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@ARTICLE{Leal:807737,
      author       = {Leal, Ana Rita and Cruz, Rui and Bur, Daniel and Huesgen,
                      Pitter and Faro, Rosário and Manadas, Bruno and Wlodawer,
                      Alexander and Faro, Carlos and Simões, Isaura},
      title        = {{E}nzymatic properties, evidence for in vivo expression,
                      and intracellular localization of shewasin {D}, the pepsin
                      homolog from {S}hewanella denitrificans},
      journal      = {Scientific reports},
      volume       = {6},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2016-02155},
      pages        = {23869},
      year         = {2016},
      abstract     = {The widespread presence of pepsin-like enzymes in
                      eukaryotes together with their relevance in the control of
                      multiple biological processes is reflected in the large
                      number of studies published so far for this family of
                      enzymes. By contrast, pepsin homologs from bacteria have
                      only recently started to be characterized. The work with
                      recombinant shewasin A from Shewanella amazonensis provided
                      the first documentation of this activity in prokaryotes.
                      Here we extend our studies to shewasin D, the pepsin homolog
                      from Shewanella denitrificans, to gain further insight into
                      this group of bacterial peptidases that likely represent
                      ancestral versions of modern eukaryotic pepsin-like enzymes.
                      We demonstrate that the enzymatic properties of recombinant
                      shewasin D are strongly reminiscent of eukaryotic pepsin
                      homologues. We determined the specificity preferences of
                      both shewasin D and shewasin A using proteome-derived
                      peptide libraries and observed remarkable similarities
                      between both shewasins and eukaryotic pepsins, in particular
                      with BACE-1, thereby confirming their phylogenetic
                      proximity. Moreover, we provide first evidence of expression
                      of active shewasin D in S. denitrificans cells, confirming
                      its activity at acidic pH and inhibition by pepstatin.
                      Finally, our results revealed an unprecedented localization
                      for a family A1 member by demonstrating that native shewasin
                      D accumulates preferentially in the cytoplasm.},
      cin          = {ZEA-3},
      ddc          = {000},
      cid          = {I:(DE-Juel1)ZEA-3-20090406},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000373170500001},
      doi          = {10.1038/srep23869},
      url          = {https://juser.fz-juelich.de/record/807737},
}