Role of potassium levels in pkBADH heterogeneity of NAD+ binding site.

Journal of Bioenergetics and Biomembranes
César Muñoz-BacasehuaElisa M Valenzuela-Soto

Abstract

Betaine aldehyde dehydrogenase (BADH) catalyzes the oxidation of betaine aldehyde to glycine betaine using NAD+ as a coenzyme. Studies in porcine kidney BADH (pkBADH) suggested that the enzyme exhibits heterogeneity of active sites and undergoes potassium-induced conformational changes. This study aimed to analyze if potassium concentration plays a role in the heterogeneity of pkBADH active sites through changes in NAD+ affinity constants, in its secondary structure content and stability. The enzyme was titrated with NAD+ 1 mM at fixed-variable KCl concentration, and the interaction measured by Isothermal Titration Calorimetry (ITC) and Circular Dichroism (CD). ITC data showed that K+ increased the first active site affinity in a manner dependent on its concentration; KD values to the first site were 14.4, 13.1, and 10.4 μM, at 25, 50, and 75 mM KCl. ΔG values showed that the coenzyme binding is a spontaneous reaction without changes between active sites or depending on KCl concentration. ΔH and TΔSb values showed that NAD+ binding to the active site is an endothermic process and is carried out at the expense of changes in entropy. α-Helix content increased as KCl increased, enzyme (Tm)app values were 2.6 °C and 3.3 °C higher a...Continue Reading

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Sep 4, 2020·Journal of Molecular Recognition : JMR·César Muñoz-BacasehuaElisa M Valenzuela-Soto

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Citations

Sep 4, 2020·Journal of Molecular Recognition : JMR·César Muñoz-BacasehuaElisa M Valenzuela-Soto
Jan 4, 2021·Molecular and Cellular Biochemistry·Ramses Cruz-ValenciaElisa M Valenzuela-Soto
Jul 3, 2021·Luminescence : the Journal of Biological and Chemical Luminescence·César Muñoz-BacasehuaElisa M Valenzuela-Soto

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