Enolase: Difference between revisions
David Canner (talk | contribs) No edit summary |
David Canner (talk | contribs) No edit summary |
||
| Line 4: | Line 4: | ||
==Structure== | ==Structure== | ||
The <scene name='Cory_Tiedeman_Sandbox_1/Secondary_structure/1'>secondary structure</scene> of enolase contains both alpha helices and beta sheets. The beta sheets are mainly parallel<ref>{{web site| title=SCOP: Protein: Enolase from Baker's yeast (Saccharomyces cerevisiae)|url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.b.bc.b.b.html|}}</ref>. As shown in the figure, enolase has about 36 alpha helices and 22 beta sheets (18 alpha helices and 11 beta sheets per domain). Enolase consists of two domains. | The <scene name='Cory_Tiedeman_Sandbox_1/Secondary_structure/1'>secondary structure</scene> of enolase contains both alpha helices and beta sheets. The beta sheets are mainly parallel<ref>{{web site| title=SCOP: Protein: Enolase from Baker's yeast (Saccharomyces cerevisiae)|url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.b.bc.b.b.html|}}</ref>. As shown in the figure, enolase has about 36 alpha helices and 22 beta sheets (18 alpha helices and 11 beta sheets per domain). Enolase consists of two domains. | ||
'''Structural Clasification of Proteins (SCOP)<ref>{{web site| title=SCOP: Protein: Enolase from Baker's yeast (Saccharomyces cerevisiae)|url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.b.bc.b.b.html|}}</ref>''' | '''Structural Clasification of Proteins (SCOP)<ref>{{web site| title=SCOP: Protein: Enolase from Baker's yeast (Saccharomyces cerevisiae)|url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.b.bc.b.b.html|}}</ref>''' | ||
Enolase is in the alpha and beta proteins class and has a fold of TIM beta/alpha-barrel. It comes from the Superfamily on Enolase C-terminal domain-like and is in the enolase family. | Enolase is in the alpha and beta proteins class and has a fold of TIM beta/alpha-barrel. It comes from the Superfamily on Enolase C-terminal domain-like and is in the enolase family. | ||
==Mechanism== | ==Mechanism== | ||
| Line 21: | Line 19: | ||
==Kinetics== | ==Kinetics== | ||
[[Image:enolase kinetics.jpeg|left| | [[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> | ||
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. | ||
==Regulation== | ==Regulation== | ||