Kinetic Properties of Enzymes

Enzymes are biological catalysts that function to improve the rate of a chemical reaction without even being consumed or modified in the process. Each sort of reaction and just one, or even a tiny proportion of strongly linked reactant molecules known as substrates are particular to that type of response and those substrates only. In the cell, enzymes are essential because many biological reactions are too slow to maintain life if they were not present.The analysis of enzyme reaction rates as well as the factors that influence them is known as enzyme kinetics. Enzyme structure and function, as well as their clinical relevance and theories of enzyme kinetics, will be discussed in detail in this article.Enzymes are biological catalysts with a globular tertiary structure, which is common in nature. Because of the existence of a catalytic site, in which the reaction takes place, their structure has an impact particular to the response they catalyze and, consequently, to the reactants involved in a chemical reaction. When the enzyme is activated, a small gap within the enzyme with a specific amino acid structure allows the substrate to attach to it and create the enzyme-substrate complex (ES), which would be bound together through weak links to permit separation of the combination once the reaction is complete. The remainder of the enzyme serves as a scaffold, putting these essential amino acids together in a cohesive manner.

Enzymes

Biological enzymes are proteins that aid in the speeding up of metabolic activities, or the chemical reactions that take place in the human body. Some substances are formed, while others are decomposed or destroyed by the bacteria. Enzymes are found in every living thing. Enzymes are produced by our bodies on a natural basis.In all living organisms, biological processes are chemical reactions, and the majority of these reactions are regulated by enzymes. Many of these processes would not occur at all if enzymes were not present to speed them along. Enzymes are responsible for catalyzing every aspect of cell metabolism. 

Kinetic Properties Of Enzymes

1.Catalytic Properties

Enzymes have catalytic properties, which means that they are biological catalysts. The small number of enzymes is responsible for catalyzing the large number of substances. This means that enzymes have such a high option to transform large amounts of substrate into useful products. Enzymes catalyze reactions by increasing the rate of the reaction while remaining unchanged by the reaction that they catalyze.

2.Specificity of enzymes

In nature, enzymes are extremely specific, meaning that a specific enzyme can only catalyze a certain process. For instance, the enzyme starch is only capable of catalyzing the hydrolysis of sucrose.

Properties Of Enzymes

1.Enzymes Usually Work Quickly:–

An enzyme’s function and velocity are expressed as changeover numbers. Per minute, an enzyme converts one substrate molecule into a product. This quantity varies between 100 and several millions for most enzymes. Enzyme that breaks down hydrogen peroxide into water and oxygen. If you want to see how much energy an enzyme uses, put a slice of liver in some hydrogen peroxide and watch it bubble away as the oxygen is released.

2.Enzymes Work Both Ways:

This is because the proportional proportions of the interacting substrates and products generate a reversible metabolic reaction. The reaction continues until the substrates and products are in equilibrium. In order to maintain equilibrium, an enzyme that catalyzes the creation of items from substrates will also lead the results to be divided into element substrates.

3.Catalyzed Reactions Do Not Destroy Or Alter Enzymes:

Unlike enzymes, the reactions they catalyze do not destroy them. However, enzymes are unstable and can be inactivated by heat, acids, and alkaline substances, unlike inorganic catalysts which are stable and can be reused indefinitely.

4.Enzymes Are pH Sensitive:

Enzymes work best at specified pH ranges, and any changes can hinder their action. Most internal enzymes prefer a pH of 7. Some digestive enzymes prefer an alkaline or acidic environment. This explains why pepsin, a protein breaking enzyme that only works in an acidic environment (pH 2.0), is located in the stomach.

5.Enzymes Act In Specific Ways:

Inorganic catalysts cannot catalyze enzyme processes. It varies between enzymes in terms of catalytic specificity. In contrast, some digestive enzymes act on a variety of substrates that are linked to intracellular enzymes. However, an enzyme like pancreatic lipase is less selective and can digest a range of fats, unlike catalase which only splits H2O2

6.Heat Inactivates Enzymes:–

Enzymes are proteins and dislike hot temperatures. For the same reason that very few cells can endure temperatures beyond 45°C, enzymes are denatured by heat. Heat-resistant enzymes or the ability to regulate body temperature are required for organisms that live in environments where temperatures reach 45 degrees Celsius. Hot spring blue-green algae is a wonderful example of an organism with heat-resistant enzymes.

kinetic parameters of enzymes

The kinetics parameters rmax and Km are two of the most important in the Michaelis–Menten equation. When practically all enzymes were coupled with the substrates to create an intermediate complex, the highest reaction rate was represented by the value rmax. The Km value is a measure of the affinity between a substrate and its enzyme counterpart.A low Km value indicates a high interaction between both the enzyme and the substrate, making dissociation more difficult. A high Km value shows the polar opposite of the situation. Therefore, Km is an intrinsic parameter whose value is influenced by the properties of the enzyme-catalyzed reaction mechanism as well as the process conditions; as such, Km is a parameter that represents the features of the enzyme-catalyzed reaction system. The substrate concentration needed for an enzyme to achieve 50 percent of its maximal reaction rate, rmax, is denoted by the symbol Km.

Conclusion

Chemical kinetics, often known as enzyme kinetics, is the study of the speeds at which chemical reactions are catalyzed by enzymes. It is possible to learn more about an enzyme’s kinetics by looking at its catalytic mechanism, its involvement in metabolism, how its activity is controlled in the cell, and how medications and poisons can interfere with its activity by studying its kinetics.It is enzymes that alter various compounds — the enzymes’ substrates — in order to perform their functions. The enzymatic process is a sequence of stages where these targets are capable of binding to an enzyme’s active site and are converted into products by the action of the enzyme. In some cases, an enzyme can interact with more than one substrate and/or produce more than one product, such as when a protease degrades 1 protein source into twin polypeptide products.