% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Kovacic:821075,
      author       = {Kovacic, Filip and Bleffert, Florian and Caliskan, Muttalip
                      and Wilhelm, Susanne and Granzin, Joachim and
                      Batra-Safferling, Renu and Jaeger, Karl-Erich},
      title        = {{A} membrane-bound esterase {PA}2949 from
                      {P}seudomonas aeruginosa is expressed and purified from
                      {E}scherichia coli},
      journal      = {FEBS Open Bio},
      volume       = {6},
      number       = {5},
      issn         = {2211-5463},
      address      = {Cambridge},
      publisher    = {Elsevier on behalf of the Federation of European
                      Biochemical Societies},
      reportid     = {FZJ-2016-06319},
      pages        = {484 - 493},
      year         = {2016},
      abstract     = {Pseudomonas aeruginosa strain 1001 produces an esterase
                      (EstA) that can hydrolyse the racemic methyl ester of
                      b-acetylthioisobutyrate to produce the (D)-enantiomer, which
                      serves as a precursor of captopril, a drug used for
                      treatment of hypertension. We show here that PA2949 from P.
                      aeruginosa PA01, a homologue of EstA, can efficiently be
                      expressed in an enzymatically active form in E. coli. The
                      enzyme is membrane-associated as demonstrated by cell
                      fractionation studies. PA2949 was purified to homogeneity
                      after solubilisation with the nonionic detergent, Triton
                      X-100, and was shown to possess a conserved esterase
                      catalytic triad consisting of Ser137–His258–Asp286. Our
                      results should allow the development of an expression and
                      purification strategy to produce this biotechnologically
                      relevant esterase in a pure form with a high yield.},
      cin          = {ICS-6 / IMET},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)IMET-20090612},
      pnm          = {553 - Physical Basis of Diseases (POF3-553) / 581 -
                      Biotechnology (POF3-581)},
      pid          = {G:(DE-HGF)POF3-553 / G:(DE-HGF)POF3-581},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000375915100012},
      pubmed       = {pmid:27419054},
      doi          = {10.1002/2211-5463.12061},
      url          = {https://juser.fz-juelich.de/record/821075},
}