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@ARTICLE{Riccardi:834628,
      author       = {Riccardi, Laura and Arencibia, Jose M. and Bono, Luca and
                      Armirotti, Andrea and Girotto, Stefania and De Vivo, Marco},
      title        = {{L}id domain plasticity and lipid flexibility modulate
                      enzyme specificity in human monoacylglycerol lipase},
      journal      = {Biochimica et biophysica acta / Molecular and cell biology
                      of lipids},
      volume       = {1862},
      number       = {5},
      issn         = {1388-1981},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {FZJ-2017-04536},
      pages        = {441 - 451},
      year         = {2017},
      abstract     = {Human monoacylglycerol lipase (MAGL) is a
                      membrane-interacting enzyme that generates pro-inflammatory
                      signaling molecules. For this reason, MAGL inhibition is a
                      promising strategy to treat pain, cancer, and
                      neuroinflammatory diseases. MAGL can hydrolyze
                      monoacylglycerols bearing an acyl chain of different lengths
                      and degrees of unsaturation, cleaving primarily the
                      endocannabinoid 2-arachidonoylglycerol. Importantly, the
                      enzymatic binding site of MAGL is confined by a
                      75-amino-acid-long, flexible cap domain, named ‘lid
                      domain’, which is structurally similar to that found in
                      several other lipases. However, it is unclear how lid domain
                      plasticity affects catalysis in MAGL. By integrating
                      extensive molecular dynamics simulations and free-energy
                      calculations with mutagenesis and kinetic experiments, we
                      here define a lid-domain-mediated mechanism for substrate
                      selection and binding in MAGL catalysis. In particular, we
                      clarify the key role of Phe159 and Ile179, two conserved
                      residues within the lid domain, in regulating substrate
                      specificity in MAGL. We conclude by proposing that other
                      structurally related lipases may share this
                      lid-domain-mediated mechanism for substrate specificity.},
      cin          = {IAS-5 / INM-9},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000400715800001},
      pubmed       = {pmid:28088576},
      doi          = {10.1016/j.bbalip.2017.01.002},
      url          = {https://juser.fz-juelich.de/record/834628},
}