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@ARTICLE{Kovai:202106,
      author       = {Kovačić, Filip and Granzin, Joachim and Wilhelm, Susanne
                      and Kojić-Prodić, Biserka and Batra-Safferling, Renu and
                      Jaeger, Karl-Erich},
      title        = {{S}tructural and functional characterisation of {T}es{A} -
                      a novel lysophospholipase {A} from {P}seudomonas
                      aeruginosa.},
      journal      = {PLoS one},
      volume       = {8},
      number       = {7},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2015-04395},
      pages        = {e69125 -},
      year         = {2013},
      abstract     = {TesA from Pseudomonas aeruginosa belongs to the GDSL
                      hydrolase family of serine esterases and lipases that
                      possess a broad substrate- and regiospecificity. It shows
                      high sequence homology to TAP, a multifunctional enzyme from
                      Escherichia coli exhibiting thioesterase, lysophospholipase
                      A, protease and arylesterase activities. Recently, we
                      demonstrated high arylesterase activity for TesA, but only
                      minor thioesterase and no protease activity. Here, we
                      present a comparative analysis of TesA and TAP at the
                      structural, biochemical and physiological levels. The
                      crystal structure of TesA was determined at 1.9 Å and
                      structural differences were identified, providing a possible
                      explanation for the differences in substrate specificities.
                      The comparison of TesA with other GDSL-hydrolase structures
                      revealed that the flexibility of active-site loops
                      significantly affects their substrate specificity. This
                      assumption was tested using a rational approach: we have
                      engineered the putative coenzyme A thioester binding site of
                      E. coli TAP into TesA of P. aeruginosa by introducing
                      mutations D17S and L162R. This TesA variant showed increased
                      thioesterase activity comparable to that of TAP. TesA is the
                      first lysophospholipase A described for the opportunistic
                      human pathogen P. aeruginosa. The enzyme is localized in the
                      periplasm and may exert important functions in the
                      homeostasis of phospholipids or detoxification of
                      lysophospholipids.},
      keywords     = {Oligonucleotides (NLM Chemicals) / Lysophospholipase (NLM
                      Chemicals)},
      cin          = {ICS-6 / IMET},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)IMET-20090612},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23874889},
      pmc          = {pmc:PMC3715468},
      UT           = {WOS:000324146200060},
      doi          = {10.1371/journal.pone.0069125},
      url          = {https://juser.fz-juelich.de/record/202106},
}