Birrer Sandbox 2: Difference between revisions

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-The Mechanism for alcohol dehydrogenase follows an Ordered bisubstrate mechanism.<ref>Voet, et. al. ''Fundamentals of Biochemistry: 3rd Edition''. Hoboken: Wiley & Sons, Inc, 2008.</ref> In the mechanism, the NAD+ and alcohol bind to the enzyme, so that the enzyme is now attached to the two subtrates. While attached, the hydrogen is formally transferred from the alcohol to NAD, resulting in the products NADH and a ketone or aldehyde. The two products are then released, and the enzyme has catalyzed the reaction.
+The Mechanism for alcohol dehydrogenase follows an random bisubstrate mechanism.<ref>Voet, et. al. ''Fundamentals of Biochemistry: 3rd Edition''. Hoboken: Wiley & Sons, Inc, 2008.</ref> In the mechanism, the NAD+ and alcohol bind to the enzyme, so that the enzyme is now attached to the two subtrates. While attached, the hydrogen is formally transferred from the alcohol to NAD, resulting in the products NADH and a ketone or aldehyde. The two products are then released, and the enzyme has catalyzed the reaction.
 ==Kinetics==
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+The alcohol dehydrogenase catalyzed aldehyde-NADH reaction show kinetics consistent with a  random-order mechanism, and the rate-limiting step is the dissociation of the product enzyme-NAD+ complex.