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BIOCHEMISTRY: Enzyme Motions Inside and Out

Access to the article is free, however registration and sign-in are required. How does an enzyme reduce the free-energy barrier for a chemical transformation? The authors have reviewed the progression of hypothetical answers to this question and identified a common feature of the various rationales--namely, the requirement for conformational flexibility within the enzyme and substrates. They also discuss how Masgrau et al. examined the importance of dynamics for catalysis by the enzyme aromatic amine dehydrogenase in the oxidation of tryptamine.

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Resource Type: Journal article/Issue, Review, Diagram
Audience Level: High school upper division 11-12, Undergraduate lower division 13-14, Undergraduate upper division 15-16, Graduate

Author and Copyright

Authors and Editors: Stephen J. Benkovic of Department of Chemistry, Pennsylvania State University, Sharon Hammes-Schiffer of Department of Chemistry, Pennsylvania State University
Publisher: AAAS
Format: text/html
Copyright and other restrictions: Yes
Cost: No


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