6.5: Enzyme Regulation

The allosteric inhibitor of an enzyme

• Causes the enzyme to work faster

• Binds to the active site

• Participates in feedback regulation

• Denatures the enzyme

A receptor site that a molecule can bind to that changes the shape of the active site is called a(n):

• Allosteric Site

• Active Site

• Activation site

• Reactant site

How does a noncompetitive inhibitor decrease reaction rates?

• Binds to the active site

• Binds to the allosteric site

• Increases the free energy

• Increases the substrate concentration

Describes the process by which an enzyme's function at the active site may be either activated or inhibited by the binding of a regulatory molecule at a separate site.

• Allosteric Interactions

• Feedback Inhibition

• Competitive Inhibition

• Noncompetitive Inhibition

Key metabolic enzymes are often inhibited by the end product of the pathway they control.

• Competitive inhibition

• Non-competitive inhibition

• Feedback inhibition

• Cofactors

This best describes positive cooperativity of hemoglobin

• As 1 O₂ binds to a heme group, it causes a sudden shift of polarity, attracting more O₂

• As 1 O₂ binds to a heme group, a conformational change occurs, making it more likely for additional O₂ to bind

• As 1 O₂ binds to a heme group, hemoglobin becomes slightly less hydrophilic

• As 1 O₂ binds to a globin group, the binding site of O₂ within the molecule becomes more exposed