What Is the Mechanism of Enzyme Action with Steps and Models
Enzymes are proteinaceous molecules that help in catalysing the biochemical reactions in our body. Due to this property, they are also known as biocatalysts. As they are proteinaceous in nature, they also possess secondary and tertiary structures. When the enzymes are present in their tertiary structure, their protein chains get folded upon themselves, and due to this, many crevices are formed that are termed as active. These active sites are mainly responsible for the mechanism of enzyme action and also the mechanism of enzyme catalysis.
The human body is made up of many cells, tissues, and organs, and all of them work accordingly. The body releases certain types of chemicals known as enzymes. These enzymes control biological processes like respiration, reproduction, excretion, digestion, and excretion, and try to act as per the body clock. They are important not only to human survival, but also to look after the same biological activities in animals. Mostly, they are made up of proteins which act as a catalyst in a biological process.
The initial stage of biological activity is triggered by the enzyme which interacts with the molecule in the human body, called a “substrate”. They are further processed to form “products”. Mostly, the enzymes have proteins, except those related to the RNA. We can find enzymes in most of the organs and cells of human and animal bodies. Intracellular enzymes are the enzymes that help in metabolic activity. Enzymes are generally made up of chains of amino acids and are three dimensional in structure. Enzymes are temperature and pH sensitive, they lose their function when the pH or temperature increases or decreases. They vary in size based on the amino acid molecules.
Enzymes are divided into oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases; this division is based on the functional use of the enzymes. Oxidoreductases are enzymes that transfer electrons from one place to another place and control oxidation activity. Transferases are the enzymes that help in transporting from the donors to the receptors in the human body. Hydrolases help in catalysing hydrolysis activity in the human body. Lyases are the enzymes that add ammonia, water, and carbon dioxide to the bonds.
Enzyme Type and Functions
Enzyme Action
To understand the enzyme mechanism and enzyme action, two hypotheses were proposed. They were:
1. Lock and Key Hypothesis:
This hypothesis was proposed by Emil Fischer in 1894. This hypothesis helps us understand the mechanism of action of enzymes. According to this hypothesis, the enzyme and substrate molecules exhibit various geometrical shapes and these shapes are very specific. Just as the lock and key model, this hypothesis states that the active sites of enzymes act as a lock that has specific molecules, such as -COOH and -SH. These enzyme molecules can only be opened with the help of specific substrate complexes. This hypothesis explains the specificity of enzymes and also the mode of action of enzymes. The substrate comes in contact with the active site of the enzyme complex and then forms an enzyme-substrate complex. When this complex is formed, it undergoes chemical changes, and then, eventually, a product is formed. When this product is formed, it no longer fits into the active site and escapes out into the surrounding area. In this way, the active site is available again for fresh substrates. By this hypothesis, it can be concluded that a very small amount of enzyme can act upon large substrate molecules. It also explains how the enzymes are not used in the reaction and can be used again and again. Moreover, it helps us to understand the mechanism of competitive inhibition.
2. Induced Fit Hypothesis:
Koshland proposed this hypothesis in the year 1960. This hypothesis is actually quite different from the previous hypothesis. It states that the active site of the enzyme is flexible in shape and can change its shape according to the nature of the substrate, which means that it can form its active site complementary to the substrate. It is easy to understand how a hand induces a change in the glove, that is, the same way an active site induces a change in the chemical substrate. The substrate gets into the active site of the enzyme. According to this, the structure of the active site of an enzyme is flexible. There are two types of groups that are present in the active site of the enzyme. One is a buttressing group and the other is a catalytic group. The buttressing group helps in supporting the substrate, whereas the catalytic group helps to explain the mechanism of enzyme catalyses. When the buttressing group comes in contact with the substrate, changes take place in the active site and these changes help to bring the catalytic group opposite to the substrate bonds that are needed to be broken. The above two models help us deeply understand and describe the mechanism of enzyme action.
Mechanism of Enzyme Catalysis
Enzymes are responsible for bringing out the high rate of chemical conversions. The substrates are converted into products. The substrates get bound to the active site of the enzyme, and then, there are changes in the enzyme complex, which bring about changes in the enzyme-substrate complex, and thus, a product is formed from the substrate. This enzyme-substrate complex is formed for a very short time and is thus known as a transient phenomenon. The transient state structure is formed when the substrate gets bound to the active site of the enzyme. Then, some making/breaking of bonds takes place and a final product is formed. Activation energy is the energy that is required to start the reaction. Enzymes work by lowering these high activation energies of the reactions.
Nature of Enzyme Action
There is a presence of an active site on each enzyme molecule. Substrate comes in contact with the enzyme and then an enzyme-substrate complex is formed. After a while, the enzyme-substrate complex changes to enzyme-product complex, and then the product gets separated from it. This way, the enzyme is not used up in the reaction. The catalytic cycle helps to explain the mechanism of enzyme action through the following points:
The substrate gets bound to the active site.
This induces an alteration in the shape of the enzyme.
The enzyme-product complex is formed by making and breaking bonds.
Enzyme releases away from the product and it is available again for a fresh batch of substrates.
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Factors Affecting Mechanism of Enzyme Catalysis
Three factors are responsible for affecting the mechanism of enzyme catalysis:
Temperature: Enzyme catalysis works in a narrow range of temperature. Optimum temperature is the temperature at which the enzymes show the highest catalytic activity. Anything above and below the optimum temperature declines the enzyme activity. Low temperature makes the enzymes inactive, whereas high temperature denatures the structure of enzymes.
