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@ARTICLE{GimnezDejoz:281887,
      author       = {Giménez-Dejoz, Joan and Kolář, Michal H. and Ruiz,
                      Francesc X. and Crespo, Isidro and Cousido-Siah, Alexandra
                      and Podjarny, Alberto and Barski, Oleg A. and Fanfrlík,
                      Jindřich and Parés, Xavier and Farrés, Jaume and Porté,
                      Sergio},
      title        = {{S}ubstrate {S}pecificity, {I}nhibitor {S}electivity and
                      {S}tructure-{F}unction {R}elationships of {A}ldo-{K}eto
                      {R}eductase 1{B}15: {A} {N}ovel {H}uman {R}etinaldehyde
                      {R}eductase},
      journal      = {PLoS one},
      volume       = {10},
      number       = {7},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2016-01549},
      pages        = {e0134506 -},
      year         = {2015},
      abstract     = {Human aldo-keto reductase 1B15 (AKR1B15) is a newly
                      discovered enzyme which shares $92\%$ amino acid sequence
                      identity with AKR1B10. While AKR1B10 is a well characterized
                      enzyme with high retinaldehyde reductase activity, involved
                      in the development of several cancer types, the enzymatic
                      activity and physiological role of AKR1B15 are still poorly
                      known. Here, the purified recombinant enzyme has been
                      subjected to substrate specificity characterization, kinetic
                      analysis and inhibitor screening, combined with structural
                      modeling. AKR1B15 is active towards a variety of carbonyl
                      substrates, including retinoids, with lower kcat and Km
                      values than AKR1B10. In contrast to AKR1B10, which strongly
                      prefers all-trans-retinaldehyde, AKR1B15 exhibits superior
                      catalytic efficiency with 9-cis-retinaldehyde, the best
                      substrate found for this enzyme. With ketone and dicarbonyl
                      substrates, AKR1B15 also shows higher catalytic activity
                      than AKR1B10. Several typical AKR inhibitors do not
                      significantly affect AKR1B15 activity. Amino acid
                      substitutions clustered in loops A and C result in a
                      smaller, more hydrophobic and more rigid active site in
                      AKR1B15 compared with the AKR1B10 pocket, consistent with
                      distinct substrate specificity and narrower inhibitor
                      selectivity for AKR1B15.},
      cin          = {INM-9 / IAS-5},
      ddc          = {500},
      cid          = {I:(DE-Juel1)INM-9-20140121 / I:(DE-Juel1)IAS-5-20120330},
      pnm          = {574 - Theory, modelling and simulation (POF3-574)},
      pid          = {G:(DE-HGF)POF3-574},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000358836800146},
      pubmed       = {pmid:26222439},
      doi          = {10.1371/journal.pone.0134506},
      url          = {https://juser.fz-juelich.de/record/281887},
}