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@ARTICLE{Konjik:119340,
      author       = {V. Konjik and S. Brünle and U. Demmer and A. Vanselow and
                      R. Sandhoff$^*$ and U. Ermler and M. Mack},
      title        = {{T}he {C}rystal {S}tructure of {R}os{B}: {I}nsights into
                      the {R}eaction {M}echanism of the {F}irst {M}ember of a
                      {F}amily of {F}lavodoxin-like {E}nzymes.},
      journal      = {Angewandte Chemie / International edition},
      volume       = {56},
      number       = {4},
      issn         = {1433-7851},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {DKFZ-2017-00095},
      pages        = {1146 - 1151},
      year         = {2017},
      abstract     = {8-demethyl-8-aminoriboflavin-5'-phosphate (AFP) synthase
                      (RosB) catalyzes the key reaction of roseoflavin
                      biosynthesis by forming AFP from riboflavin-5'-phosphate
                      (RP) and glutamate via the intermediates
                      8-demethyl-8-formylriboflavin-5'-phosphate (OHC-RP) and
                      8-demethyl-8-carboxylriboflavin-5'-phosphate (HO2 C-RP). To
                      understand this reaction in which a methyl substituent of an
                      aromatic ring is replaced by an amine we structurally
                      characterized RosB in complex with OHC-RP (2.0 Å) and AFP
                      (1.7 Å). RosB is composed of four flavodoxin-like
                      subunits which have been upgraded with specific extensions
                      and a unique C-terminal arm. It appears that RosB has
                      evolved from an electron- or hydride-transferring
                      flavoprotein to a sophisticated multi-step enzyme which uses
                      RP as a substrate (and not as a cofactor). Structure-based
                      active site analysis was complemented by mutational and
                      isotope-based mass-spectrometric data to propose an
                      enzymatic mechanism on an atomic basis.},
      cin          = {G131},
      ddc          = {540},
      cid          = {I:(DE-He78)G131-20160331},
      pnm          = {317 - Translational cancer research (POF3-317)},
      pid          = {G:(DE-HGF)POF3-317},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:27981706},
      doi          = {10.1002/anie.201610292},
      url          = {https://inrepo02.dkfz.de/record/119340},
}