Allen sandbox 1: Difference between revisions

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Justin Allen

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 ==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 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 regulated by the concentration of Mg2+ and the previous steps of glycolysis.