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@ARTICLE{Lu:642757,
      author       = {Lu, Zixuan and Witek, Wojciech and Ruszkowski, Milosz and
                      Imiolczyk, Barbara and Paulish, Nataliya and Joshi, Jaya and
                      Jaskolski, Mariusz and Marsolais, Frédéric},
      title        = {{B}enzoic and salicylic acids inhibit β-substituted
                      alanine synthase 4;1 in common bean},
      journal      = {Plant physiology},
      volume       = {199},
      number       = {3},
      issn         = {0032-0889},
      address      = {Oxford},
      publisher    = {Oxford University Press},
      reportid     = {PUBDB-2025-05606},
      pages        = {kiaf485},
      year         = {2025},
      abstract     = {The nutritionally essential sulfur amino acids, methionine
                      and cysteine, are present at suboptimal levels in legumes,
                      such as common bean (Phaseolus vulgaris L.). β-Substituted
                      alanine synthase 4;1 (BSAS4;1) is the major isoform of
                      cytosolic cysteine synthase present in the developing seeds
                      of common bean. There is evidence that in addition to
                      cysteine, this enzyme is also involved in the biosynthesis
                      of the non-proteinogenic amino acid S-methylcysteine, which
                      accumulates in the form of a γ-glutamyl dipeptide. Here, we
                      report the high-resolution structure of recombinant BSAS4;1.
                      Unexpectedly, the crystal structure showed the presence of a
                      molecule of benzoic acid near the active site, which
                      appeared to have been co-purified from Escherichia coli.
                      Kinetic analysis indicated that benzoic acid acts as a
                      competitive inhibitor of BSAS4;1 with respect to
                      O-acetylserine. IC50 values for benzoic acid and the
                      structurally related salicylic acid were both equal to
                      0.6 mm. Using developing cotyledons grown in vitro,
                      quantification of the incorporation of 13C3- and 15N-labeled
                      serine into cysteine and downstream metabolites indicated
                      that benzoic acid effectively inhibited cysteine
                      biosynthesis in vivo at a concentration of 1.2 mm. The
                      results of experiments tracking the incorporation of
                      13C-labeled sodium thiomethoxide provided further evidence
                      that BSAS4;1 may be involved in the formation of free
                      S-methylcysteine, through the condensation of O-acetylserine
                      with methanethiol.},
      cin          = {EMBL-User},
      ddc          = {580},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1093/plphys/kiaf485},
      url          = {https://bib-pubdb1.desy.de/record/642757},
}