Enzymes - Explanation
Enzymes can be defined as the catalysts that are found in the living cells and they are constituted of protein substances, which help in facilitating the complex biochemical as well as metabolic reactions. Since they are catalysts, the enzymes don’t directly participate in biological reactions but they assist with their efficient occurrence. This is why an enzyme can be brought to use usually without getting exhausted.
Some of the examples of the enzymes are Protease, and Proteases, Lipase, Amylase, and Lactase. The enzymes are formed when the specific number (a few thousand) of the amino acids are linked together within the chains using amide or peptide bonds. The enzymes are generally added in beverages, bread, chocolates, washing powders, pre-digested baby foods, and curd for effective and efficient preparation.
The Structure of the Enzymes
Enzymes are made using several amino acids and thus they are structured similarly to the proteins. The enzyme has an active site or the substrate-binding site. This is the site where the chemical reaction takes place and the substrate gets attached. The enzyme is able to break the bigger molecule into simpler molecules or vice versa.
The enzyme also has a site known as the inhibitor site. The inhibitor site tends to be functional when the enzyme is in the inactivated stage. Enzymes also have the model of the lock and key structure. In 1958, scientist Daniel Koshland suggested that the active sites of the enzymes are modifiable and flexible, and thus can be reshaped by interactions with corresponding substrates.
Fit Model of the Enzyme
The common equation which can be used to describe the functioning of the enzyme through enzyme-substrate reaction is Substrate + Enzyme = (Substrate-Enzyme) > (Product-Enzyme or the intermediate) = Product + Enzyme.
The interaction of the enzyme-substrate can be better explained with the lock and key structure mechanism. The lock is represented by the enzyme whereas the key is represented by the substrate. Each substrate belongs specifically to its enzyme, similar to the keys belonging to the specific locks.
Affecting Factors for the Enzyme
The presence of the right temperature is essential for the functioning of the enzyme. If the temperature is above the specified limit then it can completely destroy the enzyme and lead to its disintegration thus rendering it useless.
The correct extent of the basic, acidic, or natural environment is key.
Some specific vitamins and non-protein substances, in humans as well as animals, might serve as “co-factors” for helping enzymes function efficiently by assisting in the binding process. The presence or absence of these “co-factors” has an impact on the working of enzymes.
The presence of an inhibitor can have an adverse impact on the functioning of the enzyme.
The concentration of enzymes is also a major factor that has a big impact on the reaction.
Action and Nature of the Enzymes
As we have discussed, the enzymes are naturally protein and thus they are made of various amino acids.
The enzymes are formed by paracrine glands and exocrine glands and they are transferred to the required place viaducts.
Enzymes are the catalysts that speed up the chemical reaction within the body.
Enzymes lower the required activation energy for the chemical reaction and thus less energy is needed for carrying the reaction forward.
FAQs on Enzymes
1. What are the different classifications of enzymes based on their function?
Based on their function, the enzymes can be classified into six types. These types are as follows: Oxidoreductases, Transferases, Hydrolases, Lyases, Ligases, and Isomerases. The Oxidoreductases catalyze the oxidation-reduction reaction via the facilitation of electron transfers. The electrons that are transferred are usually hydrogen atoms or hydride ions. The Transferases, on the other hand, are the enzymes that facilitate the group transfer processes where the molecule is the donor whereas another molecule acts as the acceptor.
2. How does a lactose molecule represent the lock and key mechanism in enzymes?
The lactose molecule only binds to the lactase enzyme since it has a substrate-binding site that is specific to that substrate and it is called the active site. Once the substrate is bound to an enzyme, the reaction happens where the old bonds are disintegrated and the formation of the new bonds happens thus making the new molecule. The new molecule is essentially the product and it is made possible by the lock and key mechanism of the enzymes.
3. Why is the presence of inhibitor site bad for the enzyme function?
Generally, the inhibitor site is functional when the enzyme tends to be in the inactivated stage. If the inhibitor site gets filled by an inhibitor within the enzyme, then the shape of the active site gets changed and it prevents any of the substrates from getting attached to the active site. This prevents the processing of any further reaction in the enzymes. This is why the presence of an inhibitor site has an adverse effect on the enzyme function.
4. What is the benefit of referring to the Vedantu notes on “Enzymes”?
The Vedantu notes on “Enzymes” provide comprehensive documentation of all the important topics and sub-sections associated with enzymes. The structure and presentation of the content is done in a simple as well as lucid format to help the students grasp the concept thoroughly. These notes contain graphic images, charts, and illustrations wherever necessary for providing the students with the best guide for their chapters.
5. How do I download the Vedantu notes on “Enzymes”?
The Vedantu notes on “Enzymes” can be downloaded from the Vedantu app or the website. The Vedantu app provides easy access to some of the highest quality and best learning resources on the web. For downloading the notes on “Enzymes” you need to visit the specific link and then click on the “Download PDF” option provided on the page. This will download the file on your specific device for your reference.
