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Enzymes are protein catalyst that increase the rate of reaction without changing itself in the end of the process.
Enzymes are classified according to International Union of Biochemistry and Molecular Biology (IUBMB). Most enzyme-catalyzed reactions are highly efficient by increasing the reactions 103 to 108 faster compared uncatalyzed reactions. Basically, all the chemical reactions have the energy barrier separating the reactants and products as shown in Figure 3. Leonor Michaelis and Maude Menten proposed a enzyme reaction model where the enzyme combines reversibly to substrate to form enzyme-substrate complex and subsequently form product and free enzyme (Figure 4).


Michaelis-Menten equation describes how the reaction velocity is affected by concentration as shown in Figure 5 and Figure 6.
The rate of reaction is directly proportional to enzyme concentration at all concentration of substrates. Sufficient amount concentration of substrates will reach the Vmax same with reaction without inhibitors. Proteases: Protein-digesting enzymes added to detergent to remove protein stains from clothes.
The noncompetitive inhibitors do not compete with substrate for active sites, so the Km is remain the same.


The higher the free activation of energy, the slower the chemical reaction to form products.
Example of Ubiquitin-activating enzyme binds with substrate ubiquitin as shown in Figure 2. Enzymes increase the rate of reactions by providing an alternative reaction pathway with lower free energy of activation.



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