Enolase: Difference between revisions

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==Kinetics==
==Kinetics==
[[Image:enolase kinetics.jpeg|left|250px|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|200px|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 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.