Allosteric effects make enzyme behavior more complicated than what the traditional Michaelis-Menten model shows.
The Michaelis-Menten model thinks of enzymes as having a single way to bind with a substance. But with allosteric regulation, enzymes can change shape when they attach to substrates.
Key Challenges:
Multiple States: Allosteric enzymes can be in both active and inactive forms. This affects how fast reactions happen.
Sigmoidal Kinetics: Instead of showing a straight line like the Michaelis-Menten model, allosteric enzymes show a curve. This curve shows that they work together in groups when binding happens.
Example: Hemoglobin isn’t an enzyme, but it behaves in an allosteric way. Once the first oxygen molecule attaches to it, hemoglobin grabs onto the next oxygen more easily.
This shows how allosteric effects help us understand enzyme behavior much better than the traditional model does.
Allosteric effects make enzyme behavior more complicated than what the traditional Michaelis-Menten model shows.
The Michaelis-Menten model thinks of enzymes as having a single way to bind with a substance. But with allosteric regulation, enzymes can change shape when they attach to substrates.
Key Challenges:
Multiple States: Allosteric enzymes can be in both active and inactive forms. This affects how fast reactions happen.
Sigmoidal Kinetics: Instead of showing a straight line like the Michaelis-Menten model, allosteric enzymes show a curve. This curve shows that they work together in groups when binding happens.
Example: Hemoglobin isn’t an enzyme, but it behaves in an allosteric way. Once the first oxygen molecule attaches to it, hemoglobin grabs onto the next oxygen more easily.
This shows how allosteric effects help us understand enzyme behavior much better than the traditional model does.