Explore enzyme kinetics and how enzymes speed up reactions by lowering activation energy. Learn about the two-step process of enzyme catalysis, understand the concept of Vmax, and learn about …

Graphs like the one shown below (graphing reaction rate as a function of substrate concentration) are often used to display information about enzyme kinetics. They provide a lot of useful information, but …

Kinetics is the study of reaction rates and how they are affected. Many factors, such as concentration, pressure, temperature, and enzyme activity, can impact the rate of a reaction.

Continue your exploration of enzyme kinetics with a focus on Michaelis-Menten kinetics and the steady-state assumption. Explore how enzymes speed up reactions, the role of substrate concentrations, …

This article delves into the specific effects of various enzyme inhibitors on these kinetic graphs and highlights how these visual tools can be used to pinpoint the type of inhibition involved.

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 substrate …

This articles reviews positive and negative cooperativity in enzymes and how this is expressed numerically by the Hill coefficient.

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The cells of your body are capable of making many different enzymes, and at first you might think: great, let’s crank all of those enzymes up and metabolize as fast as possible!

MCAT Course: MCAT > Unit 6 Lesson 4: Enzyme kinetics Enzyme kinetics questions Google Classroom Microsoft Teams