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@ARTICLE{Porta:910242,
      author       = {Porta, Nicola and Fejzagić, Alexander Veljko and
                      Dumschott, Kathryn and Paschold, Beatrix and Usadel, Björn
                      and Pietruszka, Jörg and Classen, Thomas and Gohlke,
                      Holger},
      title        = {{I}dentification and {C}haracterization of the
                      {H}aloperoxidase {VPO}-{RR} from {R}hodoplanes roseus by
                      {G}enome {M}ining and {S}tructure-{B}ased {C}atalytic {S}ite
                      {M}apping},
      journal      = {Catalysts},
      volume       = {12},
      number       = {10},
      issn         = {2073-4344},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2022-03704},
      pages        = {1195 -},
      year         = {2022},
      abstract     = {Halogenating enzymes have evolved in considerable
                      mechanistic diversity. The apparent need for secondary
                      metabolism coincides with the current need to introduce
                      halogens in synthetic products. The potential of
                      halogenating enzymes and, especially, vanadate-dependent
                      haloperoxidases has been insufficiently exploited for
                      synthetic purposes. In this work, we identified potential
                      halogenase sequences by screening algal, fungal, and
                      protobacterial sequence databases, structural modeling of
                      putative halogenases, and mapping and comparing active
                      sites. In a final step, individual haloperoxidases were
                      expressed and kinetically characterized. A
                      vanadate-dependent haloperoxidase from Rhodoplanes roseus
                      was heterologously expressible by E. coli and could be
                      purified to homogeneity. The kinetic data revealed a higher
                      turnover number than the known VClPO-CI and no inhibitory
                      effect from bromide, rendering this enzyme a promising
                      biocatalyst. Other predicted haloperoxidases were not
                      expressed successfully yet but these enzymes were predicted
                      to be present in a wide taxonomic variety.},
      cin          = {IBG-4 / IBG-1 / JSC / NIC / IBI-7 / IBOC},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBG-4-20200403 / I:(DE-Juel1)IBG-1-20101118 /
                      I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)NIC-20090406 /
                      I:(DE-Juel1)IBI-7-20200312 / I:(DE-Juel1)IBOC-20090406},
      pnm          = {2171 - Biological and environmental resources for
                      sustainable use (POF4-217) / 5111 - Domain-Specific
                      Simulation $\&$ Data Life Cycle Labs (SDLs) and Research
                      Groups (POF4-511) / Forschergruppe Gohlke $(hkf7_20200501)$
                      / BioSC - Bioeconomy Science Center (BioSC) / 5241 -
                      Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-2171 / G:(DE-HGF)POF4-5111 /
                      $G:(DE-Juel1)hkf7_20200501$ / G:(DE-Juel1)BioSC /
                      G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000872566300001},
      doi          = {10.3390/catal12101195},
      url          = {https://juser.fz-juelich.de/record/910242},
}