This preview has intentionally blurred sections. Sign up to view the full version.View Full Document
Unformatted text preview: Chapter 7: The Behavior of Proteins: Enzymes, Mechanisms, and Control 1. The Behavior of Allosteric Enzymes a. Allosteric enzymes undergo cooperative effects caused by subtle changes in quaternary structure from the interaction of subunits through noncovalent forces i. Positive cooperativity refers to the fact that the binding of low levels of substrate facilitates the action of the protein at higher levels of substrate, whether the action is catalytic or some other kind of binding ii. In addition to displaying cooperative kinetics, allosteric enzymes have a different response to the presence of inhibitors from that of nonallosteric enzymes b. Feedback inhibition (end-product inhibition) i. The end product of the sequence of reactions inhibits the first reaction in the series ii. Feedback inhibition is an efficient control mechanism because the entire series of reactions can be shut down when an excess of the final product exists, thus preventing...
View Full Document
- Spring '07
- Enzyme, Transition state, transition state analog, transition state analogs