Allen sandbox 1: Difference between revisions
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Enolase is in the Alpha and Beta protein class (mainly parallel beta sheets) and has a fold of TIM beta/alpha-barrel, which consists of parallel barrels composed of beta sheets. Enolase also belongs to the Enolase C-terminal domain-like protein Superfamily, which means it can bind metal ions (magnesium or manganese) in a conserved site inside barrel N-terminal alpha+beta domains. | Enolase is in the Alpha and Beta protein class (mainly parallel beta sheets) and has a fold of TIM beta/alpha-barrel, which consists of parallel barrels composed of beta sheets. Enolase also belongs to the Enolase C-terminal domain-like protein Superfamily, which means it can bind metal ions (magnesium or manganese) in a conserved site inside barrel N-terminal alpha+beta domains. | ||
==Mechanism== | ==Mechanism== | ||
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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>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 without the need for additional substrate<ref>{{journal2}}</ref>. | ||
==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 cells such as monocytes, T cells and B cells, neuronal cells and endothelial cells. Enolase in muscle cells can bind other glycolytic enzymes, such as phosphoglycerate mutase, muscle creatine kinase, pyruvate kinase, and muscle troponin, with high affinity. This suggests that enolase helps facilitate muscle contraction by creating a functional glycolytic segment in the muscle where ATP production occurs. Myc-binding protein (MBP-1) is similar to the α-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 cells such as monocytes, T cells and B cells, neuronal cells and endothelial cells. Enolase in muscle cells can bind other glycolytic enzymes, such as phosphoglycerate mutase, muscle creatine kinase, pyruvate kinase, and muscle troponin, with high affinity. This suggests that enolase helps facilitate muscle contraction by creating a functional glycolytic segment in the muscle where ATP production occurs. Myc-binding protein (MBP-1) is similar to the α-enolse structure and is found in the nucleus as a DNA-binding protein<ref>{{journal}}</ref>. | ||
Additional levels of enolase regulation occur through the addition of flouride ion, F-. | Additional levels of enolase regulation occur through the addition of flouride ion, F-. F- forms a complex with Mg2+ already bound at the enzyme's active site. This blocks enolase from binding the substrate 2PG, causing it to build up and thereby slowing the process of glycolysis. | ||
==Additional Resources== | ==Additional Resources== | ||
