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