The influence of potassium on folding parameters of porcine kidney betaine aldehyde dehydrogenase

Jesús A. Rosas-Rodríguez, Mario Almada, Luis Alberto Zamora-Álvarez, Anabel Félix-Arredondo, David Encinas-Basurto, Edgar F. Moran-Palacio, Sergio G. Hernandez-Leon, Elisa M. Valenzuela-Soto, César Muñoz-Bacasehua*

*Autor correspondiente de este trabajo

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

Resumen

Porcine kidney betaine aldehyde dehydrogenase (pkBADH) uses NAD+ as a coenzyme to convert betaine aldehyde to glycine betaine. In previous studies we described the impact of potassium on the affinity of pkBADH for NAD+, the effect on the tertiary and secondary structure, and changes in the flexibility of the amino acids involved in the formation of the pkBADH-NAD+. However, there are still unanswered questions about how K+ influences the folding and maintenance of the quaternary structure. Thus, this work aims to analyze the impact of the K+ concentration on the enzyme's folding and thermal stability parameters. Fluorescence data indicate that thermal stability is dependent on the K+ concentration. The analysis of (Tm)app from pkBADH showed a value of 44.5 °C; addition of 25 mM, 50 mM, and 100 mM K+ increased the (Tm)app to 48.8 °C or 50.7 and 51.0 °C, respectively. The analysis of the thermodynamic parameters indicates that the thermal stability of the pkBADH structure increases depending on the concentration of K+, and the molecular dynamics simulation of pkBADH results in better structural stability in presence of potassium ions, as evidenced by more minor fluctuations and lower root mean square deviation (RMSD) values compared to the system without K+.

Idioma originalInglés
Número de artículo151065
PublicaciónBiochemical and Biophysical Research Communications
Volumen742
DOI
EstadoPublicada - ene. 2025

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