What is catalytic efficiency

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A key substrate must be inserted and turned chemical reaction , then the lock enzyme opens production of products. Note that an enzyme might have more than one active site. Another theory on the active site-substrate relationship is the induced fit theory, which is quite opposite of the lock and key theory where the active site is seemingly inflexible.

In the induced fit theory, the active site of the enzyme is very flexible, and only changes its conformation when the substrate binds to it. Enzymes work as a catalyst by lowering the Gibbs free energy of activation of the enzyme-substrate complex. Below are two figures showing a basic enzymatic reaction with and without a catalyst:.

Figure 1: The energies of the stages of a chemical reaction. Uncatalyzed dashed line , substrates need a lot of activation energy to reach a transition state, which then decays into lower-energy products. German biochemist Leonor Michaelis and Canadian biochemist Maud Menten derived an equation describing this system, later known as the "Michaelis-Menten Equation", shown below:.

This equation gives the rate of the reaction at a given substrate concentration, assuming a known V max , which is the maximum rate the reaction can proceed at, and K M , the Michaelis constant. However, in a practical application of the Michaelis-Menten, V 0 is often measured, and V max is observed as a saturation or plateau in a data plot. Because the substrate concentration is known, K M is usually the calculated value of interest.

Submitted 05 Dec Accepted 21 Feb First published 21 Feb Download Citation. Request permissions. Social activity. Search articles by author Shanshan Yu.

Peiyuan Yao. Jinlong Li. Jinhui Feng.