Enolase: Difference between revisions
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<scene name='Cory_Tiedeman_Sandbox_1/Enolase/1'>Enolase</scene> is an enzyme that catalyzes a reaction of glycolysis. Glycolysis converts glucose into two 3-carbon molecules called pyruvate. The energy released during glycolysis is used to make ATP.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=487|}}</ref> Enolase is used to convert 2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) in the 9th reaction of glycolysis: it is a reversible dehydration reaction.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=500|}}</ref>. Enolase is expressed abundantly in most cells and has been proven useful as a model to study mechanisms of enzyme action and structural analysis <ref>{{journal}}</ref>. | <scene name='Cory_Tiedeman_Sandbox_1/Enolase/1'>Enolase</scene> is an enzyme that catalyzes a reaction of glycolysis. Glycolysis converts glucose into two 3-carbon molecules called pyruvate. The energy released during glycolysis is used to make ATP.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=487|}}</ref> Enolase is used to convert 2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) in the 9th reaction of glycolysis: it is a reversible dehydration reaction.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=500|}}</ref>. Enolase is expressed abundantly in most cells and has been proven useful as a model to study mechanisms of enzyme action and structural analysis <ref>{{journal}}</ref>. As with the reaction below, Enolase must have a divalent metal cation present to activate or deactivate the enzyme. The best cofactor would be Mg2+, but many, including Zn2+, Mn2+ and Co2+ can be used. The metal ion works by binding to the enzyme at the active site and producing a conformational change. This makes it possible for the substrate (2-PGA) to bind at the Enolase active site. Once this happens, a second metal ion comes in and binds to the enzyme to activate the Enolase catalytic ability. | ||
==Structure== | ==Structure== | ||
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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. | Enolase is regulated by the concentration of Mg2+ and the previous steps of glycolysis. | ||
==Other interesting information== | |||
Enolase is present in all tissues and organisms with the ability to do glycolysis or fermentation. Recent studies have Enolase concentration samples in order to determine certain conditions and their severity. For instance, high concentrations of Enolase in cerebrospinal fluid (CSF) are more strongly associated with astrocytoma than other enzymes like aldolase, pyruvate kinase, and creatine kinase. High concentrations of Enolase in the CSF are also linked to the fastest rate of tumor growth and increased chances of heart attack or stroke. | |||
Enolase can be competitively inhibited by fluoride for the substrate 2-PGA. In drinking water with added fluorination, oral bacteria Enolase activity is inhibited without harmed humans. This works to prevent cavities. | |||
==3D structures of enolase== | ==3D structures of enolase== | ||