Allen sandbox 1: Difference between revisions

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==Kinetics==
==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>
[[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>The kinetics of the enolase reaction can be affected by the concentration of magnesium ion, Mg2+. The graph to the left shows velocity vs. [PGA], in which PGA stands for 2-PG. The upper curve is the reaction at normal [Mg2+], 0.01 M, while the lower curve shows the same reaction at an increased concentration of [MG2+], 0.1 M. This shows that upon addition of Mg2+, the Vmax is lowered to sub-optimal levels, while the Km remains relatively unchanged. Therefore, the upper curve (lower [Mg2+] is more desirable because it achieves a greater Vmax without the need for additional substrate<ref>{{journal2}}</ref>.
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.  
 
 
 
 
 
 
 
 
 
 


==Regulation==
==Regulation==

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Justin Allen