% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Funke:626476,
      author       = {Funke, Franziska Jasmin and Schlee, Sandra and Bento,
                      Isabel and Bourenkov, Gleb and Sterner, Reinhard and
                      Wilmanns, Matthias},
      title        = {{A}ctivity {R}egulation of a {G}lutamine {A}midotransferase
                      {B}ienzyme {C}omplex by {S}ubstrate-{I}nduced {S}ubunit
                      {I}nterface {E}xpansion},
      journal      = {ACS catalysis},
      volume       = {15},
      number       = {5},
      issn         = {2155-5435},
      address      = {Washington, DC},
      publisher    = {ACS},
      reportid     = {PUBDB-2025-01440},
      pages        = {4359 - 4373},
      year         = {2025},
      abstract     = {Glutamine amidotransferases are multienzyme machineries in
                      which reactive ammonia is generated by a glutaminase and
                      then transferred through a sequestered protein tunnel to a
                      synthase active site for incorporation into diverse
                      metabolites. To avoid wasteful metabolite consumption, there
                      is a requirement for synchronized catalysis, but any
                      generally applicable mechanistic insight is still lacking.
                      As synthase activity depends on glutamine turnover, we
                      investigated possible mechanisms controlling glutaminase
                      catalysis using aminodeoxychorismate synthase involved in
                      folate biosynthesis as a model. By analyzing this system in
                      distinct states of catalysis, we found that incubation with
                      glutamine leads to a subunit interface expansion by
                      one-third of its original area. These changes completely
                      enclose the glutaminase active site for sequestered
                      catalysis and the subsequent transport of volatile ammonia
                      to the synthase active site. In view of similar
                      rearrangements in other glutamine amidotransferases, our
                      observations may provide a general mechanism for the
                      catalysis synchronization of this multienzyme family.},
      cin          = {EMBL-User / EMBL / CSSB-CF-SPC},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731 /
                      I:(DE-H253)CSSB-CF-SPC-20210520},
      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       = {40365074},
      UT           = {WOS:001433007100001},
      doi          = {10.1021/acscatal.4c07438},
      url          = {https://bib-pubdb1.desy.de/record/626476},
}