“…A possible mechanism was proposed whereby high K + concentrations could influence the chemical environment in the catalytic center, leading to increased affinity for NAD + . 24,25 Initially, addition of 500 mM KCl was attempted. The activity of SpALDH2 remained unchanged while the activity of SpALDH1 increased by approximately 5-fold, indicating that SpALDH1 is K + -activated.…”
SpALDH1 and SpALDH2 from Sphingobium sp. SYK-6 exhibit distinct enzymatic properties. Computational simulation reveals that the different substrate specificity could be attributed to the hydrophobicity of substrate binding pockets.
“…A possible mechanism was proposed whereby high K + concentrations could influence the chemical environment in the catalytic center, leading to increased affinity for NAD + . 24,25 Initially, addition of 500 mM KCl was attempted. The activity of SpALDH2 remained unchanged while the activity of SpALDH1 increased by approximately 5-fold, indicating that SpALDH1 is K + -activated.…”
SpALDH1 and SpALDH2 from Sphingobium sp. SYK-6 exhibit distinct enzymatic properties. Computational simulation reveals that the different substrate specificity could be attributed to the hydrophobicity of substrate binding pockets.
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