Overview
Allosteric regulation is a vital concept in biochemistry that describes how the activity of enzymes can be modulated by the binding of molecules at sites other than the active site. This regulation is crucial for maintaining metabolic balance and allows for fine-tuning of enzyme activity in response...
Key Terms
Example: The allosteric site on hemoglobin allows for oxygen binding.
Example: ATP acts as an activator for some enzymes.
Example: Amylase breaks down starch into sugars.
Example: Hemoglobin exhibits positive cooperativity in oxygen binding.
Example: Glucose is the substrate for hexokinase.
Example: Penicillin inhibits bacterial enzymes.
Related Topics
Enzyme Kinetics
The study of the rates of enzyme-catalyzed reactions and how they change with varying conditions.
intermediateProtein Structure
Understanding the three-dimensional arrangement of proteins and how it relates to their function.
intermediateMetabolic Pathways
The series of chemical reactions occurring within a cell that lead to the conversion of substrates into products.
advancedBiochemical Regulation
The mechanisms that control the activity of enzymes and metabolic pathways.
advancedKey Concepts
Allosteric sitesEffectorsEnzyme activityCooperativity