARTICLE{Nutschel:893205,
      author       = {Nutschel, Christina and Coscolín, Cristina and David,
                      Benoit and Mulnaes, Daniel and Ferrer, Manuel and Jaeger,
                      Karl-Erich and Gohlke, Holger},
      title        = {{P}romiscuous {E}sterases {C}ounterintuitively {A}re {L}ess
                      {F}lexible than {S}pecific {O}nes},
      journal      = {Journal of chemical information and modeling},
      volume       = {61},
      number       = {5},
      issn         = {1549-960X},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2021-02622},
      pages        = {2383 - 2395},
      year         = {2021},
      abstract     = {Understanding mechanisms of promiscuity is increasingly
                      important from a fundamental and application point of view.
                      As to enzyme structural dynamics, more promiscuous enzymes
                      generally have been recognized to also be more flexible.
                      However, examples for the opposite received much less
                      attention. Here, we exploit comprehensive experimental
                      information on the substrate promiscuity of 147 esterases
                      tested against 96 esters together with computationally
                      efficient rigidity analyses to understand the molecular
                      origin of the observed promiscuity range. Unexpectedly, our
                      data reveal that promiscuous esterases are significantly
                      less flexible than specific ones, are significantly more
                      thermostable, and have a significantly increased specific
                      activity. These results may be reconciled with a model
                      according to which structural flexibility in the case of
                      specific esterases serves for conformational proofreading.
                      Our results signify that an esterase sequence space can be
                      screened by rigidity analyses for promiscuous esterases as
                      starting points for further exploration in biotechnology and
                      synthetic chemistry.},
      cin          = {IBG-4 / NIC / JSC / IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBG-4-20200403 / I:(DE-Juel1)NIC-20090406 /
                      I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5111 - Domain-Specific Simulation $\&$ Data Life Cycle Labs
                      (SDLs) and Research Groups (POF4-511) / 2171 - Biological
                      and environmental resources for sustainable use (POF4-217) /
                      2172 - Utilization of renewable carbon and energy sources
                      and engineering of ecosystem functions (POF4-217) / 511 -
                      Computational Science and Mathematical Methods (POF3-511) /
                      Forschergruppe Gohlke $(hkf7_20200501)$},
      pid          = {G:(DE-HGF)POF4-5111 / G:(DE-HGF)POF4-2171 /
                      G:(DE-HGF)POF4-2172 / G:(DE-HGF)POF3-511 /
                      $G:(DE-Juel1)hkf7_20200501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {33949194},
      UT           = {WOS:000656118800025},
      doi          = {10.1021/acs.jcim.1c00152},
      url          = {https://juser.fz-juelich.de/record/893205},
}