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Structural and evolutionary analysis unveil functional adaptations in the promiscuous behavior of serum albumins
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  • Ana Julia Velez Rueda,
  • Guillermo Ignacio Benitez,
  • Leandro Matías Sommese,
  • Sebastián Ardanaz,
  • Estefanía Borucki,
  • Nicolas Palopoli,
  • Luis Iglesias,
  • gustavo parisi
Ana Julia Velez Rueda
Universidad Nacional de Quilmes
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Guillermo Ignacio Benitez
Universidad Nacional de Quilmes
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Leandro Matías Sommese
Universidad Nacional de Quilmes
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Sebastián Ardanaz
Universidad Nacional de Quilmes
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Estefanía Borucki
Universidad Nacional de Quilmes
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Nicolas Palopoli
Universidad Nacional de Quilmes
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Luis Iglesias
Universidad Nacional de Quilmes
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gustavo parisi
Universidad Nacional de Quilmes
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Abstract

Promiscuous activities have been related to the capacity to catalyze reactions different from those a protein has evolved to sustain. From this evolutionary perspective, we rethought the serum albumins promiscuous behavior. We found that the cross aldol condensation of acetone and p-formylbenzonitrile is a promiscuous reaction conserved in humans and other mammals. Structural and evolutionary analysis indicates that the involved residues could have evolved for a still unknown biological function. Our results could contribute to better characterize the serum albumin family and raise questions about the evolution of protein promiscuity and function.

Peer review status:UNDER REVIEW

03 May 2021Submitted to PROTEINS: Structure, Function, and Bioinformatics
04 May 2021Assigned to Editor
04 May 2021Submission Checks Completed
11 May 2021Reviewer(s) Assigned
10 Jun 2021Review(s) Completed, Editorial Evaluation Pending