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@ARTICLE{Nowak:626505,
      author       = {Nowak, Jan S. and Olesen, Sune and Tian, Pengfei and
                      Bærentsen, René L. and Brodersen, Ditlev E. and Otzen,
                      Daniel E.},
      title        = {{R}ole of electrostatics in cold adaptation: {A}
                      comparative study of eury- and stenopsychrophilic triose
                      phosphate isomerase},
      journal      = {Biochimica et biophysica acta / Proteins and proteomics},
      volume       = {1873},
      number       = {4},
      issn         = {0006-3002},
      address      = {Amsterdam [u.a.]},
      publisher    = {[Verlag nicht ermittelbar]},
      reportid     = {PUBDB-2025-01458},
      pages        = {141072},
      year         = {2025},
      abstract     = {Psychrophilic (cold-active) organisms have developed
                      enzymes that facilitate sufficient metabolic activity at low
                      temperatures to sustain life. This occurs through molecular
                      adaptations that tend to increase protein flexibility at the
                      expense of stability. However, psychrophiles also vary in
                      their growth conditions. Eurypsychrophiles thrive over a
                      wide temperature range and often prefer temperatures above
                      20 °C, while stenopsychrophiles grow optimally below 15 °C
                      and are more narrowly adapted to cold temperatures. To
                      elucidate differences between these two classes of enzymes,
                      we here compare the stability and unfolding kinetics of two
                      orthologues of the basal household enzyme triose phosphate
                      isomerase, one from the stenopsychrophilic Antarctic
                      permafrost bacterium Rhodonellum psychrophilum (sTPI) and
                      the other from the eurypsychrophilic Greenland ikaite column
                      bacterium Rhodococcus sp. JG-3 (eTPI). Remarkably, sTPI
                      proved significantly more thermostable and resistant to
                      chemical denaturation than its eurypsychrophilic
                      counterpart, eTPI, in the absence of ionic components in
                      solution, whereas inclusion of electrostatic screening
                      agents in the form of sodium chloride or the charged
                      denaturant guanidinium chloride largely cancelled out this
                      difference. Thus, electrostatics play a prominent role in
                      stabilizing the stenopsychrophilic sTPI, and a mandatory
                      low-temperature growth environment does not preclude the
                      development of considerable thermotolerance for individual
                      enzymes. We were able to increase the thermostability of
                      sTPI using an evolutionary machine learning model, which
                      transferred several sTPI residues into the eTPI active site.
                      While the stabilizing effect was modest, the combination of
                      individual mutations was additive, underscoring the
                      potential of combining multiple beneficial mutations to
                      achieve enhanced enzyme properties.},
      cin          = {EMBL-User},
      ddc          = {570},
      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-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {40220927},
      UT           = {WOS:001472890600001},
      doi          = {10.1016/j.bbapap.2025.141072},
      url          = {https://bib-pubdb1.desy.de/record/626505},
}