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@ARTICLE{Amariei:911150,
      author       = {Amariei, Diana A. and Pozhydaieva, Nadiia and David, Benoit
                      and Schneider, Pascal and Classen, Thomas and Gohlke, Holger
                      and Weiergräber, Oliver H. and Pietruszka, Jörg},
      title        = {{E}nzymatic {C}3-{M}ethylation of {I}ndoles {U}sing
                      {M}ethyltransferase {P}sm{D}─{C}rystal {S}tructure,
                      {C}atalytic {M}echanism, and {P}reparative {A}pplications},
      journal      = {ACS catalysis},
      volume       = {12},
      number       = {22},
      issn         = {2155-5435},
      address      = {Washington, DC},
      publisher    = {ACS},
      reportid     = {FZJ-2022-04465},
      pages        = {14130 - 14139},
      year         = {2022},
      abstract     = {Enantioselective methylation is a challenging task in
                      organic chemistry, yet often desirable in drug discovery and
                      optimization. S-Adenosyl methionine (SAM)-dependent
                      methyltransferases (MTases) offer a selective alternative to
                      chemical synthesis and an abundance of potential scaffolds.
                      The crystal structure of C3-indole MTase PsmD from
                      Streptomyces griseofuscus, involved in the biosynthesis of
                      the acetylcholinesterase inhibitor physostigmine, was
                      determined via X-ray crystallography. The amino acid
                      residues essential for catalysis were identified by
                      site-directed mutagenesis, and a mechanism of action was
                      proposed. Furthermore, a PsmD ortholog was identified and
                      characterized. The variant catalyzed enantioselective
                      C-methylation over a broad substrate scope while displaying
                      increased stability. Using this enzyme, preparative-scale
                      enzymatic methylation was performed in cell-free extracts in
                      combination with an SAM recycling system, eliminating the
                      need for cofactor supplementation.},
      cin          = {IBG-4 / IBI-7 / IBOC / IBG-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBG-4-20200403 / I:(DE-Juel1)IBI-7-20200312 /
                      I:(DE-Juel1)IBOC-20090406 / I:(DE-Juel1)IBG-1-20101118},
      pnm          = {2171 - Biological and environmental resources for
                      sustainable use (POF4-217) / 5241 - Molecular Information
                      Processing in Cellular Systems (POF4-524)},
      pid          = {G:(DE-HGF)POF4-2171 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000881780200001},
      doi          = {10.1021/acscatal.2c04240},
      url          = {https://juser.fz-juelich.de/record/911150},
}