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@ARTICLE{Qin:613905,
      author       = {Qin, Chuan and Graf, Leonie G. and Striska, Kilian and
                      Janetzky, Markus and Geist, Norman and Specht, Robin and
                      Schulze, Sabrina and Palm, Gottfried and Girbardt, Britta
                      and Dörre, Babett and Berndt, Leona and Kemnitz, Stefan and
                      Doerr, Mark and Bornscheuer, Uwe T. and Delcea, Mihaela and
                      Lammers, Michael},
      title        = {{A}cetyl-{C}o{A} synthetase activity is enzymatically
                      regulated by lysine acetylation using acetyl-{C}o{A} or
                      acetyl-phosphate as donor molecule},
      journal      = {Nature Communications},
      volume       = {15},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {PUBDB-2024-05684},
      pages        = {6002},
      year         = {2024},
      note         = {German Research Foundation grant No. LA2984-6/1 and
                      LA2984-8/1 (DFG, Deutsche Forschungsgemeinschaft).},
      abstract     = {The AMP-forming acetyl-CoA synthetase is regulated by
                      lysine acetylation both in bacteria and eukaryotes. However,
                      the underlying mechanism is poorly understood. The Bacillus
                      subtilis acetyltransferase AcuA and the AMP-forming
                      acetyl-CoA synthetase AcsA form an AcuA•AcsA complex,
                      dissociating upon lysine acetylation of AcsA by AcuA.
                      Crystal structures of AcsA from Chloroflexota bacterium in
                      the apo form and in complex with
                      acetyl-adenosine-5′-monophosphate (acetyl-AMP) support the
                      flexible C-terminal domain adopting different conformations.
                      AlphaFold2 predictions suggest binding of AcuA stabilizes
                      AcsA in an undescribed conformation. We show the AcuA•AcsA
                      complex dissociates upon acetyl-coenzyme A (acetyl-CoA)
                      dependent acetylation of AcsA by AcuA. We discover an
                      intrinsic phosphotransacetylase activity enabling
                      AcuA•AcsA generating acetyl-CoA from acetyl-phosphate
                      (AcP) and coenzyme A (CoA) used by AcuA to acetylate and
                      inactivate AcsA. Here, we provide mechanistic insights into
                      the regulation of AMP-forming acetyl-CoA synthetases by
                      lysine acetylation and discover an intrinsic
                      phosphotransacetylase allowing modulation of its activity
                      based on AcP and CoA levels.},
      cin          = {EMBL-User},
      ddc          = {500},
      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},
      pubmed       = {pmid:39019872},
      UT           = {WOS:001272173500031},
      doi          = {10.1038/s41467-024-49952-0},
      url          = {https://bib-pubdb1.desy.de/record/613905},
}