What term describes the phenomenon in allosteric enzymes where the velocity increases over a narrower range of substrate concentration, compared to Michaelis-Menten enzymes?
Understand the Problem
The question is asking us to define the behavior of allosteric enzymes that causes them to increase in velocity across a narrower range of concentrations of a substrate, compared to Michaelis-Menten enzymes. This phenomenon is related to the cooperativity observed in the enzyme.
Answer
Sigmoidal kinetics describes the steeper velocity increase in allosteric enzymes over a narrow substrate concentration range, compared to Michaelis-Menten enzymes.
The phenomenon where allosteric enzymes exhibit a steeper increase in velocity over a narrower range of substrate concentration compared to Michaelis-Menten enzymes is described by sigmoidal kinetics.
Answer for screen readers
The phenomenon where allosteric enzymes exhibit a steeper increase in velocity over a narrower range of substrate concentration compared to Michaelis-Menten enzymes is described by sigmoidal kinetics.
More Information
Allosteric enzymes do not follow traditional Michaelis-Menten kinetics. Instead, they display sigmoidal kinetics due to cooperativity between multiple binding sites.
Tips
A common mistake is to assume all enzymes follow Michaelis-Menten kinetics. Allosteric enzymes are an important exception.
Sources
- Why does allosteric binding produce a sigmoidal curve? - chemistry.stackexchange.com
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