Join thousands of students who trust us to help them ace their exams!Watch the first video
Multiple Choice
How can inhibitors prevent an enzyme from functioning normally?
A
Binding to the free enzyme.
B
Binding to the ES-complex.
C
Blocking the active site.
D
Altering the active site.
E
Destroying the enzyme.
F
All options are true.
Verified step by step guidance
1
Understand the role of enzymes: Enzymes are biological catalysts that speed up chemical reactions in cells. They have specific active sites where substrates bind to form an enzyme-substrate (ES) complex.
Explore how inhibitors affect enzymes: Inhibitors are molecules that decrease enzyme activity. They can bind to the enzyme or the ES complex, preventing the enzyme from functioning normally.
Binding to the free enzyme: Some inhibitors bind directly to the enzyme before the substrate can bind, preventing the formation of the ES complex. This is known as competitive inhibition.
Binding to the ES-complex: Inhibitors can also bind to the ES complex, preventing the reaction from proceeding. This is known as uncompetitive inhibition.
Blocking or altering the active site: Inhibitors can block the active site or alter its shape, preventing substrate binding or catalysis. This can occur through non-competitive inhibition or allosteric regulation, where the inhibitor binds to a site other than the active site, causing a conformational change.