required for maintenance of its active conformation. At low concentrations, the enzyme is totally inactivated upon removal of K+. NAD+ protects against inactivation by absence of K+, betaine aldehyde affords partial protection. NH4+ but not Na+ can mimic the effect of K+. At pH 7.0 in the absence of K+ in a buffer of low ionic strength, the active tetrameric form dissociates into inactive monomers
required for maintenance of its active conformation. At low concentrations, the enzyme is totally inactivated upon removal of K+. NAD+ protects against inactivation by absence of K+, betaine aldehyde incrrases the inactivation rate of the enzyme. NH4+ but not Na+ can mimic the effect of K+. At pH 7.0 in the absence of K+ in a buffer of low ionic strength, the active tetrameric form dissociates into inactive monomers
presence of K+ stabilizes the enzyme secondary structure and maintains its alpha-helix content. K+ increases the thermal stability of the pkBADHNAD+ complex by 5.3°C
required for binding of cofactor NAD+. K+ causes small changes in secondary and tertiary structures that influences the active site conformation, binding of K+ to the enzyme caused changes in the alpha-helix content of 4% and 12% in the presence of 25 mM and 100 mM K+, respectively