Allen sandbox 1: Difference between revisions

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 ==Kinetics==
 [[Image:enolase kinetics.jpeg|left|150px|V vs. [PGA]; PGA is 2PG, the top curve has [Mg2+] of 10^-3 M and the bottom curve has [Mg2+] of 106-2 M]]<ref>{{journal2}}</ref>
-Since Mg2+ is essential for binding the substrate, 2-PG, it is also needed at a specific quality in order to have a good rate, or velocity.  The graph shows the V vs. [PGA], in which PGA is 2-PG, with two different concentrations of Mg2+.  The upper curve, which also has greater Vmax, has an Mg2+ concentration of 10^-3 M while the lower curve, which has a lower Vmax, has an Mg2+ concentration of 10^-2 M<ref>{{journal2}}</ref>.  The Km is also larger the upper curve making the higher [Mg2+] more desirable.
+Since Mg2+ is essential for binding the substrate, 2-PG, it is also needed at a specific quantity in order to have a sufficient reaction velocity.  This graph shows the Velocity vs. [PGA], in which PGA is 2-PG, at two different concentrations of Mg2+.  The upper curve (Mg2+ concentration of 10^-3 M) attains a greater Vmax than the lower curve (Mg2+ concentration of 10^-2 M)<ref>{{journal2}}</ref>. The Km of upper curve is also larger than the lower curve, which means a greater concentration of substrate is needed to attain the higher Vmax. Therefore, the lower Mg2+ concentration (upper curve) is more desirable. Clearly, upon addition of Mg2+, the reaction velocity is lowered to sub-optimum levels, thereby inhibiting the activity of enolase.