9 Questions
How many types of allosteric regulation ?
3 types
What is allosteric regulation?
Allosteric regulation is the regulation of enzyme activity by molecules that bind weakly to a specific receptor on the enzyme that is not the active site, and can either inhibit or stimulate enzyme activity.
How is the end product acts on the pathway ?
acts as an inhibitor
What is the function of allosteric activators?
Allosteric activators stabilize the conformation of the enzyme that has a functional activity.
What are allosteric activators?
Molecules that stabilize the conformation of the enzyme's active form
Where are the allosteric sites often located?
Where subunits are joined
What is the function of allosteric regulation in many cases?
To behave like reversible noncompetitive inhibitors
How many conformational shapes does the whole protein exist in?
Two
What is the nature of most allosterically regulated enzymes?
Constructed of two or more polypeptide chains
Study Notes
Allosteric Regulation of Enzymes
- Allosteric regulation involves molecules binding to a specific receptor site on the enzyme, not the active site, to regulate enzyme activity
- These molecules can either inhibit or stimulate enzyme activity
- Most allosterically regulated enzymes are multimeric, consisting of two or more polypeptide chains
Allosteric Sites and Conformational States
- Allosteric sites are often located where subunits are joined
- The whole protein exists in two conformational shapes:
- The active form
- The inactive form
Allosteric Activators and Inhibitors
- Allosteric activators stabilize the conformation that has a functional active site
- Allosteric inhibitors stabilize the conformation that has an inactive or less active site
Test your knowledge of the control of metabolism with this quiz on allosteric regulation of enzymes, including topics such as allosteric activation, allosteric inhibition, feedback inhibition, and cooperativity regulation. This quiz covers the molecular mechanisms that naturally regulate enzyme activity.
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