TY - JOUR
T1 - The influence of potassium on folding parameters of porcine kidney betaine aldehyde dehydrogenase
AU - Rosas-Rodríguez, Jesús A.
AU - Almada, Mario
AU - Zamora-Álvarez, Luis Alberto
AU - Félix-Arredondo, Anabel
AU - Encinas-Basurto, David
AU - Moran-Palacio, Edgar F.
AU - Hernandez-Leon, Sergio G.
AU - Valenzuela-Soto, Elisa M.
AU - Muñoz-Bacasehua, César
N1 - Publisher Copyright:
© 2024 Elsevier Inc.
PY - 2025/1
Y1 - 2025/1
N2 - 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+.
AB - 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+.
KW - Betaine aldehyde dehydrogenase
KW - Conformational changes
KW - Folding parameters
KW - Molecular dynamics
KW - Potassium
UR - http://www.scopus.com/inward/record.url?scp=85210749946&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2024.151065
DO - 10.1016/j.bbrc.2024.151065
M3 - Artículo
C2 - 39626370
AN - SCOPUS:85210749946
SN - 0006-291X
VL - 742
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
M1 - 151065
ER -