Cory Tiedeman Sandbox 1: Difference between revisions
No edit summary |
No edit summary |
||
| Line 6: | Line 6: | ||
==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). | 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. | ||
| Line 24: | Line 24: | ||
==Kinetics== | ==Kinetics== | ||
[[Image:enolase kinetics.jpeg|left| | [[Image:enolase kinetics.jpeg|left|150px]]<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== | ||
Enolase is found on the surface of a variety of eukaryotic cells as a strong plamingoen-binding receptor and on the surface of hematopietic celss such as monocytes, T cells and B cells, neuronal celss and endothelial cells. Enolase in muscle can bind other glycolytic enzymes, such as phosphoglycerate mutase, muscle creatine kinase, pyruvate kinase, and muscle troponin, with high affinity. This suggests that they make a functional glycolytic segment in the muscle where ATP production is required in order for the muscle to contract. Myc-binding protein (MBP-1) is similar to the a-enolse structure and is found in the nucleus as a DNA-binding protein<ref>{{journal}}</ref>. | Enolase is found on the surface of a variety of eukaryotic cells as a strong plamingoen-binding receptor and on the surface of hematopietic celss such as monocytes, T cells and B cells, neuronal celss and endothelial cells. Enolase in muscle can bind other glycolytic enzymes, such as phosphoglycerate mutase, muscle creatine kinase, pyruvate kinase, and muscle troponin, with high affinity. This suggests that they make a functional glycolytic segment in the muscle where ATP production is required in order for the muscle to contract. Myc-binding protein (MBP-1) is similar to the a-enolse structure and is found in the nucleus as a DNA-binding protein<ref>{{journal}}</ref>. | ||
Enolase is regulated by the concentration of Mg2+ and the previous steps of glycolysis. | |||
==References== | ==References== | ||
<references/> | <references/> | ||