Allen sandbox 1: Difference between revisions
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==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-. Upon F- addition, it forms a complex with Mg2+ already bound at th enzyme's active site. This blocks enolase from binding the substrate 2PG, causing it to build up and thereby slowing glycolysis. | |||
==Additional Resources== | ==Additional Resources== | ||