BADH-NAD+-K+ Complex Interaction Studies Reveal a New Possible Mechanism between Potassium and Glutamic 254 at the Coenzyme Binding Site

César Muñoz-Bacasehua, Hisila Santacruz-Ortega, Elisa M. Valenzuela-Soto*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Betaine aldehyde dehydrogenase (BADH EC 1.2.1.8) catalyzes the irreversible oxidation of betaine aldehyde to glycine betaine using NAD+ as a coenzyme. Incubation of porcine kidney BADH (pkBADH) with NAD+ decreases the catalytic cysteine (C288) reactivity. Potassium ion increases the pkBADH affinity by the coenzyme. This work aimed to analyze pkBADH and NAD+ interaction in the presence and absence of K+ using 1H NMR to identify the amino acids that interact with NAD+ and/or K+ to understand the regulation process of pkBADH-NAD+ complex formation mediated by the K+ ion and their impact on the substrate binding and catalysis. Nuclear magnetic resonance spectra of pkBADH were obtained in the presence and absence of NAD+ and K+. The results show a chemical shift of the signals corresponding to the catalytic glutamic that participates in the transfer of H+ in the reaction of the pkBADH-NAD+-K+ complex formation. Furthermore, there is a widening of the signal that belongs to the catalytic cysteine indicating higher rigidity or less grade of rotation of the structure, which is consistent with the possible conformations of C288 in the catalytic process; in addition, there is evidence of changes in the chemical environment that surrounds NAD+.

Original languageEnglish
Pages (from-to)39-44
Number of pages6
JournalCell Biochemistry and Biophysics
Volume80
Issue number1
DOIs
StatePublished - Mar 2022
Externally publishedYes

Bibliographical note

Funding Information:
CMB gratefully acknowledges a scholarship from CONACyT for graduate studies.

Publisher Copyright:
© 2021, The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.

Keywords

  • Betaine aldehyde dehydrogenase
  • Cysteine reactivity
  • Glycine betaine
  • Monovalent cations
  • NAD binding

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