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@ARTICLE{Dall:894963,
      author       = {Dall, Elfriede and Stanojlovic, Vesna and Demir, Fatih and
                      Briza, Peter and Dahms, Sven O. and Huesgen, Pitter F. and
                      Cabrele, Chiara and Brandstetter, Hans},
      title        = {{T}he {P}eptide {L}igase {A}ctivity of {H}uman {L}egumain
                      {D}epends on {F}old {S}tabilization and {B}alanced
                      {S}ubstrate {A}ffinities},
      journal      = {ACS catalysis},
      volume       = {11},
      number       = {19},
      issn         = {2155-5435},
      address      = {Washington, DC},
      publisher    = {ACS},
      reportid     = {FZJ-2021-03503},
      pages        = {11885 - 11896},
      year         = {2021},
      abstract     = {Protein modification by enzymatic breaking and forming of
                      peptide bonds significantly expands the repertoire of
                      genetically encoded protein sequences. The dual
                      protease-ligase legumain exerts the two opposing activities
                      within a single protein scaffold. Primarily localized to the
                      endolysosomal system, legumain represents a key enzyme in
                      the generation of antigenic peptides for subsequent
                      presentation on the MHCII complex. Here we show that human
                      legumain catalyzes the ligation and cyclization of linear
                      peptides at near-neutral pH conditions, where legumain is
                      intrinsically unstable. Conformational stabilization
                      significantly enhanced legumain’s ligase activity, which
                      further benefited from engineering the prime substrate
                      recognition sites for improved affinity. Additionally, we
                      provide evidence that specific legumain activation states
                      allow for differential regulation of its activities.
                      Together these results set the basis for engineering
                      legumain proteases and ligases with applications in
                      biotechnology and drug development.},
      cin          = {ZEA-3},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ZEA-3-20090406},
      pnm          = {2171 - Biological and environmental resources for
                      sustainable use (POF4-217) / ProPlantStress - Proteolytic
                      processing in plant stress signal transduction and responses
                      to abiotic stress and pathogen attack (639905)},
      pid          = {G:(DE-HGF)POF4-2171 / G:(EU-Grant)639905},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {34621593},
      UT           = {WOS:000704700800008},
      doi          = {10.1021/acscatal.1c02057},
      url          = {https://juser.fz-juelich.de/record/894963},
}