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Allosteric Activators

Allosteric Activators. Jared Band Komal Vadodaria Lauren Castle Zeshan Kahn Period 4. Allosteric Regulation. How is enzyme activity regulated within the cell? Specific molecules regulate enzyme activity in the cell How do these specific molecules actually regulate enzyme activity?

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Allosteric Activators

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  1. Allosteric Activators Jared Band Komal Vadodaria Lauren Castle Zeshan Kahn Period 4

  2. Allosteric Regulation • How is enzyme activity regulated within the cell? • Specific molecules regulate enzyme activity in the cell • How do these specific molecules actually regulate enzyme activity? • The regulatory molecules change an enzyme’s shape • Then, the regulatory molecules bind to another site on the molecule • Result? The function of the active site changes (remember – each enzyme has a specific function provided by a specific “key and lock” to fit specific molecules) • Via noncovalent bonds • ALLOSTERIC REGULATION: a protein’s function is affected by a change in the binding of another molecule along another site

  3. Definition • Allosteric Activator: • Specific molecules that adaptthe shape of an enzyme in order to create more stability within the enzyme. • These activators are unique to specific enzymes • Each enzyme has a specific function • Animated Diagram: • http://course1.winona.edu/sberg/ANIMTNS/allostan.htm

  4. Substrate: the material/substance on which an enzyme acts

  5. So What? • So, allosteric activators make an enzyme more stable! • allows enzyme to perform specific function better

  6. Relating to Our Lives… • Imagine that you have a Math test first period in the morning…. • don’t eat breakfast = you do OK • eat breakfast = do even BETTER • food=energy  less distractions How does this relate to enzymes?

  7. EXAMPLE: • ATP hydrolysis: ADDING A WATER MOLECULE • plays a major role in balancing the flow of traffic between anabolic and catabolic pathways • ATP binds to several catabolic enzymes allosterically  lowers their affinity for substrate and as a result inhibits their activity while ADP acts as an activator of the same enzyme. • So if ATP production lags behind its use, ADP accumulates and activates these key enzymes that speed up catabolism, producing more ATP. • If the supply exceeds demand however, catabolism slows down as ATP molecules accumulate and bind to enzymes, inhibiting them. In this way, allosteric enzymes control the rates of key reaction in metabolic pathways. • Difference of Pathways: • catabolic = break-down pathway • anabolic = consumes energy, building complex molecules from simple molecules

  8. ATP Hydrolysis Reaction

  9. Real-Life Applications • Diabetes Research Glycokinase helps stabilize glucose by catalyzing the addition of a phosphate group to a protein of glucose in cells that express this enzyme, like pancreatic β cells and hepatocytes. A class of anti-diabetic agents act as nonessential, mixed-type GK activators (GKAs) that increase the glucose affinity and maximum velocity of GK. GKAs were added to both hepatic glucose metabolism and glucose-induced insulin secretion from isolated rodent pancreatic islets, consistent with the expression and function of GK in both cell types. In several rodent models of type 2 diabetes mellitus, GKAs lowered blood glucose levels, improving the results of glucose tolerance tests, and increased hepatic glucose uptake. These findings may lead to the development of new drug therapies for diabetes.

  10. Video http://www.youtube.com/watch?v=M5bftq-W2aY

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