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>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>.

[[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 at essentially the same Km value; a greater Vmax can be attained without the need for additional substrate<ref>{{journal2}}</ref>.

==Regulation==

Allen sandbox 1: Difference between revisions

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@@ Line 36: / Line 36: @@
 ==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>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>.
+[[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 at essentially the same Km value; a greater Vmax can be attained without the need for additional substrate<ref>{{journal2}}</ref>.
 ==Regulation==