Build on your understanding of the two-step process of enzyme catalysis and the Michaelis-Menten Equation as you uncover how allosteric regulation influences enzymatic activity.

Allosteric regulation, broadly speaking, is just any form of regulation where the regulatory molecule (an activator or inhibitor) binds to an enzyme someplace other than the active site.

A number cellular respiration enzymes are controlled by the binding of regulatory molecules at one or more allosteric sites. (An allosteric site is just a regulatory site other than the active site.)

The inhibitor can bind at an allosteric site, and when they're both bound, notice they're not competing for the enzyme, they both can be on the enzyme. This character can bind to the …

Explore the intriguing world of enzyme kinetics and cooperative binding. Delve into the two-step process of enzyme catalysis, the Michaelis Menten equation, and the effects of increasing …

In Allosteric competitive inhibition, the competitor binds somewhere else on the enzyme, changing the shape of the active site temporarily, blocking the substrate from binding because the …

Learn about covalent modifications and how they change enzyme behavior. Learn about post-translational modifications like methylation, acetylation, and glycosylation. Understand …

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So that brings me to my first point, which is that there is no hormonal control in the citric acid cycle, because it's on regardless of whether we're in the fed state or the fast state. Instead the …

Uncover the irreversible reaction from pyruvate to Acetyl-CoA, and how it's a prime target for cellular regulation. Learn about the major roles of Acetyl-CoA and the allosteric regulation of …