AndrewAlexanderSandbox1: Difference between revisions
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As indicated earlier, phosphoenolpyruvate can enhance the activity of the reaction by adding into the enzyme because it is the rate limiting step. The enzyme follows hyperbolic kinetics. Experiments found that no incorporation was found in the reaction, indicating a random, rapid dissociation of the products. This, then, assumes that the products inhibit the enzyme’s reaction by simply reversing the reaction. Both pyruvate and ATP have been shown to be non-competitive inhibitors of pyruvate kinase. <ref>{{article |author=Dann, Leighton G.; Britton, Hubert G.|title=Kinetics and Mechanism of Action of Muscle Pyruvate Kinase|volume=169|pages=39-54|}}</ref>. | As indicated earlier, phosphoenolpyruvate can enhance the activity of the reaction by adding into the enzyme because it is the rate limiting step. The enzyme follows hyperbolic kinetics. Experiments found that no incorporation was found in the reaction, indicating a random, rapid dissociation of the products. This, then, assumes that the products inhibit the enzyme’s reaction by simply reversing the reaction. Both pyruvate and ATP have been shown to be non-competitive inhibitors of pyruvate kinase. <ref>{{article |author=Dann, Leighton G.; Britton, Hubert G.|title=Kinetics and Mechanism of Action of Muscle Pyruvate Kinase|volume=169|pages=39-54|}}</ref>. | ||
With or without K+, oxalate is a noncompetitive inhibitor of ADP-Mg2+. It will form a nonproductive ternary complex which diminishes Vmax without altering the binding of ADP-Mg2+. <ref>{{article |author=Oria-Hernandez, Jesus.; Cabrera, Nallely.|title=Pyruvate Kinase Revisited: The Activating effect of K+|volume=280|pages=37924-37929|}}</ref>.: | |||
==Pyruvate Kinase Deficiency== | ==Pyruvate Kinase Deficiency== | ||