Hydrogen Ion Concentration: As there is an optimum temperature required for the enzyme to function, there is also an optimum pH concentration. Any fall or rise in pH reduces the activity of enzymes. Some enzymes show good catalytic activity in acidic medium, whereas some show good activity in alkaline medium. Every enzyme has an optimum pH, where their activity is maximum.
Substrate Concentration: Substrates act on enzymes and are then changed to products. An increase in the concentration of substrate results in increasing the velocity of enzymes.
Mechanism of Enzyme Action in Biochemistry
There are two types of changes observed in chemical compounds, that are, physical change and chemical change. Physical changes take place by only changing the shape of the compound. No bonds are broken in physical changes. Whereas, in chemical changes, new bonds are formed and broken during the transformation process. When the ice melts into water, it is termed a physical change as there is a change of state. Hydrolysis of starch into glucose is a type of chemical change. The rate of both these physical and chemical processes is the amount of product formed per unit of time. When a direction is specified to rate, it is called velocity. Temperature influences the rate of chemical and physical processes. Various types of enzymes are present and each has a unique catalytic activity or a unique chemical or metabolic reaction. A metabolic pathway is a pathway when one enzyme catalyses the reaction at different steps. When there are one or two additional reactions in the metabolic pathway, it gives rise to a variety of end products. So, this helps us to understand the mechanism of enzyme action in biochemistry.
Conclusion
From the above discussion, we can conclude that enzymes are proteinaceous in nature and are involved in catalysing various biological and biochemical processes. Different models are proposed to understand the mechanism of enzyme action, such as the Lock and Key hypothesis and Induced Fit model. A basic understanding is that enzymes have an active site on them and the substrates get bound to it, and then change into the product. In this way, the enzyme can be used again and again as it is not used in the reaction. Temperature, pH, and substrate concentration are the factors that can affect the rate of enzyme action.
FAQs on Mechanism of Enzyme Action in Biology
1. What is the mechanism of enzyme action?
The mechanism of enzyme action is the process by which an enzyme binds a substrate and converts it into a product by lowering the activation energy of a reaction. This occurs through the formation of an enzyme–substrate complex at a specific region called the active site.
- The substrate binds to the active site.
- An enzyme–substrate complex is formed.
- The enzyme stabilizes the transition state and lowers activation energy.
- The product is released, and the enzyme remains unchanged.
2. How do enzymes lower activation energy?
Enzymes lower activation energy by stabilizing the transition state and providing an alternative reaction pathway. They achieve this through several mechanisms:
- Bringing substrates closer together in the correct orientation.
- Straining substrate bonds to make them easier to break.
- Providing a favorable microenvironment (e.g., optimal pH).
- Forming temporary covalent bonds with substrates.
3. What is the enzyme–substrate complex?
The enzyme–substrate complex is a temporary intermediate formed when a substrate binds to the active site of an enzyme. This complex is essential for catalysis and represents the stage where the chemical reaction is facilitated.
- It forms through specific interactions between enzyme and substrate.
- It allows proper alignment of reactants.
- It breaks down to release product and free enzyme.
4. What are the steps involved in enzyme action?
The steps involved in enzyme action follow a specific catalytic cycle that converts substrate into product.
- Step 1: Substrate binds to the active site.
- Step 2: Formation of the enzyme–substrate complex.
- Step 3: Conversion of substrate into product (transition state stabilization).
- Step 4: Release of product and regeneration of free enzyme.
5. What is the lock and key model of enzyme action?
The lock and key model states that the active site of an enzyme is rigid and specifically shaped to fit a particular substrate. According to this model:
- The enzyme (lock) has a fixed active site.
- The substrate (key) fits exactly into the active site.
- No major structural change occurs in the enzyme during binding.
6. What is the induced fit model of enzyme action?
The induced fit model explains that the active site of an enzyme changes shape slightly to accommodate the substrate during binding. In this model:
- The substrate approaches the active site.
- The enzyme undergoes a conformational change.
- A tighter fit enhances catalysis and stabilizes the transition state.
7. What is the role of the active site in enzyme action?
The active site is the specific region of an enzyme where substrate binding and catalysis occur. It plays a crucial role in enzyme action by:
- Recognizing and binding the correct substrate.
- Providing a unique microenvironment for the reaction.
- Stabilizing the transition state.
- Facilitating conversion into product.
8. Why are enzymes highly specific?
Enzymes are highly specific because their active sites have a unique three-dimensional structure that matches only particular substrates. This specificity arises from:
- The precise arrangement of amino acids in the active site.
- Complementary shape and charge between enzyme and substrate.
- Selective binding interactions such as hydrogen bonds and ionic bonds.
9. Can you give an example of enzyme action in the human body?
An example of enzyme action in the human body is the breakdown of starch by amylase in saliva. In this process:
- Amylase binds to starch at its active site.
- An enzyme–substrate complex forms.
- Starch is hydrolyzed into maltose and smaller sugars.
- The products are released, and amylase is reused.
10. What factors affect the mechanism of enzyme action?
The mechanism of enzyme action is affected by environmental and chemical factors that influence enzyme structure and activity. Key factors include:
- Temperature – affects kinetic energy and enzyme stability.
- pH – influences ionization of amino acids at the active site.
- Substrate concentration – determines reaction rate until saturation.
- Inhibitors – molecules that reduce enzyme activity.
