The kinetic properties of the wild-type and Tyr⁵⁷Trp mutant form of human muscle FBPase.

<p>The dissociation constant of the enzyme-substrate complex (<i>K_s</i>), the inhibition constant of FBPase by its substrate (<i>K_is</i>) and β values were calculated assuming the model of partial noncompetitive inhibition by substrate <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0076669#pone.0076669-Rakus3" target="_blank">[18]</a>.</p><p>The Hill equation was used to calculate dissociation constants for Mg²⁺, Ca²⁺ and AMP.</p><p><i>K_i</i> is a dissociation (inhibitory) constant for AMP or Ca²⁺, <i>K_a</i> is a dissociation (activatory) constant for Mg²⁺ and <i>n</i> is the Hill constant.</p><p>The mean values and respective standard error calculated from 3 independent experiments are presented in the Table.