Birrer Sandbox 2: Difference between revisions
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The Mechanism for alcohol dehydrogenase follows an Ordered bisubstrate mechanism. The mechanism, then, is pretty straight forward: 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 Ordered bisubstrate mechanism.<ref>Voet, et. al. ''Fundamentals of Biochemistry: 3rd Edition''. Hoboken: Wiley & Sons, Inc, 2008.</ref> The mechanism, then, is pretty straight forward: 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. | ||