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@ARTICLE{Aleksenko:884283,
      author       = {Aleksenko, Vladimir A. and Anand, Deepak and Remeeva, Alina
                      and Nazarenko, Vera V. and Gordeliy, Valentin and Jaeger,
                      Karl-Erich and Krauss, Ulrich and Gushchin, Ivan},
      title        = {{P}hylogeny and {S}tructure of {F}atty {A}cid
                      {P}hotodecarboxylases and {G}lucose-{M}ethanol-{C}holine
                      {O}xidoreductases},
      journal      = {Catalysts},
      volume       = {10},
      number       = {9},
      issn         = {2073-4344},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2020-03175},
      pages        = {1072 -},
      year         = {2020},
      abstract     = {Glucose-methanol-choline (GMC) oxidoreductases are a large
                      and diverse family of flavin-binding enzymes found in all
                      kingdoms of life. Recently, a new related family of proteins
                      has been discovered in algae named fatty acid
                      photodecarboxylases (FAPs). These enzymes use the energy of
                      light to convert fatty acids to the corresponding Cn-1
                      alkanes or alkenes, and hold great potential for
                      biotechnological application. In this work, we aimed at
                      uncovering the natural diversity of FAPs and their relations
                      with other GMC oxidoreductases. We reviewed the available
                      GMC structures, assembled a large dataset of GMC sequences,
                      and found that one active site amino acid, a histidine, is
                      extremely well conserved among the GMC proteins but not
                      among FAPs, where it is replaced with alanine. Using this
                      criterion, we found several new potential FAP genes, both in
                      genomic and metagenomic databases, and showed that related
                      bacterial, archaeal and fungal genes are unlikely to be
                      FAPs. We also identified several uncharacterized clusters of
                      GMC-like proteins as well as subfamilies of proteins that
                      lack the conserved histidine but are not FAPs. Finally, the
                      analysis of the collected dataset of potential
                      photodecarboxylase sequences revealed the key active site
                      residues that are strictly conserved, whereas other residues
                      in the vicinity of the flavin adenine dinucleotide (FAD)
                      cofactor and in the fatty acid-binding pocket are more
                      variable. The identified variants may have different FAP
                      activity and selectivity and consequently may prove useful
                      for new biotechnological applications, thereby fostering the
                      transition from a fossil carbon-based economy to a
                      bio-economy by enabling the sustainable production of
                      hydrocarbon fuels.},
      cin          = {IBG-1 / IBI-7 / IMET},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBG-1-20101118 / I:(DE-Juel1)IBI-7-20200312 /
                      I:(DE-Juel1)IMET-20090612},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      581 - Biotechnology (POF3-581)},
      pid          = {G:(DE-HGF)POF3-551 / G:(DE-HGF)POF3-581},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000580208000001},
      doi          = {10.3390/catal10091072},
      url          = {https://juser.fz-juelich.de/record/884283},
}